PortEco : Expression : Samples and Conditions Tool for expression of mutS
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Samples and Conditions Tool for expression of mutS / DNA mismatch repair protein MutS  Open/close help

Click and drag a selection dot on the X-axis to change the current selection area (blue). The histogram shows expression values for the queried gene across all experimemts in the database.

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Big-picture idea behind the experiment(s) that generated these data. Provided by the researcher or obtained from reading a paper.

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Title: Comparative Gene Expression Profiles Following UV Exposure in Wild-Type and SOS-Deficient Escherichia coli.
Abstract: The SOS response in UV-irradiated Escherichia coli includes the upregulation of several dozen genes that are negatively regulated by the LexA repressor. Using DNA microarrays containing amplified DNA fragments from 95.5% of all open reading frames identified on the E. coli chromosome, we have examined the changes in gene expression following UV exposure in both wild-type cells and lexA1 mutants, which are unable to induce genes under LexA control. We report here the time courses of expression of the genes surrounding the 26 documented lexA-regulated regions on the E. coli chromosome. We observed 17 additional sites that responded in a lexA-dependent manner and a large number of genes that were upregulated in a lexA-independent manner although upregulation in this manner was generally not more than twofold. In addition, several transcripts were either downregulated or degraded following UV irradiation. These newly identified UV-responsive genes are discussed with respect to their possible roles in cellular recovery following exposure to UV irradiation.
Title: Comparative Gene Expression Profiles Following UV Exposure in Wild-Type and SOS-Deficient Escherichia coli.
Abstract: The SOS response in UV-irradiated Escherichia coli includes the upregulation of several dozen genes that are negatively regulated by the LexA repressor. Using DNA microarrays containing amplified DNA fragments from 95.5% of all open reading frames identified on the E. coli chromosome, we have examined the changes in gene expression following UV exposure in both wild-type cells and lexA1 mutants, which are unable to induce genes under LexA control. We report here the time courses of expression of the genes surrounding the 26 documented lexA-regulated regions on the E. coli chromosome. We observed 17 additional sites that responded in a lexA-dependent manner and a large number of genes that were upregulated in a lexA-independent manner although upregulation in this manner was generally not more than twofold. In addition, several transcripts were either downregulated or degraded following UV irradiation. These newly identified UV-responsive genes are discussed with respect to their possible roles in cellular recovery following exposure to UV irradiation.
Title: Comparative Gene Expression Profiles Following UV Exposure in Wild-Type and SOS-Deficient Escherichia coli.
Abstract: The SOS response in UV-irradiated Escherichia coli includes the upregulation of several dozen genes that are negatively regulated by the LexA repressor. Using DNA microarrays containing amplified DNA fragments from 95.5% of all open reading frames identified on the E. coli chromosome, we have examined the changes in gene expression following UV exposure in both wild-type cells and lexA1 mutants, which are unable to induce genes under LexA control. We report here the time courses of expression of the genes surrounding the 26 documented lexA-regulated regions on the E. coli chromosome. We observed 17 additional sites that responded in a lexA-dependent manner and a large number of genes that were upregulated in a lexA-independent manner although upregulation in this manner was generally not more than twofold. In addition, several transcripts were either downregulated or degraded following UV irradiation. These newly identified UV-responsive genes are discussed with respect to their possible roles in cellular recovery following exposure to UV irradiation.
Title: Comparative Gene Expression Profiles Following UV Exposure in Wild-Type and SOS-Deficient Escherichia coli.
Abstract: The SOS response in UV-irradiated Escherichia coli includes the upregulation of several dozen genes that are negatively regulated by the LexA repressor. Using DNA microarrays containing amplified DNA fragments from 95.5% of all open reading frames identified on the E. coli chromosome, we have examined the changes in gene expression following UV exposure in both wild-type cells and lexA1 mutants, which are unable to induce genes under LexA control. We report here the time courses of expression of the genes surrounding the 26 documented lexA-regulated regions on the E. coli chromosome. We observed 17 additional sites that responded in a lexA-dependent manner and a large number of genes that were upregulated in a lexA-independent manner although upregulation in this manner was generally not more than twofold. In addition, several transcripts were either downregulated or degraded following UV irradiation. These newly identified UV-responsive genes are discussed with respect to their possible roles in cellular recovery following exposure to UV irradiation.
Title: Comparative Gene Expression Profiles Following UV Exposure in Wild-Type and SOS-Deficient Escherichia coli.
Abstract: The SOS response in UV-irradiated Escherichia coli includes the upregulation of several dozen genes that are negatively regulated by the LexA repressor. Using DNA microarrays containing amplified DNA fragments from 95.5% of all open reading frames identified on the E. coli chromosome, we have examined the changes in gene expression following UV exposure in both wild-type cells and lexA1 mutants, which are unable to induce genes under LexA control. We report here the time courses of expression of the genes surrounding the 26 documented lexA-regulated regions on the E. coli chromosome. We observed 17 additional sites that responded in a lexA-dependent manner and a large number of genes that were upregulated in a lexA-independent manner although upregulation in this manner was generally not more than twofold. In addition, several transcripts were either downregulated or degraded following UV irradiation. These newly identified UV-responsive genes are discussed with respect to their possible roles in cellular recovery following exposure to UV irradiation.
Title: Comparative Gene Expression Profiles Following UV Exposure in Wild-Type and SOS-Deficient Escherichia coli.
Abstract: The SOS response in UV-irradiated Escherichia coli includes the upregulation of several dozen genes that are negatively regulated by the LexA repressor. Using DNA microarrays containing amplified DNA fragments from 95.5% of all open reading frames identified on the E. coli chromosome, we have examined the changes in gene expression following UV exposure in both wild-type cells and lexA1 mutants, which are unable to induce genes under LexA control. We report here the time courses of expression of the genes surrounding the 26 documented lexA-regulated regions on the E. coli chromosome. We observed 17 additional sites that responded in a lexA-dependent manner and a large number of genes that were upregulated in a lexA-independent manner although upregulation in this manner was generally not more than twofold. In addition, several transcripts were either downregulated or degraded following UV irradiation. These newly identified UV-responsive genes are discussed with respect to their possible roles in cellular recovery following exposure to UV irradiation.
Title: Comparative Gene Expression Profiles Following UV Exposure in Wild-Type and SOS-Deficient Escherichia coli.
Abstract: The SOS response in UV-irradiated Escherichia coli includes the upregulation of several dozen genes that are negatively regulated by the LexA repressor. Using DNA microarrays containing amplified DNA fragments from 95.5% of all open reading frames identified on the E. coli chromosome, we have examined the changes in gene expression following UV exposure in both wild-type cells and lexA1 mutants, which are unable to induce genes under LexA control. We report here the time courses of expression of the genes surrounding the 26 documented lexA-regulated regions on the E. coli chromosome. We observed 17 additional sites that responded in a lexA-dependent manner and a large number of genes that were upregulated in a lexA-independent manner although upregulation in this manner was generally not more than twofold. In addition, several transcripts were either downregulated or degraded following UV irradiation. These newly identified UV-responsive genes are discussed with respect to their possible roles in cellular recovery following exposure to UV irradiation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: Comparative Gene Expression Profiles Following UV Exposure in Wild-Type and SOS-Deficient Escherichia coli.
Abstract: The SOS response in UV-irradiated Escherichia coli includes the upregulation of several dozen genes that are negatively regulated by the LexA repressor. Using DNA microarrays containing amplified DNA fragments from 95.5% of all open reading frames identified on the E. coli chromosome, we have examined the changes in gene expression following UV exposure in both wild-type cells and lexA1 mutants, which are unable to induce genes under LexA control. We report here the time courses of expression of the genes surrounding the 26 documented lexA-regulated regions on the E. coli chromosome. We observed 17 additional sites that responded in a lexA-dependent manner and a large number of genes that were upregulated in a lexA-independent manner although upregulation in this manner was generally not more than twofold. In addition, several transcripts were either downregulated or degraded following UV irradiation. These newly identified UV-responsive genes are discussed with respect to their possible roles in cellular recovery following exposure to UV irradiation.
Title: Comparative Gene Expression Profiles Following UV Exposure in Wild-Type and SOS-Deficient Escherichia coli.
Abstract: The SOS response in UV-irradiated Escherichia coli includes the upregulation of several dozen genes that are negatively regulated by the LexA repressor. Using DNA microarrays containing amplified DNA fragments from 95.5% of all open reading frames identified on the E. coli chromosome, we have examined the changes in gene expression following UV exposure in both wild-type cells and lexA1 mutants, which are unable to induce genes under LexA control. We report here the time courses of expression of the genes surrounding the 26 documented lexA-regulated regions on the E. coli chromosome. We observed 17 additional sites that responded in a lexA-dependent manner and a large number of genes that were upregulated in a lexA-independent manner although upregulation in this manner was generally not more than twofold. In addition, several transcripts were either downregulated or degraded following UV irradiation. These newly identified UV-responsive genes are discussed with respect to their possible roles in cellular recovery following exposure to UV irradiation.
Title: Comparative Gene Expression Profiles Following UV Exposure in Wild-Type and SOS-Deficient Escherichia coli.
Abstract: The SOS response in UV-irradiated Escherichia coli includes the upregulation of several dozen genes that are negatively regulated by the LexA repressor. Using DNA microarrays containing amplified DNA fragments from 95.5% of all open reading frames identified on the E. coli chromosome, we have examined the changes in gene expression following UV exposure in both wild-type cells and lexA1 mutants, which are unable to induce genes under LexA control. We report here the time courses of expression of the genes surrounding the 26 documented lexA-regulated regions on the E. coli chromosome. We observed 17 additional sites that responded in a lexA-dependent manner and a large number of genes that were upregulated in a lexA-independent manner although upregulation in this manner was generally not more than twofold. In addition, several transcripts were either downregulated or degraded following UV irradiation. These newly identified UV-responsive genes are discussed with respect to their possible roles in cellular recovery following exposure to UV irradiation.
Title: Comparative Gene Expression Profiles Following UV Exposure in Wild-Type and SOS-Deficient Escherichia coli.
Abstract: The SOS response in UV-irradiated Escherichia coli includes the upregulation of several dozen genes that are negatively regulated by the LexA repressor. Using DNA microarrays containing amplified DNA fragments from 95.5% of all open reading frames identified on the E. coli chromosome, we have examined the changes in gene expression following UV exposure in both wild-type cells and lexA1 mutants, which are unable to induce genes under LexA control. We report here the time courses of expression of the genes surrounding the 26 documented lexA-regulated regions on the E. coli chromosome. We observed 17 additional sites that responded in a lexA-dependent manner and a large number of genes that were upregulated in a lexA-independent manner although upregulation in this manner was generally not more than twofold. In addition, several transcripts were either downregulated or degraded following UV irradiation. These newly identified UV-responsive genes are discussed with respect to their possible roles in cellular recovery following exposure to UV irradiation.
Title: Comparative Gene Expression Profiles Following UV Exposure in Wild-Type and SOS-Deficient Escherichia coli.
Abstract: The SOS response in UV-irradiated Escherichia coli includes the upregulation of several dozen genes that are negatively regulated by the LexA repressor. Using DNA microarrays containing amplified DNA fragments from 95.5% of all open reading frames identified on the E. coli chromosome, we have examined the changes in gene expression following UV exposure in both wild-type cells and lexA1 mutants, which are unable to induce genes under LexA control. We report here the time courses of expression of the genes surrounding the 26 documented lexA-regulated regions on the E. coli chromosome. We observed 17 additional sites that responded in a lexA-dependent manner and a large number of genes that were upregulated in a lexA-independent manner although upregulation in this manner was generally not more than twofold. In addition, several transcripts were either downregulated or degraded following UV irradiation. These newly identified UV-responsive genes are discussed with respect to their possible roles in cellular recovery following exposure to UV irradiation.
Title: Comparative Gene Expression Profiles Following UV Exposure in Wild-Type and SOS-Deficient Escherichia coli.
Abstract: The SOS response in UV-irradiated Escherichia coli includes the upregulation of several dozen genes that are negatively regulated by the LexA repressor. Using DNA microarrays containing amplified DNA fragments from 95.5% of all open reading frames identified on the E. coli chromosome, we have examined the changes in gene expression following UV exposure in both wild-type cells and lexA1 mutants, which are unable to induce genes under LexA control. We report here the time courses of expression of the genes surrounding the 26 documented lexA-regulated regions on the E. coli chromosome. We observed 17 additional sites that responded in a lexA-dependent manner and a large number of genes that were upregulated in a lexA-independent manner although upregulation in this manner was generally not more than twofold. In addition, several transcripts were either downregulated or degraded following UV irradiation. These newly identified UV-responsive genes are discussed with respect to their possible roles in cellular recovery following exposure to UV irradiation.
Title: Comparative Gene Expression Profiles Following UV Exposure in Wild-Type and SOS-Deficient Escherichia coli.
Abstract: The SOS response in UV-irradiated Escherichia coli includes the upregulation of several dozen genes that are negatively regulated by the LexA repressor. Using DNA microarrays containing amplified DNA fragments from 95.5% of all open reading frames identified on the E. coli chromosome, we have examined the changes in gene expression following UV exposure in both wild-type cells and lexA1 mutants, which are unable to induce genes under LexA control. We report here the time courses of expression of the genes surrounding the 26 documented lexA-regulated regions on the E. coli chromosome. We observed 17 additional sites that responded in a lexA-dependent manner and a large number of genes that were upregulated in a lexA-independent manner although upregulation in this manner was generally not more than twofold. In addition, several transcripts were either downregulated or degraded following UV irradiation. These newly identified UV-responsive genes are discussed with respect to their possible roles in cellular recovery following exposure to UV irradiation.
Title: Comparative Gene Expression Profiles Following UV Exposure in Wild-Type and SOS-Deficient Escherichia coli.
Abstract: The SOS response in UV-irradiated Escherichia coli includes the upregulation of several dozen genes that are negatively regulated by the LexA repressor. Using DNA microarrays containing amplified DNA fragments from 95.5% of all open reading frames identified on the E. coli chromosome, we have examined the changes in gene expression following UV exposure in both wild-type cells and lexA1 mutants, which are unable to induce genes under LexA control. We report here the time courses of expression of the genes surrounding the 26 documented lexA-regulated regions on the E. coli chromosome. We observed 17 additional sites that responded in a lexA-dependent manner and a large number of genes that were upregulated in a lexA-independent manner although upregulation in this manner was generally not more than twofold. In addition, several transcripts were either downregulated or degraded following UV irradiation. These newly identified UV-responsive genes are discussed with respect to their possible roles in cellular recovery following exposure to UV irradiation.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays.
Abstract: Much of the information available about factors that affect mRNA decay in Escherichia coli, and by inference in other bacteria, has been gleaned from study of less than 25 of the approximately 4,300 predicted E. coli messages. To investigate these factors more broadly, we examined the half-lives and steady-state abundance of known and predicted E. coli mRNAs at single-gene resolution by using two-color fluorescent DNA microarrays. An rRNA-based strategy for normalization of microarray data was developed to permit quantitation of mRNA decay after transcriptional arrest by rifampicin. We found that globally, mRNA half-lives were similar in nutrient-rich media and defined media in which the generation time was approximately tripled. A wide range of stabilities was observed for individual mRNAs of E. coli, although approximately 80% of all mRNAs had half-lives between 3 and 8 min. Genes having biologically related metabolic functions were commonly observed to have similar stabilities. Whereas the half-lives of a limited number of mRNAs correlated positively with their abundance, we found that overall, increased mRNA stability is not predictive of increased abundance. Neither the density of putative sites of cleavage by RNase E, which is believed to initiate mRNA decay in E. coli, nor the free energy of folding of 5' or 3' untranslated region sequences was predictive of mRNA half-life. Our results identify previously unsuspected features of mRNA decay at a global level and also indicate that generalizations about decay derived from the study of individual gene transcripts may have limited applicability.
Title: Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays.
Abstract: Much of the information available about factors that affect mRNA decay in Escherichia coli, and by inference in other bacteria, has been gleaned from study of less than 25 of the approximately 4,300 predicted E. coli messages. To investigate these factors more broadly, we examined the half-lives and steady-state abundance of known and predicted E. coli mRNAs at single-gene resolution by using two-color fluorescent DNA microarrays. An rRNA-based strategy for normalization of microarray data was developed to permit quantitation of mRNA decay after transcriptional arrest by rifampicin. We found that globally, mRNA half-lives were similar in nutrient-rich media and defined media in which the generation time was approximately tripled. A wide range of stabilities was observed for individual mRNAs of E. coli, although approximately 80% of all mRNAs had half-lives between 3 and 8 min. Genes having biologically related metabolic functions were commonly observed to have similar stabilities. Whereas the half-lives of a limited number of mRNAs correlated positively with their abundance, we found that overall, increased mRNA stability is not predictive of increased abundance. Neither the density of putative sites of cleavage by RNase E, which is believed to initiate mRNA decay in E. coli, nor the free energy of folding of 5' or 3' untranslated region sequences was predictive of mRNA half-life. Our results identify previously unsuspected features of mRNA decay at a global level and also indicate that generalizations about decay derived from the study of individual gene transcripts may have limited applicability.
Title: Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays.
Abstract: Much of the information available about factors that affect mRNA decay in Escherichia coli, and by inference in other bacteria, has been gleaned from study of less than 25 of the approximately 4,300 predicted E. coli messages. To investigate these factors more broadly, we examined the half-lives and steady-state abundance of known and predicted E. coli mRNAs at single-gene resolution by using two-color fluorescent DNA microarrays. An rRNA-based strategy for normalization of microarray data was developed to permit quantitation of mRNA decay after transcriptional arrest by rifampicin. We found that globally, mRNA half-lives were similar in nutrient-rich media and defined media in which the generation time was approximately tripled. A wide range of stabilities was observed for individual mRNAs of E. coli, although approximately 80% of all mRNAs had half-lives between 3 and 8 min. Genes having biologically related metabolic functions were commonly observed to have similar stabilities. Whereas the half-lives of a limited number of mRNAs correlated positively with their abundance, we found that overall, increased mRNA stability is not predictive of increased abundance. Neither the density of putative sites of cleavage by RNase E, which is believed to initiate mRNA decay in E. coli, nor the free energy of folding of 5' or 3' untranslated region sequences was predictive of mRNA half-life. Our results identify previously unsuspected features of mRNA decay at a global level and also indicate that generalizations about decay derived from the study of individual gene transcripts may have limited applicability.
Title: Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays.
Abstract: Much of the information available about factors that affect mRNA decay in Escherichia coli, and by inference in other bacteria, has been gleaned from study of less than 25 of the approximately 4,300 predicted E. coli messages. To investigate these factors more broadly, we examined the half-lives and steady-state abundance of known and predicted E. coli mRNAs at single-gene resolution by using two-color fluorescent DNA microarrays. An rRNA-based strategy for normalization of microarray data was developed to permit quantitation of mRNA decay after transcriptional arrest by rifampicin. We found that globally, mRNA half-lives were similar in nutrient-rich media and defined media in which the generation time was approximately tripled. A wide range of stabilities was observed for individual mRNAs of E. coli, although approximately 80% of all mRNAs had half-lives between 3 and 8 min. Genes having biologically related metabolic functions were commonly observed to have similar stabilities. Whereas the half-lives of a limited number of mRNAs correlated positively with their abundance, we found that overall, increased mRNA stability is not predictive of increased abundance. Neither the density of putative sites of cleavage by RNase E, which is believed to initiate mRNA decay in E. coli, nor the free energy of folding of 5' or 3' untranslated region sequences was predictive of mRNA half-life. Our results identify previously unsuspected features of mRNA decay at a global level and also indicate that generalizations about decay derived from the study of individual gene transcripts may have limited applicability.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays.
Abstract: Much of the information available about factors that affect mRNA decay in Escherichia coli, and by inference in other bacteria, has been gleaned from study of less than 25 of the approximately 4,300 predicted E. coli messages. To investigate these factors more broadly, we examined the half-lives and steady-state abundance of known and predicted E. coli mRNAs at single-gene resolution by using two-color fluorescent DNA microarrays. An rRNA-based strategy for normalization of microarray data was developed to permit quantitation of mRNA decay after transcriptional arrest by rifampicin. We found that globally, mRNA half-lives were similar in nutrient-rich media and defined media in which the generation time was approximately tripled. A wide range of stabilities was observed for individual mRNAs of E. coli, although approximately 80% of all mRNAs had half-lives between 3 and 8 min. Genes having biologically related metabolic functions were commonly observed to have similar stabilities. Whereas the half-lives of a limited number of mRNAs correlated positively with their abundance, we found that overall, increased mRNA stability is not predictive of increased abundance. Neither the density of putative sites of cleavage by RNase E, which is believed to initiate mRNA decay in E. coli, nor the free energy of folding of 5' or 3' untranslated region sequences was predictive of mRNA half-life. Our results identify previously unsuspected features of mRNA decay at a global level and also indicate that generalizations about decay derived from the study of individual gene transcripts may have limited applicability.
Title: Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays.
Abstract: Much of the information available about factors that affect mRNA decay in Escherichia coli, and by inference in other bacteria, has been gleaned from study of less than 25 of the approximately 4,300 predicted E. coli messages. To investigate these factors more broadly, we examined the half-lives and steady-state abundance of known and predicted E. coli mRNAs at single-gene resolution by using two-color fluorescent DNA microarrays. An rRNA-based strategy for normalization of microarray data was developed to permit quantitation of mRNA decay after transcriptional arrest by rifampicin. We found that globally, mRNA half-lives were similar in nutrient-rich media and defined media in which the generation time was approximately tripled. A wide range of stabilities was observed for individual mRNAs of E. coli, although approximately 80% of all mRNAs had half-lives between 3 and 8 min. Genes having biologically related metabolic functions were commonly observed to have similar stabilities. Whereas the half-lives of a limited number of mRNAs correlated positively with their abundance, we found that overall, increased mRNA stability is not predictive of increased abundance. Neither the density of putative sites of cleavage by RNase E, which is believed to initiate mRNA decay in E. coli, nor the free energy of folding of 5' or 3' untranslated region sequences was predictive of mRNA half-life. Our results identify previously unsuspected features of mRNA decay at a global level and also indicate that generalizations about decay derived from the study of individual gene transcripts may have limited applicability.
Title: Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays.
Abstract: Much of the information available about factors that affect mRNA decay in Escherichia coli, and by inference in other bacteria, has been gleaned from study of less than 25 of the approximately 4,300 predicted E. coli messages. To investigate these factors more broadly, we examined the half-lives and steady-state abundance of known and predicted E. coli mRNAs at single-gene resolution by using two-color fluorescent DNA microarrays. An rRNA-based strategy for normalization of microarray data was developed to permit quantitation of mRNA decay after transcriptional arrest by rifampicin. We found that globally, mRNA half-lives were similar in nutrient-rich media and defined media in which the generation time was approximately tripled. A wide range of stabilities was observed for individual mRNAs of E. coli, although approximately 80% of all mRNAs had half-lives between 3 and 8 min. Genes having biologically related metabolic functions were commonly observed to have similar stabilities. Whereas the half-lives of a limited number of mRNAs correlated positively with their abundance, we found that overall, increased mRNA stability is not predictive of increased abundance. Neither the density of putative sites of cleavage by RNase E, which is believed to initiate mRNA decay in E. coli, nor the free energy of folding of 5' or 3' untranslated region sequences was predictive of mRNA half-life. Our results identify previously unsuspected features of mRNA decay at a global level and also indicate that generalizations about decay derived from the study of individual gene transcripts may have limited applicability.
Title: Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays.
Abstract: Much of the information available about factors that affect mRNA decay in Escherichia coli, and by inference in other bacteria, has been gleaned from study of less than 25 of the approximately 4,300 predicted E. coli messages. To investigate these factors more broadly, we examined the half-lives and steady-state abundance of known and predicted E. coli mRNAs at single-gene resolution by using two-color fluorescent DNA microarrays. An rRNA-based strategy for normalization of microarray data was developed to permit quantitation of mRNA decay after transcriptional arrest by rifampicin. We found that globally, mRNA half-lives were similar in nutrient-rich media and defined media in which the generation time was approximately tripled. A wide range of stabilities was observed for individual mRNAs of E. coli, although approximately 80% of all mRNAs had half-lives between 3 and 8 min. Genes having biologically related metabolic functions were commonly observed to have similar stabilities. Whereas the half-lives of a limited number of mRNAs correlated positively with their abundance, we found that overall, increased mRNA stability is not predictive of increased abundance. Neither the density of putative sites of cleavage by RNase E, which is believed to initiate mRNA decay in E. coli, nor the free energy of folding of 5' or 3' untranslated region sequences was predictive of mRNA half-life. Our results identify previously unsuspected features of mRNA decay at a global level and also indicate that generalizations about decay derived from the study of individual gene transcripts may have limited applicability.
Title: Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays.
Abstract: Much of the information available about factors that affect mRNA decay in Escherichia coli, and by inference in other bacteria, has been gleaned from study of less than 25 of the approximately 4,300 predicted E. coli messages. To investigate these factors more broadly, we examined the half-lives and steady-state abundance of known and predicted E. coli mRNAs at single-gene resolution by using two-color fluorescent DNA microarrays. An rRNA-based strategy for normalization of microarray data was developed to permit quantitation of mRNA decay after transcriptional arrest by rifampicin. We found that globally, mRNA half-lives were similar in nutrient-rich media and defined media in which the generation time was approximately tripled. A wide range of stabilities was observed for individual mRNAs of E. coli, although approximately 80% of all mRNAs had half-lives between 3 and 8 min. Genes having biologically related metabolic functions were commonly observed to have similar stabilities. Whereas the half-lives of a limited number of mRNAs correlated positively with their abundance, we found that overall, increased mRNA stability is not predictive of increased abundance. Neither the density of putative sites of cleavage by RNase E, which is believed to initiate mRNA decay in E. coli, nor the free energy of folding of 5' or 3' untranslated region sequences was predictive of mRNA half-life. Our results identify previously unsuspected features of mRNA decay at a global level and also indicate that generalizations about decay derived from the study of individual gene transcripts may have limited applicability.
Title: Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays.
Abstract: Much of the information available about factors that affect mRNA decay in Escherichia coli, and by inference in other bacteria, has been gleaned from study of less than 25 of the approximately 4,300 predicted E. coli messages. To investigate these factors more broadly, we examined the half-lives and steady-state abundance of known and predicted E. coli mRNAs at single-gene resolution by using two-color fluorescent DNA microarrays. An rRNA-based strategy for normalization of microarray data was developed to permit quantitation of mRNA decay after transcriptional arrest by rifampicin. We found that globally, mRNA half-lives were similar in nutrient-rich media and defined media in which the generation time was approximately tripled. A wide range of stabilities was observed for individual mRNAs of E. coli, although approximately 80% of all mRNAs had half-lives between 3 and 8 min. Genes having biologically related metabolic functions were commonly observed to have similar stabilities. Whereas the half-lives of a limited number of mRNAs correlated positively with their abundance, we found that overall, increased mRNA stability is not predictive of increased abundance. Neither the density of putative sites of cleavage by RNase E, which is believed to initiate mRNA decay in E. coli, nor the free energy of folding of 5' or 3' untranslated region sequences was predictive of mRNA half-life. Our results identify previously unsuspected features of mRNA decay at a global level and also indicate that generalizations about decay derived from the study of individual gene transcripts may have limited applicability.
Title: Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays.
Abstract: Much of the information available about factors that affect mRNA decay in Escherichia coli, and by inference in other bacteria, has been gleaned from study of less than 25 of the approximately 4,300 predicted E. coli messages. To investigate these factors more broadly, we examined the half-lives and steady-state abundance of known and predicted E. coli mRNAs at single-gene resolution by using two-color fluorescent DNA microarrays. An rRNA-based strategy for normalization of microarray data was developed to permit quantitation of mRNA decay after transcriptional arrest by rifampicin. We found that globally, mRNA half-lives were similar in nutrient-rich media and defined media in which the generation time was approximately tripled. A wide range of stabilities was observed for individual mRNAs of E. coli, although approximately 80% of all mRNAs had half-lives between 3 and 8 min. Genes having biologically related metabolic functions were commonly observed to have similar stabilities. Whereas the half-lives of a limited number of mRNAs correlated positively with their abundance, we found that overall, increased mRNA stability is not predictive of increased abundance. Neither the density of putative sites of cleavage by RNase E, which is believed to initiate mRNA decay in E. coli, nor the free energy of folding of 5' or 3' untranslated region sequences was predictive of mRNA half-life. Our results identify previously unsuspected features of mRNA decay at a global level and also indicate that generalizations about decay derived from the study of individual gene transcripts may have limited applicability.
Title: Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays.
Abstract: Much of the information available about factors that affect mRNA decay in Escherichia coli, and by inference in other bacteria, has been gleaned from study of less than 25 of the approximately 4,300 predicted E. coli messages. To investigate these factors more broadly, we examined the half-lives and steady-state abundance of known and predicted E. coli mRNAs at single-gene resolution by using two-color fluorescent DNA microarrays. An rRNA-based strategy for normalization of microarray data was developed to permit quantitation of mRNA decay after transcriptional arrest by rifampicin. We found that globally, mRNA half-lives were similar in nutrient-rich media and defined media in which the generation time was approximately tripled. A wide range of stabilities was observed for individual mRNAs of E. coli, although approximately 80% of all mRNAs had half-lives between 3 and 8 min. Genes having biologically related metabolic functions were commonly observed to have similar stabilities. Whereas the half-lives of a limited number of mRNAs correlated positively with their abundance, we found that overall, increased mRNA stability is not predictive of increased abundance. Neither the density of putative sites of cleavage by RNase E, which is believed to initiate mRNA decay in E. coli, nor the free energy of folding of 5' or 3' untranslated region sequences was predictive of mRNA half-life. Our results identify previously unsuspected features of mRNA decay at a global level and also indicate that generalizations about decay derived from the study of individual gene transcripts may have limited applicability.
Title: Analysis of topoisomerase function in bacterial replication fork movement:use of DNA microarrays.
Abstract: We used DNA microarrays of the Escherichia coli genome to trace the progression of chromosomal replication forks in synchronized cells. We found that both DNA gyrase and topoisomerase IV (topo IV) promote replication fork progression. When both enzymes were inhibited, the replication fork stopped rapidly. The elongation rate with topo IV alone was 1/3 of normal. Genetic data confirmed and extended these results. Inactivation of gyrase alone caused a slow stop of replication. Topo IV activity was sufficient to prevent accumulation of (+) supercoils in plasmid DNA in vivo, suggesting that topo IV can promote replication by removing (+) supercoils in front of the chromosomal fork.
Title: DNA microarray analysis of gene expression in response to physiological and genetic changes that affect tryptophan metabolism in Escherichia coli.
Abstract: We investigated the global changes in mRNA abundance in Escherichia coli elicited by various perturbations of tryptophan metabolism. To do so we printed DNA microarrays containing 95% of all annotated E. coli ORFs. We determined the expression profile that is predominantly dictated by the activity of the tryptophan repressor. Only three operons, trp, mtr, and aroH, exhibited appreciable expression changes consistent with this profile. The quantitative changes we observed in mRNA levels for the five genes of the trp operon were consistent within a factor of 2, with expectations based on established Trp protein levels. Several operons known to be regulated by the TyrR protein, aroF-tyrA, aroL, aroP, and aroG, were down-regulated on addition of tryptophan. TyrR can be activated by any one of the three aromatic amino acids. Only one operon, tnaAB, was significantly activated by the presence of tryptophan in the medium. We uncovered a plethora of likely indirect effects of changes in tryptophan metabolism on intracellular mRNA pools, most prominent of which was the sensitivity of arginine biosynthetic operons to tryptophan starvation.
Title: DpiA binding to the replication origin of Escherichia coli plasmids and chromosomes destabilizes plasmid inheritance and induces the bacterial SOS response.
Abstract: The dpiA and dpiB genes of Escherichia coli, which are orthologs of genes that regulate citrate uptake and utilization in Klebsiella pneumoniae, comprise a two-component signal transduction system that can modulate the replication of and destabilize the inheritance of pSC101 and certain other plasmids. Here we show that perturbed replication and inheritance result from binding of the effector protein DpiA to A+T-rich replication origin sequences that resemble those in the K. pneumoniae promoter region targeted by the DpiA ortholog, CitB. Consistent with its ability to bind to A+T-rich origin sequences, overproduction of DpiA induced the SOS response in E. coli, suggesting that chromosomal DNA replication is affected. Bacteria that overexpressed DpiA showed an increased amount of DNA per cell and increased cell size-both also characteristic of the SOS response. Concurrent overexpression of the DNA replication initiation protein, DnaA, or the DNA helicase, DnaB-both of which act at A+T-rich replication origin sequences in the E. coli chromosome and DpiA-targeted plasmids-reversed SOS induction as well as plasmid destabilization by DpiA. Our finding that physical and functional interactions between DpiA and sites of replication initiation modulate DNA replication and plasmid inheritance suggests a mechanism by which environmental stimuli transmitted by these gene products can regulate chromosomal and plasmid dynamics.
Title: DpiA binding to the replication origin of Escherichia coli plasmids and chromosomes destabilizes plasmid inheritance and induces the bacterial SOS response.
Abstract: The dpiA and dpiB genes of Escherichia coli, which are orthologs of genes that regulate citrate uptake and utilization in Klebsiella pneumoniae, comprise a two-component signal transduction system that can modulate the replication of and destabilize the inheritance of pSC101 and certain other plasmids. Here we show that perturbed replication and inheritance result from binding of the effector protein DpiA to A+T-rich replication origin sequences that resemble those in the K. pneumoniae promoter region targeted by the DpiA ortholog, CitB. Consistent with its ability to bind to A+T-rich origin sequences, overproduction of DpiA induced the SOS response in E. coli, suggesting that chromosomal DNA replication is affected. Bacteria that overexpressed DpiA showed an increased amount of DNA per cell and increased cell size-both also characteristic of the SOS response. Concurrent overexpression of the DNA replication initiation protein, DnaA, or the DNA helicase, DnaB-both of which act at A+T-rich replication origin sequences in the E. coli chromosome and DpiA-targeted plasmids-reversed SOS induction as well as plasmid destabilization by DpiA. Our finding that physical and functional interactions between DpiA and sites of replication initiation modulate DNA replication and plasmid inheritance suggests a mechanism by which environmental stimuli transmitted by these gene products can regulate chromosomal and plasmid dynamics.
Title: RNase G complementation of rne null mutation identifies functional interrelationships with RNase E in Escherichia coli.
Abstract: The Escherichia coli endoribonucleases RNase E (Rne) and RNase G (Rng) have sequence similarity and broadly similar sequence specificity. Whereas the absence of Rne normally is lethal, we show here that E. coli bacteria that lack the rne gene can be made viable by overexpression of Rng. Rng-complemented cells accumulated precursors of 5S ribosomal RNA (rRNA) and the RNA component of RNase P (i.e. M1 RNA), indicating that normal processing of these Rne-cleaved RNAs was not restored by RNase G; additionally, neither 5S rRNA nor M1 RNA was generated from precursors by RNase G cleavage in vitro. Using DNA microarrays containing 4405 Escherichia coli open reading frames (ORFs), we identified mRNAs whose steady-state level was affected by Rne, Rng or the N-terminal catalytic domain of RNase E. Most transcript species affected by RNase E deficiency were also elevated in an rne deletion mutant complemented by Rng. However, approximately 100 mRNAs that accumulated in Rne-deficient cells were decreased by rng-complemention, thus identifying targets whose processing or degradation may be the basis for RNase E essentiality. Remarkably prominent in this group were mRNAs implicated in energy-generating pathways or in the synthesis or degradation of macromolecules.
Title: RNase G complementation of rne null mutation identifies functional interrelationships with RNase E in Escherichia coli.
Abstract: The Escherichia coli endoribonucleases RNase E (Rne) and RNase G (Rng) have sequence similarity and broadly similar sequence specificity. Whereas the absence of Rne normally is lethal, we show here that E. coli bacteria that lack the rne gene can be made viable by overexpression of Rng. Rng-complemented cells accumulated precursors of 5S ribosomal RNA (rRNA) and the RNA component of RNase P (i.e. M1 RNA), indicating that normal processing of these Rne-cleaved RNAs was not restored by RNase G; additionally, neither 5S rRNA nor M1 RNA was generated from precursors by RNase G cleavage in vitro. Using DNA microarrays containing 4405 Escherichia coli open reading frames (ORFs), we identified mRNAs whose steady-state level was affected by Rne, Rng or the N-terminal catalytic domain of RNase E. Most transcript species affected by RNase E deficiency were also elevated in an rne deletion mutant complemented by Rng. However, approximately 100 mRNAs that accumulated in Rne-deficient cells were decreased by rng-complemention, thus identifying targets whose processing or degradation may be the basis for RNase E essentiality. Remarkably prominent in this group were mRNAs implicated in energy-generating pathways or in the synthesis or degradation of macromolecules.
Title: Adaptation to famine: a family of stationary-phase genes revealed by microarray analysis.
Abstract: Bacterial adaptation to nutrient limitation and increased population densities is central to survival and virulence. Surprisingly, <3% of Escherichia coli genes are known to play roles specific to the stationary phase. There is evidence that the leucine-responsive regulatory protein (Lrp) may play an important role in stationary phase, so this study used microarrays representing >98% of E. coli genes to more comprehensively identify those controlled by Lrp. The primary analysis compared isogenic Lrp(+) and Lrp(-) strains in cells growing in steady state in glucose minimal medium, either in the presence or absence of leucine. More than 400 genes were significantly Lrp-responsive under the conditions used. Transcription of 147 genes was lower in Lrp(+) than in Lrp(-) cells whether or not leucine was present; most of these genes were tightly coregulated under several conditions, including a burst of synthesis on transition to stationary phase. This cluster includes 56 of 115 genes already known to play roles in stationary phase. Our results suggest that the actual number of genes induced on entrance into stationary phase is closer to 200 and that Lrp affects nearly three-quarters of them, including genes involved in response to nutrient limitation, high concentrations of organic acids, and osmotic stress.
Title: Adaptation to famine: a family of stationary-phase genes revealed by microarray analysis.
Abstract: Bacterial adaptation to nutrient limitation and increased population densities is central to survival and virulence. Surprisingly, <3% of Escherichia coli genes are known to play roles specific to the stationary phase. There is evidence that the leucine-responsive regulatory protein (Lrp) may play an important role in stationary phase, so this study used microarrays representing >98% of E. coli genes to more comprehensively identify those controlled by Lrp. The primary analysis compared isogenic Lrp(+) and Lrp(-) strains in cells growing in steady state in glucose minimal medium, either in the presence or absence of leucine. More than 400 genes were significantly Lrp-responsive under the conditions used. Transcription of 147 genes was lower in Lrp(+) than in Lrp(-) cells whether or not leucine was present; most of these genes were tightly coregulated under several conditions, including a burst of synthesis on transition to stationary phase. This cluster includes 56 of 115 genes already known to play roles in stationary phase. Our results suggest that the actual number of genes induced on entrance into stationary phase is closer to 200 and that Lrp affects nearly three-quarters of them, including genes involved in response to nutrient limitation, high concentrations of organic acids, and osmotic stress.
Title: Adaptation to famine: a family of stationary-phase genes revealed by microarray analysis.
Abstract: Bacterial adaptation to nutrient limitation and increased population densities is central to survival and virulence. Surprisingly, <3% of Escherichia coli genes are known to play roles specific to the stationary phase. There is evidence that the leucine-responsive regulatory protein (Lrp) may play an important role in stationary phase, so this study used microarrays representing >98% of E. coli genes to more comprehensively identify those controlled by Lrp. The primary analysis compared isogenic Lrp(+) and Lrp(-) strains in cells growing in steady state in glucose minimal medium, either in the presence or absence of leucine. More than 400 genes were significantly Lrp-responsive under the conditions used. Transcription of 147 genes was lower in Lrp(+) than in Lrp(-) cells whether or not leucine was present; most of these genes were tightly coregulated under several conditions, including a burst of synthesis on transition to stationary phase. This cluster includes 56 of 115 genes already known to play roles in stationary phase. Our results suggest that the actual number of genes induced on entrance into stationary phase is closer to 200 and that Lrp affects nearly three-quarters of them, including genes involved in response to nutrient limitation, high concentrations of organic acids, and osmotic stress.
Title: Adaptation to famine: a family of stationary-phase genes revealed by microarray analysis.
Abstract: Bacterial adaptation to nutrient limitation and increased population densities is central to survival and virulence. Surprisingly, <3% of Escherichia coli genes are known to play roles specific to the stationary phase. There is evidence that the leucine-responsive regulatory protein (Lrp) may play an important role in stationary phase, so this study used microarrays representing >98% of E. coli genes to more comprehensively identify those controlled by Lrp. The primary analysis compared isogenic Lrp(+) and Lrp(-) strains in cells growing in steady state in glucose minimal medium, either in the presence or absence of leucine. More than 400 genes were significantly Lrp-responsive under the conditions used. Transcription of 147 genes was lower in Lrp(+) than in Lrp(-) cells whether or not leucine was present; most of these genes were tightly coregulated under several conditions, including a burst of synthesis on transition to stationary phase. This cluster includes 56 of 115 genes already known to play roles in stationary phase. Our results suggest that the actual number of genes induced on entrance into stationary phase is closer to 200 and that Lrp affects nearly three-quarters of them, including genes involved in response to nutrient limitation, high concentrations of organic acids, and osmotic stress.
Title: RNase G complementation of rne null mutation identifies functional interrelationships with RNase E in Escherichia coli.
Abstract: The Escherichia coli endoribonucleases RNase E (Rne) and RNase G (Rng) have sequence similarity and broadly similar sequence specificity. Whereas the absence of Rne normally is lethal, we show here that E. coli bacteria that lack the rne gene can be made viable by overexpression of Rng. Rng-complemented cells accumulated precursors of 5S ribosomal RNA (rRNA) and the RNA component of RNase P (i.e. M1 RNA), indicating that normal processing of these Rne-cleaved RNAs was not restored by RNase G; additionally, neither 5S rRNA nor M1 RNA was generated from precursors by RNase G cleavage in vitro. Using DNA microarrays containing 4405 Escherichia coli open reading frames (ORFs), we identified mRNAs whose steady-state level was affected by Rne, Rng or the N-terminal catalytic domain of RNase E. Most transcript species affected by RNase E deficiency were also elevated in an rne deletion mutant complemented by Rng. However, approximately 100 mRNAs that accumulated in Rne-deficient cells were decreased by rng-complemention, thus identifying targets whose processing or degradation may be the basis for RNase E essentiality. Remarkably prominent in this group were mRNAs implicated in energy-generating pathways or in the synthesis or degradation of macromolecules.
Title: RNase G complementation of rne null mutation identifies functional interrelationships with RNase E in Escherichia coli.
Abstract: The Escherichia coli endoribonucleases RNase E (Rne) and RNase G (Rng) have sequence similarity and broadly similar sequence specificity. Whereas the absence of Rne normally is lethal, we show here that E. coli bacteria that lack the rne gene can be made viable by overexpression of Rng. Rng-complemented cells accumulated precursors of 5S ribosomal RNA (rRNA) and the RNA component of RNase P (i.e. M1 RNA), indicating that normal processing of these Rne-cleaved RNAs was not restored by RNase G; additionally, neither 5S rRNA nor M1 RNA was generated from precursors by RNase G cleavage in vitro. Using DNA microarrays containing 4405 Escherichia coli open reading frames (ORFs), we identified mRNAs whose steady-state level was affected by Rne, Rng or the N-terminal catalytic domain of RNase E. Most transcript species affected by RNase E deficiency were also elevated in an rne deletion mutant complemented by Rng. However, approximately 100 mRNAs that accumulated in Rne-deficient cells were decreased by rng-complemention, thus identifying targets whose processing or degradation may be the basis for RNase E essentiality. Remarkably prominent in this group were mRNAs implicated in energy-generating pathways or in the synthesis or degradation of macromolecules.
Title: RNase G complementation of rne null mutation identifies functional interrelationships with RNase E in Escherichia coli.
Abstract: The Escherichia coli endoribonucleases RNase E (Rne) and RNase G (Rng) have sequence similarity and broadly similar sequence specificity. Whereas the absence of Rne normally is lethal, we show here that E. coli bacteria that lack the rne gene can be made viable by overexpression of Rng. Rng-complemented cells accumulated precursors of 5S ribosomal RNA (rRNA) and the RNA component of RNase P (i.e. M1 RNA), indicating that normal processing of these Rne-cleaved RNAs was not restored by RNase G; additionally, neither 5S rRNA nor M1 RNA was generated from precursors by RNase G cleavage in vitro. Using DNA microarrays containing 4405 Escherichia coli open reading frames (ORFs), we identified mRNAs whose steady-state level was affected by Rne, Rng or the N-terminal catalytic domain of RNase E. Most transcript species affected by RNase E deficiency were also elevated in an rne deletion mutant complemented by Rng. However, approximately 100 mRNAs that accumulated in Rne-deficient cells were decreased by rng-complemention, thus identifying targets whose processing or degradation may be the basis for RNase E essentiality. Remarkably prominent in this group were mRNAs implicated in energy-generating pathways or in the synthesis or degradation of macromolecules.
Title: RNase G complementation of rne null mutation identifies functional interrelationships with RNase E in Escherichia coli.
Abstract: The Escherichia coli endoribonucleases RNase E (Rne) and RNase G (Rng) have sequence similarity and broadly similar sequence specificity. Whereas the absence of Rne normally is lethal, we show here that E. coli bacteria that lack the rne gene can be made viable by overexpression of Rng. Rng-complemented cells accumulated precursors of 5S ribosomal RNA (rRNA) and the RNA component of RNase P (i.e. M1 RNA), indicating that normal processing of these Rne-cleaved RNAs was not restored by RNase G; additionally, neither 5S rRNA nor M1 RNA was generated from precursors by RNase G cleavage in vitro. Using DNA microarrays containing 4405 Escherichia coli open reading frames (ORFs), we identified mRNAs whose steady-state level was affected by Rne, Rng or the N-terminal catalytic domain of RNase E. Most transcript species affected by RNase E deficiency were also elevated in an rne deletion mutant complemented by Rng. However, approximately 100 mRNAs that accumulated in Rne-deficient cells were decreased by rng-complemention, thus identifying targets whose processing or degradation may be the basis for RNase E essentiality. Remarkably prominent in this group were mRNAs implicated in energy-generating pathways or in the synthesis or degradation of macromolecules.
Title: RNase G complementation of rne null mutation identifies functional interrelationships with RNase E in Escherichia coli.
Abstract: The Escherichia coli endoribonucleases RNase E (Rne) and RNase G (Rng) have sequence similarity and broadly similar sequence specificity. Whereas the absence of Rne normally is lethal, we show here that E. coli bacteria that lack the rne gene can be made viable by overexpression of Rng. Rng-complemented cells accumulated precursors of 5S ribosomal RNA (rRNA) and the RNA component of RNase P (i.e. M1 RNA), indicating that normal processing of these Rne-cleaved RNAs was not restored by RNase G; additionally, neither 5S rRNA nor M1 RNA was generated from precursors by RNase G cleavage in vitro. Using DNA microarrays containing 4405 Escherichia coli open reading frames (ORFs), we identified mRNAs whose steady-state level was affected by Rne, Rng or the N-terminal catalytic domain of RNase E. Most transcript species affected by RNase E deficiency were also elevated in an rne deletion mutant complemented by Rng. However, approximately 100 mRNAs that accumulated in Rne-deficient cells were decreased by rng-complemention, thus identifying targets whose processing or degradation may be the basis for RNase E essentiality. Remarkably prominent in this group were mRNAs implicated in energy-generating pathways or in the synthesis or degradation of macromolecules.
Title: RNase G complementation of rne null mutation identifies functional interrelationships with RNase E in Escherichia coli.
Abstract: The Escherichia coli endoribonucleases RNase E (Rne) and RNase G (Rng) have sequence similarity and broadly similar sequence specificity. Whereas the absence of Rne normally is lethal, we show here that E. coli bacteria that lack the rne gene can be made viable by overexpression of Rng. Rng-complemented cells accumulated precursors of 5S ribosomal RNA (rRNA) and the RNA component of RNase P (i.e. M1 RNA), indicating that normal processing of these Rne-cleaved RNAs was not restored by RNase G; additionally, neither 5S rRNA nor M1 RNA was generated from precursors by RNase G cleavage in vitro. Using DNA microarrays containing 4405 Escherichia coli open reading frames (ORFs), we identified mRNAs whose steady-state level was affected by Rne, Rng or the N-terminal catalytic domain of RNase E. Most transcript species affected by RNase E deficiency were also elevated in an rne deletion mutant complemented by Rng. However, approximately 100 mRNAs that accumulated in Rne-deficient cells were decreased by rng-complemention, thus identifying targets whose processing or degradation may be the basis for RNase E essentiality. Remarkably prominent in this group were mRNAs implicated in energy-generating pathways or in the synthesis or degradation of macromolecules.
Title: RNase G complementation of rne null mutation identifies functional interrelationships with RNase E in Escherichia coli.
Abstract: The Escherichia coli endoribonucleases RNase E (Rne) and RNase G (Rng) have sequence similarity and broadly similar sequence specificity. Whereas the absence of Rne normally is lethal, we show here that E. coli bacteria that lack the rne gene can be made viable by overexpression of Rng. Rng-complemented cells accumulated precursors of 5S ribosomal RNA (rRNA) and the RNA component of RNase P (i.e. M1 RNA), indicating that normal processing of these Rne-cleaved RNAs was not restored by RNase G; additionally, neither 5S rRNA nor M1 RNA was generated from precursors by RNase G cleavage in vitro. Using DNA microarrays containing 4405 Escherichia coli open reading frames (ORFs), we identified mRNAs whose steady-state level was affected by Rne, Rng or the N-terminal catalytic domain of RNase E. Most transcript species affected by RNase E deficiency were also elevated in an rne deletion mutant complemented by Rng. However, approximately 100 mRNAs that accumulated in Rne-deficient cells were decreased by rng-complemention, thus identifying targets whose processing or degradation may be the basis for RNase E essentiality. Remarkably prominent in this group were mRNAs implicated in energy-generating pathways or in the synthesis or degradation of macromolecules.
Title: RNase G complementation of rne null mutation identifies functional interrelationships with RNase E in Escherichia coli.
Abstract: The Escherichia coli endoribonucleases RNase E (Rne) and RNase G (Rng) have sequence similarity and broadly similar sequence specificity. Whereas the absence of Rne normally is lethal, we show here that E. coli bacteria that lack the rne gene can be made viable by overexpression of Rng. Rng-complemented cells accumulated precursors of 5S ribosomal RNA (rRNA) and the RNA component of RNase P (i.e. M1 RNA), indicating that normal processing of these Rne-cleaved RNAs was not restored by RNase G; additionally, neither 5S rRNA nor M1 RNA was generated from precursors by RNase G cleavage in vitro. Using DNA microarrays containing 4405 Escherichia coli open reading frames (ORFs), we identified mRNAs whose steady-state level was affected by Rne, Rng or the N-terminal catalytic domain of RNase E. Most transcript species affected by RNase E deficiency were also elevated in an rne deletion mutant complemented by Rng. However, approximately 100 mRNAs that accumulated in Rne-deficient cells were decreased by rng-complemention, thus identifying targets whose processing or degradation may be the basis for RNase E essentiality. Remarkably prominent in this group were mRNAs implicated in energy-generating pathways or in the synthesis or degradation of macromolecules.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of Escherichia coli RNA degradosome function using DNA microarrays.
Abstract: RNase E, an essential endoribonuclease of Escherichia coli, interacts through its C-terminal region with multiple other proteins to form a complex termed the RNA degradosome. To investigate the degradosome's proposed role as an RNA decay machine, we used DNA microarrays to globally assess alterations in the steady-state abundance and decay of 4,289 E. coli mRNAs at single-gene resolution in bacteria carrying mutations in the degradosome constituents RNase E, polynucleotide phosphorylase, RhlB helicase, and enolase. Our results show that the functions of all four of these proteins are necessary for normal mRNA turnover. We identified specific transcripts and functionally distinguishable transcript classes whose half-life and abundance were affected congruently by multiple degradosome proteins, affected differentially by mutations in degradosome constituents, or not detectably altered by degradosome mutations. Our results, which argue that decay of some E. coli mRNAs in vivo depends on the action of assembled degradosomes, whereas others are acted on by degradosome proteins functioning independently of the complex, imply the existence of structural features or biochemical factors that target specific classes of mRNAs for decay by degradosomes.
Title: Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays.
Abstract: Much of the information available about factors that affect mRNA decay in Escherichia coli, and by inference in other bacteria, has been gleaned from study of less than 25 of the approximately 4,300 predicted E. coli messages. To investigate these factors more broadly, we examined the half-lives and steady-state abundance of known and predicted E. coli mRNAs at single-gene resolution by using two-color fluorescent DNA microarrays. An rRNA-based strategy for normalization of microarray data was developed to permit quantitation of mRNA decay after transcriptional arrest by rifampicin. We found that globally, mRNA half-lives were similar in nutrient-rich media and defined media in which the generation time was approximately tripled. A wide range of stabilities was observed for individual mRNAs of E. coli, although approximately 80% of all mRNAs had half-lives between 3 and 8 min. Genes having biologically related metabolic functions were commonly observed to have similar stabilities. Whereas the half-lives of a limited number of mRNAs correlated positively with their abundance, we found that overall, increased mRNA stability is not predictive of increased abundance. Neither the density of putative sites of cleavage by RNase E, which is believed to initiate mRNA decay in E. coli, nor the free energy of folding of 5' or 3' untranslated region sequences was predictive of mRNA half-life. Our results identify previously unsuspected features of mRNA decay at a global level and also indicate that generalizations about decay
Sample Name Experimental Condition Expression Value Intensity Significance Publication Gene Profiles
10min after UVtreatment 1', 40J, MG1655 in Davis+0.4%gluUltraviolet light-0.0110.770.01Courcelle J et al.(2001)Gene Profile
20min UVtreatment control, MG1655 in Davis+0.4%gluUltraviolet light - control-0.5910.100.75Courcelle J et al.(2001)Gene Profile
20min after UVtreatment 1', 40J, MG1655 in Davis+0.4%gluUltraviolet light0.2210.320.18Courcelle J et al.(2001)Gene Profile
40min after UVtreatment 1, 40J, MG1655 in Davis+0.4%gluUltraviolet light - control0.5011.020.53Courcelle J et al.(2001)Gene Profile
5min after UVtreatment 1, 40J, MG1655 in Davis+0.4%gluUltraviolet light - control-0.8610.410.84Courcelle J et al.(2001)Gene Profile
60min UVtreatment control, MG1655 in Davis+0.4%gluUltraviolet light - control-0.0710.560.11Courcelle J et al.(2001)Gene Profile
60min after UVtreatment 1, 40J, MG1655 in Davis+0.4%gluUltraviolet light-0.1011.200.12Courcelle J et al.(2001)Gene Profile
5' vs 0' in minimal medium +0.2% gluMinimal media1.7710.991.18Khodursky AB, et al. (2000)Gene Profile
15' vs 0' in minimal medium +0.2% gluMinimal media1.9211.081.42Khodursky AB, et al. (2000)Gene Profile
30' vs 0' in minimal medium +0.2% gluMinimal media1.9010.441.51Khodursky AB, et al. (2000)Gene Profile
0 min Novobiocin 0 ug/ml, dnaCacrD 30 min after synchr startReplication fork movement-0.339.010.61Khodursky AB et al.(2000)Gene Profile
60' vs 0' in minimal medium +0.2% glu, IIMinimal media1.349.011.52Khodursky AB, et al. (2000)Gene Profile
1 min Nov0 ug/ml, dnaCacrD 30 min after synchr startReplication fork movement-0.559.401.02Khodursky AB et al.(2000)Gene Profile
20 min Nov0 ug/ml, dnaCacrD 30 min after synchr startReplication fork movement-0.509.860.82Khodursky AB et al.(2000)Gene Profile
7 min Nov0 ug/ml, dnaCacrD 30 min after synchr startReplication fork movement-0.519.960.84Khodursky AB et al.(2000)Gene Profile
2 min Nov10 ug/ml, dnaCacrD 30 min after synchr startReplication fork movement + Novobiocin-0.5610.591.12Khodursky AB et al.(2000)Gene Profile
40 min Nov10 ug/ml, dnaCacrD 30 min after synchr startReplication fork movement + Novobiocin-0.3610.920.69Khodursky AB et al.(2000)Gene Profile
80 min Nov10 ug/ml, dnaCacrD 30 min after synchr startReplication fork movement + Novobiocin-0.3910.410.67Khodursky AB et al.(2000)Gene Profile
2 min Nov2 ug/ml, dnaCacrD 30 min after synchr startReplication fork movement + Novobiocin-0.619.741.14Khodursky AB et al.(2000)Gene Profile
40 min Nov2 ug/ml, dnaCacrD 30 min after synchr startReplication fork movement + Novobiocin-0.5810.961.00Khodursky AB et al.(2000)Gene Profile
2 min Nov5 ug/ml, dnaCacrD 30 min after synchr startReplication fork movement + Novobiocin-0.5410.461.17Khodursky AB et al.(2000)Gene Profile
40 min Nov5 ug/ml, dnaCacrD 30 min after synchr startReplication fork movement + Novobiocin-0.4910.750.93Khodursky AB et al.(2000)Gene Profile
80 min Nov5 ug/ml, dnaCacrD 30 min after synchr startReplication fork movement + Novobiocin-0.6811.051.02Khodursky AB et al.(2000)Gene Profile
5'+50ug/ml Trp vs 0' in min med +0.2% gluTryptophan2.0711.281.45Khodursky AB, et al. (2000)Gene Profile
15'+50ug/ml Trp vs 0' in min med +0.2% gluTryptophan1.729.651.59Khodursky AB, et al. (2000)Gene Profile
30'+50ug/ml Trp vs 0' in min med +0.2% gluTryptophan2.0410.811.61Khodursky AB, et al. (2000)Gene Profile
60'+50ug/ml Trp vs 0' in min med +0.2% glu, ITryptophan1.5010.681.32Khodursky AB, et al. (2000)Gene Profile
wt +trp vs. -trp, min+.2%glucose, W3110Tryptophan0.177.960.43Khodursky AB, et al. (2000)Gene Profile
tnaA2trpR2 vs. tnaA2, W3110 min +Trp 50ug/mlTryptophan-0.217.940.30Khodursky AB, et al. (2000)Gene Profile
trpR2 vs. wt, min+.2%glucose, W3110Minimal media-0.837.661.07Khodursky AB, et al. (2000)Gene Profile
trpR2+50ug/ml Trp vs. wt+50ug/ml TrpTryptophan-1.367.201.37Khodursky AB, et al. (2000)Gene Profile
trpR2 +trp vs. -trp, min+.2%glucose, W3110Tryptophan-0.018.590.07Khodursky AB, et al. (2000)Gene Profile
trpEA2(del) trpR2 vs. trpEA2(del), W3110 min +Trp 50ug/mlTryptophan0.628.560.67Khodursky AB, et al. (2000)Gene Profile
tnaA2trpA46PR9 vs. tnaA2, W3110 minTryptophan - control-0.537.610.81Khodursky AB, et al. (2000)Gene Profile
lexA 20' after NOuv vs. 0', MG1655Ultraviolet light - control-0.0110.850.06Courcelle J et al.(2001)Gene Profile
lexA 60' after NOuv vs. 0', MG1655Ultraviolet light - control0.0911.020.27Courcelle J et al.(2001)Gene Profile
lexA 10' after UV vs. 0', MG1655Ultraviolet light0.1511.360.27Courcelle J et al.(2001)Gene Profile
lexA 20' after UV vs. 0', MG1655Ultraviolet light0.2311.240.55Courcelle J et al.(2001)Gene Profile
lexA 40' after UV vs. 0', MG1655Ultraviolet light0.4811.440.84Courcelle J et al.(2001)Gene Profile
lexA 5' after UV vs. 0', MG1655Ultraviolet light0.0411.030.11Courcelle J et al.(2001)Gene Profile
lexA 60' after UV vs. 0', MG1655Ultraviolet light0.2111.610.27Courcelle J et al.(2001)Gene Profile
lexA vs. wt, before UV treatment, MG1655Ultraviolet light - control-0.0211.680.19Courcelle J et al.(2001)Gene Profile
0 min Nov500 ug/ml, dnaCacrD 30 min after synchr startReplication fork movement + Novobiocin-0.629.531.17Khodursky AB et al.(2000)Gene Profile
1 min Nov500 ug/ml, dnaCacrD 30 min after synchr startReplication fork movement + Novobiocin-0.699.811.22Khodursky AB et al.(2000)Gene Profile
20 min Nov500 ug/ml, dnaCacrD 30 min after synchr startReplication fork movement + Novobiocin-0.5510.191.05Khodursky AB et al.(2000)Gene Profile
20 min Nov50 ug/ml, dnaCacrD 30 min after synchr startReplication fork movement + Novobiocin-0.448.710.65Khodursky AB et al.(2000)Gene Profile
7 min Nov500 ug/ml, dnaCacrD 30 min after synchr startReplication fork movement + Novobiocin-0.6010.201.08Khodursky AB et al.(2000)Gene Profile
60' vs 0' in minimal medium +0.2% glu, IMinimal media0.8610.501.21Khodursky AB, et al. (2000)Gene Profile
60'+50ug/ml Trp vs 0' in min med +0.2% glu, IIMinimal media1.5110.681.28Khodursky AB, et al. (2000)Gene Profile
5' vs 0' indole acrylic acid (10 ug/ml)Indole acrylic acid0.548.100.74Khodursky AB, et al. (2000)Gene Profile
15' vs 0' indole acrylic acid (10 ug/ml)Indole acrylic acid0.608.110.87Khodursky AB, et al. (2000)Gene Profile
30' vs 0' indole acrylic acid (10 ug/ml)Indole acrylic acid0.598.430.62Khodursky AB, et al. (2000)Gene Profile
60' vs 0' indole acrylic acid (10 ug/ml)Indole acrylic acid0.778.271.00Khodursky AB, et al. (2000)Gene Profile
5' vs 0' indole acrylic acid (15 ug/ml)Indole acrylic acid1.368.821.46Khodursky AB, et al. (2000)Gene Profile
15' vs 0' indole acrylic acid (15 ug/ml)Indole acrylic acid0.946.881.31Khodursky AB, et al. (2000)Gene Profile
30' vs 0' indole acrylic acid (15 ug/ml)Indole acrylic acid1.458.191.43Khodursky AB, et al. (2000)Gene Profile
60' vs 0' indole acrylic acid (15 ug/ml)Indole acrylic acid1.028.060.93Khodursky AB, et al. (2000)Gene Profile
2' RNA Decay of MG1655 (Repaired NCM 3416) in LB at 30 CRNA decay-0.509.300.60Bernstein JA, et al. (2002)Gene Profile
4' RNA Decay of MG1655 (Repaired NCM 3416) in LB at 30 CRNA decay-1.119.021.27Bernstein JA, et al. (2002)Gene Profile
6' RNA Decay of MG1655 (Repaired NCM 3416) in LB at 30 CRNA decay-2.338.492.66Bernstein JA, et al. (2002)Gene Profile
8' RNA Decay of MG1655 (Repaired NCM 3416) in LB at 30 CRNA decay-1.578.631.38Bernstein JA, et al. (2002)Gene Profile
60' vs. 0', 50 ug/ml tryptophan, minimal +0.2% gluTryptophan1.5010.781.27Khodursky AB, et al. (2000)Gene Profile
1005 fork-blocking strain induced for TusReplication fork movement + Tus induction0.089.850.22Khodursky AB et al.(2000)Gene Profile
1005 fork-blocking strain induced for Tus fork5_2Replication fork movement + Tus induction-0.0710.330.21Khodursky AB et al.(2000)Gene Profile
1005 fork-blocking strain induced for Tus fork5_3Replication fork movement + Tus induction0.0710.690.14Khodursky AB et al.(2000)Gene Profile
2' RNA Decay of MG1655 (Repaired NCM 3416) in M9 + 0.2% Glucose Trial ARNA decay-0.0110.750.05Bernstein JA, et al. (2002)Gene Profile
4' RNA Decay of MG1655 (Repaired NCM 3416) in M9 + 0.2% Glucose Trial ARNA decay-0.0010.900.15Bernstein JA, et al. (2002)Gene Profile
6' RNA Decay of MG1655 (Repaired NCM 3416) in M9 + 0.2% Glucose Trial ARNA decay-0.0211.210.17Bernstein JA, et al. (2002)Gene Profile
8' RNA Decay of MG1655 (Repaired MCM 3416) in M9 + 0.2% Glucose Trial ARNA decay0.0311.600.20Bernstein JA, et al. (2002)Gene Profile
2' RNA Decay of MG1655 (Repaired NCM 3416) in M9 + 0.2% Glucose Trial BRNA decay0.0811.000.27Bernstein JA, et al. (2002)Gene Profile
4' RNA Decay of MG1655 (Repaired NCM 3416) in M9 + 0.2% Glucose Trial BRNA decay-0.2611.040.16Bernstein JA, et al. (2002)Gene Profile
6' RNA Decay of MG1655 (Repaired NCM 3416) in M9 + 0.2% Glucose Trial BRNA decay-0.6111.300.40Bernstein JA, et al. (2002)Gene Profile
8' RNA Decay of MG1655 (Repaired NCM 3416) in M9 + 0.2% Glucose Trial BRNA decay-0.1010.420.01Bernstein JA, et al. (2002)Gene Profile
dnaC2 synchrony 30' after shift, print 7 arrayReplication fork movement - control-0.4112.210.92Khodursky AB et al.(2000)Gene Profile
60' vs 0' in minimal medium +0.2% gluMinimal media0.8810.701.24Khodursky AB, et al. (2000)Gene Profile
WT1088 vs. dpiA 2x Overexpression pHI1429 in LB at 37 Mid Log Phase Trial AOverexpression0.3210.090.39Miller C, et al. (2003) 
WT1088 vs. dpiA 2x Overexpression pHI1429 in LB at 37 Mid Log Phase Trial BOverexpression0.2310.110.18Miller C, et al. (2003) 
N3433 (wt) vs N3433 (rne deletion) pBAD-RNE w/out Arabinose in LB at 30 degrees Trial AWild type vs Mutant0.1511.120.20Lee K, et al. (2002)Gene Profile
N3433 (wt) vs N3433 (rng deletion) in LB at 30 degrees C Trial BWild type vs Mutant0.2211.600.50Lee K, et al. (2002)Gene Profile
wt + Leu vs. wt - LeuLeucine-0.019.100.14Tani TH, et al. (2002) 
lrp- + Leu vs. wt - LeuLeucine-0.528.320.68Tani TH, et al. (2002) 
lrp- - Leu vs. wt - LeuLeucine-0.388.670.57Tani TH, et al. (2002) 
lrp- + Leu vs. lrp- - LeuLeucine0.118.380.08Tani TH, et al. (2002) 
N3433 (wt) vs N3433 (rne deletion) pBADRNE in LB at 30 degrees C Trial B *Wild type vs Mutant0.7111.200.62Lee K, et al. (2002)Gene Profile
N3433 (wt) vs N3433 (wt) pRNG3 in LB at 30 degrees Trial A *Overexpression0.3511.120.43Lee K, et al. (2002)Gene Profile
N3433 (wt) vs N3433 (wt) pRNG3 in LB at 30 degrees Trial B *Overexpression0.1210.180.22Lee K, et al. (2002)Gene Profile
N3433 (wt) vs N3433 (rne deletion) pRNG3 at 30 degrees C Trial A *Wild type vs Mutant1.2911.270.93Lee K, et al. (2002)Gene Profile
N3433 (wt) vs N3433 (rne deletion) pRNG3 at 30 degrees C Trial B *Wild type vs Mutant0.6210.470.46Lee K, et al. (2002)Gene Profile
N3433 (wt) vs N3433 (rne deletion) pNRNE5 at 30 degrees C Trial A *Wild type vs Mutant-0.9010.120.71Lee K, et al. (2002)Gene Profile
N3433 (wt) vs N3433 (rne deletion) pNRNE5 at 30 degrees C Trial B *Wild type vs Mutant-0.5810.140.49Lee K, et al. (2002)Gene Profile
N3433 (wt) vs N3433 (rng deletion) LB at 30 C Trial A *Wild type vs Mutant0.2810.700.55Lee K, et al. (2002)Gene Profile
1.5' RNA Decay of RhlB- (SU02) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Replicate ARNA decay0.089.890.23Bernstein JA, et al. (2004)Gene Profile
1.5' RNA Decay of RhlB- (SU02) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Replicate BRNA decay-0.238.250.36Bernstein JA, et al. (2004)Gene Profile
3' RNA Decay of RhlB- (SU02) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid LogRNA decay-0.587.900.70Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay of RhlB- (SU02) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Replicate ARNA decay0.278.960.27Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay of RhlB- (SU02) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Replicate BRNA decay-0.799.250.63Bernstein JA, et al. (2004)Gene Profile
WT (N3433) vs RhlB- (SU02) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Trial AWild type vs Mutant-0.118.690.19Bernstein JA, et al. (2004) 
WT (N3433) vs RhlB- (SU02) in M9 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Trial BWild type vs Mutant-0.357.610.43Bernstein JA, et al. (2004) 
WT (N3433) vs RhlB- (SU02) in M9 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Trial CWild type vs Mutant-0.157.690.25Bernstein JA, et al. (2004) 
1.5' RNA Decay of WT (K10) in M9 0.2% Glycerol 0.2% Tryptone, 40 mM Suc. at 30 C Mid Log Rep ARNA decay-0.607.640.60Bernstein JA, et al. (2004)Gene Profile
1.5' RNA Decay of WT (K10) in M9 0.2% Glycerol 0.2% Tryptone 40 mM Suc.at 30 C Mid Log Rep BRNA decay-0.236.800.40Bernstein JA, et al. (2004)Gene Profile
3' RNA Decay of WT (K10) in M9 0.2% Glycerol 0.2% Tryptone 40 mM Suc. at 30 C Mid LogRNA decay-1.058.560.76Bernstein JA, et al. (2004)Gene Profile
4.5' RNA Decay of WT (K10) in M9 0.2% Glycerol 0.2% Tryptone 40 mM Suc. at 30 C Mid LogRNA decay-1.216.690.78Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay of WT (K10) in M9 0.2% Glycerol 0.2% Tryptone 40 mM Suc. at 30 C Mid Log Rep ARNA decay-0.278.130.16Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay of WT (K10) in M9 0.2% Glycerol 0.2% Tryptone 40 mM Suc. at 30 C Mid Log Rep BRNA decay-1.158.150.76Bernstein JA, et al. (2004)Gene Profile
1.5' RNA Decay of Eno- (DF261) in M9 0.2% Glycerol 0.2% Tryptone, 40 mM Suc.at 30 C Mid Log Rep ARNA decay-0.269.320.28Bernstein JA, et al. (2004)Gene Profile
1.5' RNA Decay of Eno- (DF261) in M9 0.2% Glycerol 0.2% Tryptone 40 mM Suc. at 30 C Mid Log Rep BRNA decay-0.128.690.05Bernstein JA, et al. (2004)Gene Profile
3' RNA Decay of Eno- (DF261) in M9 0.2% Glycerol 0.2% Tryptone 40 mM Suc. at 30 C Mid Log Rep ARNA decay1.009.910.67Bernstein JA, et al. (2004)Gene Profile
3' RNA Decay of Eno- (DF261) in M9 0.2% Glycerol 0.2% Tryptone at 40 mM Suc. 30 C Mid Log Rep BRNA decay-0.948.530.69Bernstein JA, et al. (2004)Gene Profile
4.5' RNA Decay of Eno- (DF261) in M9 0.2% Glycerol 0.2% Tryptone 40 mM Suc. at 30 C Mid LogRNA decay-1.007.810.81Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay of Eno- (DF261) in M9 0.2% Glycerol 0.2% Tryptone 40 mM Suc. at 30 C Mid Log Rep ARNA decay-0.178.790.13Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay of Eno- (DF261) in M9 0.2% Glycerol 0.2% Tryptone 40 mM Suc. at 30 C Mid Log Rep BRNA decay-1.048.510.70Bernstein JA, et al. (2004)Gene Profile
WT (K10) vs Eno- (DF261) in M9 + 0.2% Glycerol, 0.2% Tryptone, 40 mM Suc. at 30 C Mid Log Trial AWild type vs Mutant0.249.600.31Bernstein JA, et al. (2004) 
WT (K10) vs Eno- (DF261) in M9 0.2% Glycerol, 0.2% Tryptone, 40 mM Suc. at 30 C Mid Log Trial BWild type vs Mutant0.419.100.38Bernstein JA, et al. (2004) 
1.5' RNA Decay of WT (N3433) in M9 0.2% Glycerol 0.2% Tryptone at 30 C Mid Log Replicate A1RNA decay-0.598.051.06Bernstein JA, et al. (2004)Gene Profile
1.5' RNA Decay of WT (N3433) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Replicate B1RNA decay-0.408.770.86Bernstein JA, et al. (2004)Gene Profile
3' RNA Decay of WT (N3433) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log1RNA decay-1.988.922.58Bernstein JA, et al. (2004)Gene Profile
4.5' RNA Decay of WT (N3433) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log1RNA decay-1.278.701.25Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay of WT (N3433) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Replicate A1RNA decay-0.688.650.78Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay of WT (N3433) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Replicate B1RNA decay-1.568.511.54Bernstein JA, et al. (2004)Gene Profile
1.5' RNA Decay of RhlB- (SU02) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Replicate A1RNA decay-0.167.970.50Bernstein JA, et al. (2004)Gene Profile
1.5' RNA Decay of RhlB- (SU02) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Replicate B1RNA decay-0.309.730.58Bernstein JA, et al. (2004)Gene Profile
3' RNA Decay of RhlB- (SU02) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log1RNA decay-1.118.791.64Bernstein JA, et al. (2004)Gene Profile
4.5' RNA Decay of RhlB- (SU02) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log1RNA decay-3.197.732.96Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay of RhlB- (SU02) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Replicate A1RNA decay-0.568.510.67Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay of RhlB- (SU02) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Replicate B1RNA decay-0.568.510.70Bernstein JA, et al. (2004)Gene Profile
WT (N3433) vs RhlB- (SU02) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Trial A1Wild type vs Mutant-0.198.840.38Bernstein JA, et al. (2004) 
WT (N3433) vs RhlB- (SU02) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Trial B1Wild type vs Mutant-0.339.700.44Bernstein JA, et al. (2004) 
WT (N3433) vs RhlB- (SU02) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Trial C1Wild type vs Mutant-0.099.290.13Bernstein JA, et al. (2004) 
1.5' RNA Decay of WT (N3433) in M9 0.2% Glycerol 0.2% Tryptone at 30 C Mid Log Rep. A2RNA decay0.948.771.58Bernstein JA, et al. (2004)Gene Profile
1.5' RNA Decay of WT (N3433) in M9 0.2% Glycerol 0.2% Tryptone at 30 C Mid Log Rep. B2RNA decay0.267.940.63Bernstein JA, et al. (2004)Gene Profile
3' RNA Decay of WT (N3433) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log 2RNA decay-0.567.060.64Bernstein JA, et al. (2004)Gene Profile
4.5' RNA Decay of WT (N3433) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log 2RNA decay-0.847.270.85Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay of WT (N3433) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Rep A2RNA decay-0.397.990.38Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay of WT (N3433) in M9 + 0.2% Glycerol, .2% Tryptone at 30 C Mid Log Rep B2RNA decay0.438.300.48Bernstein JA, et al. (2004)Gene Profile
1.5' RNA Decay of Pnp- (YHC012) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Rep. A2RNA decay0.079.560.26Bernstein JA, et al. (2004)Gene Profile
1.5' RNA Decay of Pnp- (YHC012) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Rep. B2RNA decay-0.148.530.40Bernstein JA, et al. (2004)Gene Profile
3' RNA Decay of Pnp- (YHC012) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log 2RNA decay-0.398.010.64Bernstein JA, et al. (2004)Gene Profile
4.5' RNA Decay of Pnp- (YHC012) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log 2RNA decay-0.278.420.34Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay of Pnp- (YHC012) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Rep. A2RNA decay-0.129.030.13Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay of Pnp- (YHC012) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Rep. B2RNA decay-0.449.250.57Bernstein JA, et al. (2004)Gene Profile
WT (N3433) vs Pnp- (YHC012) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Trial A2Wild type vs Mutant0.377.410.71Bernstein JA, et al. (2004) 
WT (N3433) vs Pnp- (YHC012) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Trial B2Wild type vs Mutant0.888.761.00Bernstein JA, et al. (2004) 
WT (N3433) vs Pnp- (YHC012) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Trial C2Wild type vs Mutant0.868.920.80Bernstein JA, et al. (2004) 
1.5' RNA Decay N-RNaseE (BZ453) in M9 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Rep. ARNA decay0.079.390.27Bernstein JA, et al. (2004)Gene Profile
1.5' RNA Decay N-RNaseE (BZ453) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Rep. BRNA decay0.129.760.44Bernstein JA, et al. (2004)Gene Profile
3' RNA Decay N-RNaseE (BZ453) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log RNA decay-0.1910.470.38Bernstein JA, et al. (2004)Gene Profile
4.5' RNA Decay N-RNaseE (BZ453) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log RNA decay-0.218.590.35Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay N-RNaseE (BZ453) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Rep. ARNA decay-0.409.020.62Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay N-RNaseE (BZ453) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Rep. BRNA decay-0.369.510.56Bernstein JA, et al. (2004)Gene Profile
WT (SH3208) vs N-RNaseE (BZ453) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Trial AWild type vs Mutant0.318.970.24Bernstein JA, et al. (2004) 
WT (SH3208) vs N-RNaseE (BZ453) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Trial BWild type vs Mutant0.378.780.31Bernstein JA, et al. (2004) 
WT (SH3208) vs N-RNaseE (BZ453) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Trial CWild type vs Mutant0.238.980.04Bernstein JA, et al. (2004) 
1.5' RNA Decay of WT (SH3208) in M9 0.2% Glycerol 0.2% Tryptone at 30 C Mid Log Rep. A1RNA decay0.028.660.03Bernstein JA, et al. (2004)Gene Profile
1.5' RNA Decay of WT (SH3208) in M9 0.2% Glycerol 0.2% Tryptone at 30 C Mid Log Rep. B1RNA decay-0.238.620.57Bernstein JA, et al. (2004)Gene Profile
3' RNA Decay of WT (SH3208) in M9 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log 1RNA decay-1.168.221.51Bernstein JA, et al. (2004)Gene Profile
4.5' RNA Decay of WT (SH3208) in M9 0.2% Glycerol, .2% Tryptone at 30 C Mid Log 1RNA decay-2.027.782.19Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay of WT (SH3208) in M9 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Rep A1RNA decay-0.448.150.35Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay of WT (SH3208) in M9 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Rep B1RNA decay-0.378.310.30Bernstein JA, et al. (2004)Gene Profile
1.5' RNA Decay N-RNaseE (BZ453) in M9 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Rep. A1RNA decay0.069.770.23Bernstein JA, et al. (2004)Gene Profile
1.5' RNA Decay N-RNaseE (BZ453) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Rep. B1RNA decay0.049.060.18Bernstein JA, et al. (2004)Gene Profile
3' RNA Decay N-RNaseE (BZ453) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log 1RNA decay0.088.950.32Bernstein JA, et al. (2004)Gene Profile
4.5' RNA Decay N-RNaseE (BZ453) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log 1RNA decay-0.0910.790.09Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay N-RNaseE (BZ453) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Rep. A1RNA decay-0.319.800.50Bernstein JA, et al. (2004)Gene Profile
6' RNA Decay N-RNaseE (BZ453) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Rep. B1RNA decay-0.489.681.17Bernstein JA, et al. (2004)Gene Profile
WT (SH3208) vs N-RNaseE (BZ453) in M9 + 0.2% Glycerol, 0.2% Tryptone at 30 C Mid Log Wild type vs Mutant0.388.540.26Bernstein JA, et al. (2004) 
WT (K10) vs Eno- (DF261) M9 + 0.2% Glycerol, 0.2% Tryptone, 40 mM Suc. at 30 C Mid Log Trial A1Wild type vs Mutant0.439.930.53Bernstein JA, et al. (2004) 
WT (K10) vs Eno- (DF261) M9 + 0.2% Glycerol, 0.2% Tryptone, 40 mM Suc. at 30 C Mid Log Trial B1Wild type vs Mutant0.519.050.64Bernstein JA, et al. (2004) 
Transcript Abundance in M9 at 30 degrees OD600=0.8 Trial AMinimal media-2.159.461.33Bernstein JA, et al. (2002) 
Transcript Abundance in M9 at 30 degrees OD600=0.8 Trial BMinimal media-2.279.621.65Bernstein JA, et al. (2002) 
Transcript Abundance in LB at 30 degrees OD600=0.8 Trial AMinimal media-2.0210.151.24Bernstein JA, et al. (2002) 
Transcript Abundance in LB at 30 degrees OD600=0.8 Trial BMinimal media-2.629.700.87Bernstein JA, et al. (2002) 
KSL2009-RraA overexpressionOverexpression-0.689.860.98Lee K, et al. (2003)Gene Profile
KSL2000-Rne depletionRNase E depletion0.3610.570.20Lee K, et al. (2003)Gene Profile
KSL2009-N-Rne depletionN-RNase E depletion0.5611.270.27Lee K, et al. (2003)Gene Profile
KSL2000-RraA overexpressionOverexpression0.099.860.13Lee K, et al. (2003)Gene Profile
rraA deletion, OD600=0.3Wild type vs Mutant-0.1912.490.46Unpublished Experiment Set: 2257 
rraA deletion, OD600=0.5Wild type vs Mutant-0.2811.840.53Unpublished Experiment Set: 2257 
rraA deletion, OD600=1.0Wild type vs Mutant0.3612.300.62Unpublished Experiment Set: 2257 
ecd3-c-0081429 wt vs dpiAoverexpressorOverexpression-0.1612.030.38Miller C, et al. (2003) 
ecd3-c-0101429 wt vs dpiAoverexpressorOverexpression-0.0511.520.16Miller C, et al. (2003) 
BW25113 planktonic cells at 30CBiofilm + Planktonic0.0110.910.26Lee J, et al. (2008)Gene Profile
BW25113 sdiA(del) planktonic cells at 30C, no indoleBiofilm + Planktonic-0.1710.820.27Lee J, et al. (2008)Gene Profile
BW25113 luxS(del) planktonic cells at 30C, no AI-2Autoinducer-2 + Mutant - control-0.1510.830.29Lee J, et al. (2008)Gene Profile
BW25113 luxS(del) planktonic cells at 30C, 3 h after add'n of 100 uM AI-2Autoinducer-2 + Mutant-0.0310.890.02Lee J, et al. (2008)Gene Profile
BW25113 luxS(del) planktonic cells at 37C, 3 h after add'n of 100 uM AI-2Autoinducer-2 + Mutant-0.0510.880.03Lee J, et al. (2008)Gene Profile
BW25113 luxS(del) planktonic cells at 37C, no AI-2Autoinducer-2 + Mutant - control0.2011.000.68Lee J, et al. (2008)Gene Profile
BW25113 tnaA(del) 7-h biofilm cells at 37C, mock treatment with DMFBiofilm + Mock treatment-0.0310.890.20Lee J, et al. (2008)Gene Profile
BW25113 tnaA(del) 7-h biofilm cells at 37C with 1 mM indoleBiofilm + Indole0.1710.990.55Lee J, et al. (2008)Gene Profile
BW25113 sdiA(del) 7-h biofilm cells at 30C with 1 mM indoleBiofilm + Indole-0.0610.880.02Lee J, et al. (2008)Gene Profile
BW25113 sdiA(del) 7-h biofilm cells at 30C, mock treatment with DMFBiofilm + Mock treatment0.0710.940.16Lee J, et al. (2008)Gene Profile
K-12 MG1655 + untreated, 5 min, rep. 3Cefsulodin, Mecillinam - control0.269.090.45Laubacher ME and Ades SE (2008)Gene Profile
K-12 MG1655 + untreated, 10 min, rep. 1Cefsulodin, Mecillinam - control0.149.030.65Laubacher ME and Ades SE (2008)Gene Profile
K-12 MG1655 + untreated, 10 min, rep. 2Cefsulodin, Mecillinam - control0.369.140.84Laubacher ME and Ades SE (2008)Gene Profile
K-12 MG1655 + untreated, 10 min, rep. 3Cefsulodin, Mecillinam - control-0.038.940.17Laubacher ME and Ades SE (2008)Gene Profile
K-12 MG1655 + untreated, 60 min, rep. 1Cefsulodin, Mecillinam - control-0.448.740.58Laubacher ME and Ades SE (2008)Gene Profile
K-12 MG1655 + untreated, 60 min, rep. 2Cefsulodin, Mecillinam - control-0.398.760.86Laubacher ME and Ades SE (2008)Gene Profile
K-12 MG1655 + untreated, 60min, rep. 3Cefsulodin, Mecillinam - control-0.328.800.77Laubacher ME and Ades SE (2008)Gene Profile
K-12 MG1655 + untreated, 40 min, rep. 4_2Cefsulodin, Mecillinam - control-0.368.780.46Laubacher ME and Ades SE (2008)Gene Profile
K-12 MG1655 + Cefsulodin, 5 min, rep. 1Cefsulodin0.339.120.85Laubacher ME and Ades SE (2008)Gene Profile
K-12 MG1655 + Cefsulodin, 5 min, rep. 2Cefsulodin0.279.090.62Laubacher ME and Ades SE (2008)Gene Profile
K-12 MG1655 + Cefsulodin, 20 min, rep. 1Cefsulodin0.269.090.45Laubacher ME and Ades SE (2008)Gene Profile
K-12 MG1655 + Cefsulodin, 10 min, rep. 1Cefsulodin0.028.970.27Laubacher ME and Ades SE (2008)Gene Profile
K-12 MG1655 + Cefsulodin, 10 min, rep. 2Cefsulodin0.048.980.00Laubacher ME and Ades SE (2008)Gene Profile
K-12 MG1655 + Cefsulodin, 10 min, rep. 3Cefsulodin0.199.050.42Laubacher ME and Ades SE (2008)Gene Profile
K-12 MG1655 + Mecillinam, 60 min, rep. 1Mecillinam-0.028.950.11Laubacher ME and Ades SE (2008)Gene Profile
K-12 MG1655 + Mecillinam, 60 min, rep. 2Mecillinam0.099.000.32Laubacher ME and Ades SE (2008)Gene Profile
K-12 MG1655 + Mecillinam, 60 min, rep. 3Mecillinam-0.138.890.23Laubacher ME and Ades SE (2008)Gene Profile
K-12 MG1655 + Cefsulodin + Mecillinam, 40 min, rep. 4_2Cefsulodin + Mecillinam-0.938.491.19Laubacher ME and Ades SE (2008)Gene Profile
K-12 MG1655 araBAD(del) leu+, rep. 1Wild type vs Mutant-0.008.760.26Moon K and Gottesman S (2009)Gene Profile
K-12 MG1655 araBAD(del) leu+, rep. 2Wild type vs Mutant0.208.860.44Moon K and Gottesman S (2009)Gene Profile
K-12 MG1655 araBAD(del) leu+ mgrR(del)::FRT-kan-FRT, rep. 1Mutant-0.088.720.01Moon K and Gottesman S (2009)Gene Profile
K-12 MG1655 araBAD(del) leu+ mgrR(del)::FRT-kan-FRT, rep. 2Mutant0.178.850.55Moon K and Gottesman S (2009)Gene Profile
K-12 KM100 mgrR(del)::FRT-kan-FRT + empty vector, rep. 1Overexpression - control-0.068.730.07Moon K and Gottesman S (2009)Gene Profile
K-12 KM100 mgrR(del)::FRT-kan-FRT + empty vector, rep. 2Overexpression - control-0.058.730.09Moon K and Gottesman S (2009)Gene Profile
K-12 KM100 mgrR(del)::FRT-kan-FRT + plasmid-borne mgrR, rep. 1Overexpression-0.088.720.11Moon K and Gottesman S (2009)Gene Profile
K-12 KM100 mgrR(del)::FRT-kan-FRT + plasmid-borne mgrR, rep. 2Overexpression-0.128.700.12Moon K and Gottesman S (2009)Gene Profile
Biofilm_Inside_rep1Biofilm0.2810.050.81Ito A, et al. (2009)Gene Profile
Biofilm_Inside_rep2Biofilm0.2910.050.86Unpublished Experiment Set: 4767 
Biofilm_Inside_rep3Biofilm0.3410.080.90Unpublished Experiment Set: 4767 
Biofilm_Outside_rep1Biofilm-0.149.840.01Unpublished Experiment Set: 4767 
Biofilm_Outside_rep2Biofilm0.059.930.40Unpublished Experiment Set: 4767 
Biofilm_Outside_rep3Biofilm0.159.980.63Ito A, et al. (2009)Gene Profile
Planktonic_Exponential_rep1Biofilm + Planktonic0.4710.140.86Unpublished Experiment Set: 4767 
Planktonic_Exponential_rep2Biofilm + Planktonic0.4010.110.74Unpublished Experiment Set: 4767 
Planktonic_Exponential_rep3Biofilm + Planktonic0.3210.070.65Unpublished Experiment Set: 4767 
Planktonic_Stationary_rep1Biofilm + Planktonic-1.709.061.50Unpublished Experiment Set: 4767 
Planktonic_Stationary_rep2Biofilm + Planktonic-1.439.191.21Unpublished Experiment Set: 4767 
Planktonic_Stationary_rep3Biofilm + Planktonic-0.729.540.51Ito A, et al. (2009)Gene Profile
K-12 W3110, 15 min before oxygen downshiftAerobic growth0.0910.770.16Soini J, et al. (2008)Gene Profile
K-12 W3110, 15 min after oxygen downshiftAnaerobic growth0.2210.830.46Soini J, et al. (2008)Gene Profile
K-12 W3110, 45 min after oxygen downshiftAnaerobic growth-0.1110.670.43Soini J, et al. (2008)Gene Profile
K-12 W3110, 75 min after oxygen downshiftAnaerobic growth-0.2510.600.62Soini J, et al. (2008)Gene Profile
P4X (wild-type argR) (1753) ReferenceArginine + Parental strain - Control-0.018.210.09Caldara M, et al. (2006)Gene Profile
P4X (wild-type argR) (1765) ReferenceArginine + Parental strain - Control0.208.321.22Caldara M, et al. (2006)Gene Profile
P4X (wild-type argR) (1989) ReferenceArginine + Parental strain - Control0.118.270.76Caldara M, et al. (2006)Gene Profile
P4X (wild-type argR) (1754) in ArginineArginine + Parental strain-0.018.210.47Caldara M, et al. (2006)Gene Profile
P4X (wild-type argR) (1766) in ArginineArginine + Parental strain0.148.290.63Caldara M, et al. (2006)Gene Profile
P4X (wild-type argR) (1990) in ArginineArginine + Parental strain-0.238.100.85Caldara M, et al. (2006)Gene Profile
P4XB2 (argR mutant) (1992) in ArginineArginine + Mutant-0.138.150.11Caldara M, et al. (2006)Gene Profile
P4XB2 (argR mutant) (1993) in ArginineArginine + Mutant-0.018.210.18Caldara M, et al. (2006)Gene Profile
P4XB2 (argR mutant) (1994) in ArginineArginine + Mutant-0.118.160.33Caldara M, et al. (2006)Gene Profile
E. coli K-12 BW25113 sdiA(del) + multicopy sdiA+ biofilm cells at 30COverexpression0.2511.430.65Lee J, et al. (2009)Gene Profile
E. coli K-12 BW25113 sdiA(del) + multicopy sdiA1E11 biofilm cells at 30COverexpression-0.0411.280.07Lee J, et al. (2009)Gene Profile
E. coli K-12 BW25113 sdiA(del) + empty vector biofilm cells at 30COverexpression - control-0.2511.180.69Lee J, et al. (2009)Gene Profile
E. coli K-12 MG1655 no drug, rep. 1Bicyclomycin - control-0.079.680.23Cardinale CJ, et al. (2008) 
E. coli K-12 MG1655 no drug, rep. 2Bicyclomycin - control0.259.840.43Cardinale CJ, et al. (2008) 
E. coli K-12 MG1655 + bicyclomycin 10 mcg/ml, rep. 1Bicyclomycin0.099.760.26Cardinale CJ, et al. (2008) 
E. coli K-12 MG1655 + bicyclomycin 10 mcg/ml, rep. 2Bicyclomycin-0.059.690.10Cardinale CJ, et al. (2008) 
E. coli K-12 MG1655 + bicyclomycin 25 mcg/ml, rep. 1Bicyclomycin0.059.740.26Cardinale CJ, et al. (2008) 
E. coli K-12 MG1655 + bicyclomycin 25 mcg/ml, rep. 2Bicyclomycin-0.159.640.01Cardinale CJ, et al. (2008) 
E. coli K-12 MG1655 + bicyclomycin 100 mcg/ml, rep. 1Bicyclomycin-0.559.440.28Cardinale CJ, et al. (2008) 
E. coli K-12 MG1655 + bicyclomycin 100 mcg/ml, rep. 2Bicyclomycin-0.539.450.43Cardinale CJ, et al. (2008) 
E. coli K-12 MDS42 no drug, rep. 1Bicyclomycin - control0.189.800.21Cardinale CJ, et al. (2008) 
E. coli K-12 MDS42 no drug, rep. 2Bicyclomycin - control0.199.810.22Cardinale CJ, et al. (2008) 
E. coli K-12 MDS42 + bicyclomycin 100 mcg/ml, rep. 1Bicyclomycin-0.529.460.61Cardinale CJ, et al. (2008) 
E. coli K-12 MDS42 + bicyclomycin 100 mcg/ml, rep. 2Bicyclomycin-0.449.500.55Cardinale CJ, et al. (2008) 
E. coli K-12 MDS42 nusA(del), rep. 1Mutant-0.099.670.10Cardinale CJ, et al. (2008) 
E. coli K-12 MDS42 nusA(del), rep. 2Mutant0.8510.141.05Cardinale CJ, et al. (2008) 
E. coli K-12 MDS42 nusG(del), rep. 1Mutant-0.069.680.05Cardinale CJ, et al. (2008) 
E. coli K-12 MDS42 nusG(del), rep. 2Mutant0.169.790.23Cardinale CJ, et al. (2008) 
E. coli K-12 W3110 in minimal glucose medium, rep1Wild type vs Mutant-0.187.260.41Li Y and Zhang Y (2007)Gene Profile
E. coli K-12 W3110 in minimal glucose medium, rep. 2Wild type vs Mutant0.007.360.04Li Y and Zhang Y (2007)Gene Profile
E. coli K-12 W3110 in minimal glucose medium, rep. 3Wild type vs Mutant0.177.440.56Li Y and Zhang Y (2007)Gene Profile
E. coli K-12 W3110 phoU::miniTn10Kan, rep. 1Mutant-0.057.330.08Li Y and Zhang Y (2007)Gene Profile
K-12 M1655 soxR(del) no paraquat, t=0 min, rep. 1Paraquat - control-0.199.350.09Blanchard JL, et al. (2007)Gene Profile
E. coli K-12 W3110 phoU::miniTn10Kan, rep. 2Mutant-0.057.330.10Li Y and Zhang Y (2007)Gene Profile
K-12 M1655 soxR(del) + paraquat t=2 min, rep. 1Paraquat-0.189.360.12Blanchard JL, et al. (2007)Gene Profile
E. coli K-12 W3110 phoU::miniTn10Kan, rep. 3Mutant0.097.400.49Li Y and Zhang Y (2007)Gene Profile
K-12 M1655 soxR(del) + paraquat, t=4 min, rep. 1Paraquat-0.209.340.40Blanchard JL, et al. (2007)Gene Profile
K-12 M1655 soxR(del) + paraquat, t=6 min, rep. 1Paraquat-0.209.340.28Blanchard JL, et al. (2007)Gene Profile
K-12 M1655 soxR(del) + paraquat, t=8 min, rep. 1Paraquat-0.249.330.28Blanchard JL, et al. (2007)Gene Profile
K-12 M1655 soxR(del) + paraquat, t=10 min, rep. 1Paraquat-0.269.310.32Blanchard JL, et al. (2007)Gene Profile
wild type rpoD, 0 g/L EtOH, replicate 1Ethanol - control-0.018.920.37Alper H and Stephanopoulos G (2007)Gene Profile
K-12 M1655 no paraquat, t=0 min, rep. 1Paraquat - control0.309.590.60Blanchard JL, et al. (2007)Gene Profile
wild type rpoD, 0 g/L EtOH, replicate 2Ethanol - control0.138.990.96Alper H and Stephanopoulos G (2007)Gene Profile
K-12 M1655 + paraquat, t=2 min, rep. 1Paraquat0.549.710.86Blanchard JL, et al. (2007)Gene Profile
wild type rpoD, 0 g/L EtOH, replicate 3Ethanol - control-0.098.880.39Alper H and Stephanopoulos G (2007)Gene Profile
K-12 M1655 + paraquat, t=4 min, rep. 1Paraquat0.299.590.53Blanchard JL, et al. (2007)Gene Profile
mutant rpoD from round 1, 0 g/L EtOH, replicate 1Ethanol - control-0.248.801.40Alper H and Stephanopoulos G (2007)Gene Profile
K-12 M1655 + paraquat, t=6 min, rep. 1Paraquat0.319.600.74Blanchard JL, et al. (2007)Gene Profile
mutant rpoD from round 1, 0 g/L EtOH, replicate 2Ethanol - control0.078.950.42Alper H and Stephanopoulos G (2007)Gene Profile
K-12 M1655 + paraquat, t=8min, rep. 1Paraquat0.189.530.46Blanchard JL, et al. (2007)Gene Profile
mutant rpoD from round 1, 0 g/L EtOH, replicate 3Ethanol - control0.118.980.77Alper H and Stephanopoulos G (2007)Gene Profile
K-12 M1655 + paraquat, t=10 min, rep. 1Paraquat0.239.560.42Blanchard JL, et al. (2007)Gene Profile
mutant rpoD from round 2, 0 g/L EtOH, replicate 1Ethanol - control0.048.940.24Alper H and Stephanopoulos G (2007)Gene Profile
K-12 M1655 no paraquat, t=0 min, rep. 2Paraquat - control0.139.510.34Blanchard JL, et al. (2007)Gene Profile
mutant rpoD from round 2, 0 g/L EtOH, replicate 2Ethanol - control-0.018.910.23Alper H and Stephanopoulos G (2007)Gene Profile
K-12 M1655 + paraquat, t=2 min, rep. 2Paraquat-0.319.290.40Blanchard JL, et al. (2007)Gene Profile
mutant rpoD from round 2, 0 g/L EtOH, replicate 3Ethanol - control-0.008.920.18Alper H and Stephanopoulos G (2007)Gene Profile
K-12 M1655 + paraquat, t=4 min, rep. 2Paraquat-0.189.360.15Blanchard JL, et al. (2007)Gene Profile
mutant rpoD from round 3, 0 g/L EtOH, replicate 1Ethanol - control-0.048.900.02Alper H and Stephanopoulos G (2007)Gene Profile
K-12 M1655 + paraquat, t=6 min, rep. 2Paraquat-0.289.300.32Blanchard JL, et al. (2007)Gene Profile
mutant rpoD from round 3, 0 g/L EtOH, replicate 2Ethanol - control-0.018.920.46Alper H and Stephanopoulos G (2007)Gene Profile
K-12 M1655 + paraquat, t=8 min, rep. 2Paraquat-0.179.360.16Blanchard JL, et al. (2007)Gene Profile
mutant rpoD from round 3, 20 g/L EtOH, replicate 1Ethanol-0.098.880.45Alper H and Stephanopoulos G (2007)Gene Profile
K-12 M1655 + paraquat, t=10 min, rep. 2Paraquat-0.219.340.20Blanchard JL, et al. (2007)Gene Profile
mutant rpoD from round 3, 20 g/L EtOH, replicate 2Ethanol0.148.990.29Alper H and Stephanopoulos G (2007)Gene Profile
mutant rpoD from round 3, 20 g/L EtOH, replicate 3Ethanol0.018.930.31Alper H and Stephanopoulos G (2007)Gene Profile
mutant rpoD from round 3, 40 g/L EtOH, replicate 1Ethanol-0.288.781.45Alper H and Stephanopoulos G (2007)Gene Profile
mutant rpoD from round 3, 40 g/L EtOH, replicate 2Ethanol0.048.940.33Alper H and Stephanopoulos G (2007)Gene Profile
mutant rpoD from round 3, 40 g/L EtOH, replicate 3Ethanol-0.108.870.58Alper H and Stephanopoulos G (2007)Gene Profile
BW25113/pCA24N LB 2 mM IPTG suspension cellsOverexpression - control-0.3910.831.56Garcia-Contreras R, et al. (2008)Gene Profile
wild type rpoD, 20 g/L EtOH, replicate 1Ethanol0.138.980.47Alper H and Stephanopoulos G (2007)Gene Profile
BW25113/pCA24N-hha LB 2 mM IPTG suspension cellsOverexpression0.3111.181.23Garcia-Contreras R, et al. (2008)Gene Profile
wild type rpoD, 20 g/L EtOH, replicate 2Ethanol-0.028.910.42Alper H and Stephanopoulos G (2007)Gene Profile
wild type rpoD, 20 g/L EtOH, replicate 3Ethanol0.138.980.37Alper H and Stephanopoulos G (2007)Gene Profile
K-12 MG1655 (is yncC+) - cells from colonyBiofilm-0.0310.790.12Zhang XS, et al. (2008)Gene Profile
E. coli K-12 MG1655, biofilm 15 hrBiofilm + Parental strain-0.0610.710.38Kim Y, et al. (2009)Gene Profile
K-12 MG1655 yncC(del) - cells from colonyBiofilm0.0310.830.60Zhang XS, et al. (2008)Gene Profile
E. coli K-12 BW25113, biofilm 8 hrBiofilm + Parental strain0.0210.750.27Kim Y, et al. (2009)Gene Profile
E. coli K-12 MG1655 with 5 toxin-antitoxin loci deleted (LVM100), biofilm 15 hrBiofilm-0.0510.720.28Kim Y, et al. (2009)Gene Profile
E. coli K-12 BW25113 yjgK(del), biofilm 8 hrBiofilm + Mutant0.0910.790.58Kim Y, et al. (2009)Gene Profile
E. coli K-12 str. Frag1 no treatment, biological rep. 2Hyperosmotic - control-0.906.101.01Shabala L, et al. (2009) 
E. coli K-12 str. ATCC 25404 biofilm cells + mock treatment, rep. 1Biofilm + Mock treatment0.1311.870.58Unpublished Experiment Set: 4732 
E. coli K-12 str. ATCC 25404 biofilm cells + 5-fluorouracil, rep. 1Biofilm + 5-fluorouracil0.0811.840.50Attila C, et al. (2009)Gene Profile
E. coli K-12 str. ATCC 25404 biofilm cells + mock treatment, rep. 2Biofilm + Mock treatment-0.0911.760.42Attila C, et al. (2009)Gene Profile
E. coli K-12 str. Frag1 + ionic (NaCl) hyperosmotic treatment, biological rep. 1Hyperosmotic0.376.730.51Shabala L, et al. (2009) 
E. coli K-12 str. ATCC 25404 biofilm cells + 5-flurouracil, rep. 2Biofilm + 5-fluorouracil-0.1411.730.75Unpublished Experiment Set: 4730 
E. coli K-12 str. Frag1 + ionic (NaCl) hyperosmotic treatment, biological rep. 2Hyperosmotic0.236.660.61Shabala L, et al. (2009) 
E. coli K-12 MG1655 appY(del) Aerobic, rep. 1Aerobic growth + Mutant-0.029.170.23Covert MW, et al. (2004)Gene Profile
E. coli K-12 MG1655 appY(del) Aerobic, rep. 2Aerobic growth + Mutant-0.029.170.29Covert MW, et al. (2004)Gene Profile
E. coli K-12 MG1655 appY(del) Aerobic, rep. 3Aerobic growth + Mutant0.089.230.43Covert MW, et al. (2004)Gene Profile
E. coli K-12 arcA(del) Aerobic growth, rep. 1Aerobic growth + Mutant-0.049.170.15Covert MW, et al. (2004)Gene Profile
E. coli K-12 arcA(del) Aerobic growth, rep. 2Aerobic growth + Mutant0.119.240.64Covert MW, et al. (2004)Gene Profile
E. coli K-12 arcA(del) Aerobic growth, rep. 3Aerobic growth + Mutant-0.009.180.25Covert MW, et al. (2004)Gene Profile
E. coli K-12 arcAfnr(del) Aerobic growth, rep. 1Aerobic growth + Mutant-0.029.170.04Covert MW, et al. (2004)Gene Profile
E. coli K-12 arcAfnr(del) Aerobic growth, rep. 2Aerobic growth + Mutant0.179.270.62Covert MW, et al. (2004)Gene Profile
E. coli K-12 arcAfnr(del) Aerobic growth, rep. 3Aerobic growth + Mutant0.199.280.80Covert MW, et al. (2004)Gene Profile
E. coli K-12 fnr(del) Aerobic growth, rep. 1Aerobic growth + Mutant-0.049.160.08Covert MW, et al. (2004)Gene Profile
E. coli K-12 fnr(del) Aerobic growth, rep. 2Aerobic growth + Mutant-0.129.130.28Covert MW, et al. (2004)Gene Profile
E. coli K-12 fnr(del) Aerobic growth, rep. 3Aerobic growth + Mutant-0.169.100.20Covert MW, et al. (2004)Gene Profile
E. coli K-12 oxyR(del) Aerobic growth, rep. 1Aerobic growth + Mutant0.109.240.57Covert MW, et al. (2004)Gene Profile
E. coli K-12 oxyR(del) Aerobic growth, rep. 2Aerobic growth + Mutant-0.059.160.15Covert MW, et al. (2004)Gene Profile
E. coli K-12 oxyR(del) Aerobic growth, rep. 3Aerobic growth + Mutant-0.339.020.75Covert MW, et al. (2004)Gene Profile
E. coli K-12 soxS(del) Aerobic growth, rep. 1Aerobic growth + Mutant0.139.250.72Covert MW, et al. (2004)Gene Profile
E. coli K-12 soxS(del) Aerobic growth, rep. 2Aerobic growth + Mutant0.209.291.07Covert MW, et al. (2004)Gene Profile
E. coli K-12 soxS(del) Aerobic growth, rep. 3Aerobic growth + Mutant-0.009.180.36Covert MW, et al. (2004)Gene Profile
E. coli K-12 MG1655 Aerobic, rep. 1Aerobic growth + Parental strain-0.079.150.10Covert MW, et al. (2004)Gene Profile
E. coli K-12 MG1655 Aerobic, rep. 2Aerobic growth + Parental strain0.019.190.05Covert MW, et al. (2004)Gene Profile
E. coli K-12 MG1655 Aerobic, rep. 3Aerobic growth + Parental strain-0.548.911.36Covert MW, et al. (2004)Gene Profile
E. coli K-12 MG1655 appY(del) Anaerobic, rep. 1Anaerobic growth + Mutant0.099.230.46Covert MW, et al. (2004)Gene Profile
E. coli K-12 MG1655 appY(del) Anaerobic, rep. 2Anaerobic growth + Mutant0.219.290.72Unpublished Experiment Set: 4757 
E. coli K-12 MG1655 appY(del) Anaerobic, rep. 3Anaerobic growth + Mutant0.259.310.83Covert MW, et al. (2004)Gene Profile
E. coli K-12 arcA(del) Anaerobic growth, rep. 1Anaerobic growth + Mutant0.009.180.06Unpublished Experiment Set: 4757 
E. coli K-12 arcA(del) Anaerobic growth, rep. 2Anaerobic growth + Mutant-0.089.140.13Unpublished Experiment Set: 4757 
E. coli K-12 arcA(del) Anaerobic growth, rep. 3Anaerobic growth + Mutant0.099.230.32Covert MW, et al. (2004)Gene Profile
E. coli K-12 arcAfnr(del) Anaerobic growth, rep. 1Anaerobic growth + Mutant0.299.330.89Covert MW, et al. (2004)Gene Profile
E. coli K-12 arcAfnr(del) Anaerobic growth, rep. 2Anaerobic growth + Mutant-0.079.150.08Covert MW, et al. (2004)Gene Profile
E. coli K-12 arcAfnr(del) Anaerobic growth, rep. 3Anaerobic growth + Mutant-0.189.090.26Covert MW, et al. (2004)Gene Profile
E. coli K-12 fnr(del) Anaerobic growth, rep. 1Anaerobic growth + Mutant-0.329.030.61Covert MW, et al. (2004)Gene Profile
E. coli K-12 fnr(del) Anaerobic growth, rep. 2Anaerobic growth + Mutant-0.309.030.58Unpublished Experiment Set: 4757 
E. coli K-12 fnr(del) Anaerobic growth, rep. 3Anaerobic growth + Mutant-0.289.050.50Covert MW, et al. (2004)Gene Profile
E. coli K-12 oxyR(del) Anaerobic growth, rep. 1Anaerobic growth + Mutant0.089.220.31Covert MW, et al. (2004)Gene Profile
E. coli K-12 oxyR(del) Anaerobic growth, rep. 2Anaerobic growth + Mutant-0.019.180.09Unpublished Experiment Set: 4757 
E. coli K-12 oxyR(del) Anaerobic growth, rep. 3Anaerobic growth + Mutant-0.129.120.12Covert MW, et al. (2004)Gene Profile
E. coli K-12 soxS(del) Anaerobic growth, rep. 1Anaerobic growth + Mutant0.009.190.14Unpublished Experiment Set: 4757 
E. coli K-12 soxS(del) Anaerobic growth, rep. 2Anaerobic growth + Mutant-0.069.150.05Unpublished Experiment Set: 4757 
E. coli K-12 soxS(del) Anaerobic growth, rep. 3Anaerobic growth + Mutant-0.009.180.03Covert MW, et al. (2004)Gene Profile
E. coli K-12 MG1655 Anaerobic, rep. 1Anaerobic growth + Parental strain0.249.300.70Covert MW, et al. (2004)Gene Profile
E. coli K-12 MG1655 Anaerobic, rep. 2Anaerobic growth + Parental strain0.259.310.64Covert MW, et al. (2004)Gene Profile
E. coli K-12 MG1655 Anaerobic, rep. 3Anaerobic growth + Parental strain0.129.240.33Unpublished Experiment Set: 4757 
E. coli K-12 MG1655 Anaerobic, rep. 4Anaerobic growth + Parental strain-0.199.090.35Unpublished Experiment Set: 4757 
K-12 W3110, pH 7.6, 0 min, rep. 1Alkaline medium-0.088.940.01Unpublished Experiment Set: 4721 
K-12 W3110, pH 7.6, 0 min, rep. 2Alkaline medium-0.048.960.05Kannan G, et al. (2008)Gene Profile
K-12 W3110, pH 7.6, 0 min, rep. 3Alkaline medium0.028.990.03Unpublished Experiment Set: 4721 
E. coli K-12 MG1655 in gnotobiotic mouse, cecum sample 1Cecum0.126.970.47Reigstad CS, et al. (2007)Gene Profile
K-12 W3110, pH 7.6, 0 min, rep. 4Alkaline medium-0.128.920.47Kannan G, et al. (2008)Gene Profile
E. coli K-12 MG1655 in gnotobiotic mouse, cecum sample 2Cecum-0.106.860.10Reigstad CS, et al. (2007)Gene Profile
K-12 W3110, pH 7.6, 0 min, rep. 5Alkaline medium-0.088.940.14Kannan G, et al. (2008)Gene Profile
K-12 W3110, pH 5.5, 1 min, rep. 1Acidic medium-0.148.910.47Unpublished Experiment Set: 4721 
E. coli K-12 MG1655 in gnotobiotic mouse, cecum sample 4Cecum-0.116.860.07Reigstad CS, et al. (2007)Gene Profile
K-12 W3110, pH 5.5, 1 min, rep. 2Acidic medium-0.048.960.25Kannan G, et al. (2008)Gene Profile
E. coli K-12 MG1655 in gnotobiotic mouse, cecum sample 5Cecum0.497.161.32Reigstad CS, et al. (2007)Gene Profile
K-12 W3110, pH 5.5, 1 min, rep. 3Acidic medium-0.178.890.55Unpublished Experiment Set: 4721 
E. coli UTI89 in gnotobiotic mouse, cecum sample 1Cecum-0.266.790.19Reigstad CS, et al. (2007)Gene Profile
K-12 W3110, pH 5.5, 1 min, rep. 4Acidic medium-0.438.760.55Kannan G, et al. (2008)Gene Profile
E. coli UTI89 in gnotobiotic mouse, cecum sample 2Cecum0.257.040.86Reigstad CS, et al. (2007)Gene Profile
K-12 W3110, pH 5.5, 1 min, rep. 5Acidic medium-0.158.900.29Kannan G, et al. (2008)Gene Profile
E. coli UTI89 in gnotobiotic mouse, cecum sample 3Cecum0.217.020.88Reigstad CS, et al. (2007)Gene Profile
K-12 W3110, pH 5.5, 5 min, rep. 1Acidic medium0.209.070.69Kannan G, et al. (2008)Gene Profile
E. coli UTI89 in gnotobiotic mouse, cecum sample 4Cecum0.467.141.15Reigstad CS, et al. (2007)Gene Profile
K-12 W3110, pH 5.5, 5 min, rep. 2Acidic medium0.079.010.55Unpublished Experiment Set: 4721 
E. coli UTI89 in gnotobiotic mouse, cecum sample 5Cecum0.267.050.95Reigstad CS, et al. (2007)Gene Profile
K-12 W3110, pH 5.5, 5 min, rep. 3Acidic medium-0.028.970.32Unpublished Experiment Set: 4721 
K-12 W3110, pH 5.5, 5 min, rep. 4Acidic medium0.129.040.43Kannan G, et al. (2008)Gene Profile
K-12 W3110, pH 5.5, 5 min, rep. 5Acidic medium0.309.130.90Kannan G, et al. (2008)Gene Profile
K-12 W3110, pH 5.5, 10 min, rep. 1Acidic medium0.109.030.56Kannan G, et al. (2008)Gene Profile
K-12 W3110, pH 5.5, 10 min, rep. 2Acidic medium0.149.050.40Kannan G, et al. (2008)Gene Profile
K-12 W3110, pH 5.5, 10 min, rep. 3Acidic medium0.109.030.32Unpublished Experiment Set: 4721 
K-12 W3110, pH 5.5, 10 min, rep. 4Acidic medium0.089.020.23Unpublished Experiment Set: 4721 
K-12 W3110, pH 5.5, 10 min, rep. 5Acidic medium-0.038.960.09Unpublished Experiment Set: 4721 
K-12 W3110 luxS(del), LB medium OD 2.4, rep. 1Stationary phase-0.079.090.08Wang L, et al. (2005)Gene Profile
K-12 W3110, LB medium OD 2.4, rep. 1Stationary phase0.059.150.44Wang L, et al. (2005)Gene Profile
K-12 W3110, LB medium OD 2.4, rep. 2Stationary phase-0.029.110.23Wang L, et al. (2005)Gene Profile
K-12 W3110 luxS(del), LB medium OD 2.4, rep. 2Stationary phase0.049.150.16Wang L, et al. (2005)Gene Profile
E. coli K-12 MG1655 rpoS(del)::FRT, Biofilm rep. 1Biofilm0.146.790.55Ito A, et al. (2008)Gene Profile
E. coli K-12 MG1655, LB, Exponential Phase, rep. 1Exponential phase0.1110.540.73Dong T, et al. (2008)Gene Profile
E. coli K-12 MG1655 rpoS(del)::FRT, Biofilm rep. 2Biofilm-0.436.510.39Ito A, et al. (2008)Gene Profile
E. coli K-12 MG1655, LB, Exponential Phase, rep. 2Exponential phase0.0410.510.62Dong T, et al. (2008)Gene Profile
E. coli K-12 MG1655 rpoS(del)::FRT, Biofilm rep. 3Biofilm-0.176.640.08Ito A, et al. (2008)Gene Profile
E. coli K-12 MG1655, LB, Exponential Phase, rep. 3Exponential phase0.0410.500.41Dong T, et al. (2008)Gene Profile
E. coli K-12 MG1655 rpoS(del)::FRT, LB, Exponential Phase, rep. 1Exponential phase-0.0210.480.44Dong T, et al. (2008)Gene Profile
E. coli K-12 MG1655, Biofilm rep. 2Biofilm0.326.880.97Ito A, et al. (2008)Gene Profile
E. coli K-12 MG1655 rpoS(del)::FRT, LB, Exponential Phase, rep. 2Exponential phase-0.1210.431.00Dong T, et al. (2008)Gene Profile
E. coli K-12 MG1655, Biofilm rep. 3Biofilm0.056.750.76Ito A, et al. (2008)Gene Profile
E. coli K-12 MG1655 rpoS(del)::FRT, LB, Exponential Phase, rep. 3Exponential phase-0.0610.460.51Dong T, et al. (2008)Gene Profile
E. coli K-12 MG1655 rpoS(del)::FRT, Planktonic Exponential, rep. 1Biofilm + Planktonic-0.106.670.25Ito A, et al. (2008)Gene Profile
E. coli K-12 MG1655 rpoS(del)::FRT, Planktonic Exponential, rep. 2Biofilm + Planktonic-0.116.670.15Ito A, et al. (2008)Gene Profile
E. coli K-12 MG1655 rpoS(del)::FRT, Planktonic Exponential, rep. 3Biofilm + Planktonic0.346.890.79Ito A, et al. (2008)Gene Profile
E. coli K-12 MG1655, Planktonic Exponential, rep. 1Biofilm + Planktonic0.086.760.39Ito A, et al. (2008)Gene Profile
E. coli K-12 MG1655, Planktonic Exponential, rep. 2Biofilm + Planktonic0.076.760.40Ito A, et al. (2008)Gene Profile
E. coli K-12 MG1655, Planktonic Exponential, rep. 3Biofilm + Planktonic-0.146.650.10Ito A, et al. (2008)Gene Profile
E. coli K-12 MG1655, Planktonic Stationary, rep. 1Biofilm + Planktonic-0.516.470.29Ito A, et al. (2008)Gene Profile
E. coli K-12 MG1655, Planktonic Stationary, rep. 2Biofilm + Planktonic-0.366.540.09Ito A, et al. (2008)Gene Profile
E. coli K-12 MG1655 rpoS(del)::FRT, Planktonic Stationary, rep. 1Biofilm + Planktonic0.066.750.40Ito A, et al. (2008)Gene Profile
E. coli K-12 MG1655 rpoS(del)::FRT, Planktonic Stationary, rep. 2Biofilm + Planktonic0.466.950.77Ito A, et al. (2008)Gene Profile
E. coli K-12 MG1655 rpoS(del)::FRT, Planktonic Stationary, rep. 3Biofilm + Planktonic-0.076.690.33Ito A, et al. (2008)Gene Profile
E. coli K-12 MG1655, Untreated (-5 min), rep. 1no treatment control-0.289.220.32Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655, Untreated (-5 min), rep. 2no treatment control0.209.460.32Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655, Untreated (-5 min), rep. 3no treatment control0.389.550.73Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655, Untreated (5 min), rep. 1no treatment control0.109.410.27Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655, Untreated (5 min), rep. 2no treatment control0.069.390.23Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655, Untreated (20 min), rep. 1no treatment control0.069.390.41Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655, Untreated (20 min), rep. 2no treatment control-0.349.190.56Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655, Untreated (20 min), rep. 3no treatment control-0.069.330.04Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655, Untreated (40 min), rep. 1no treatment control-0.069.330.15Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655, Untreated (40 min), rep. 2no treatment control-0.069.330.07Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655, Untreated (40 min), rep. 3no treatment control-0.129.300.07Laubacher ME and Ades SE (2008) 
E. coli K-12 BW25113, 24 h biofilmBiofilm0.137.071.00Lee J, et al. (2007)Gene Profile
E. coli K-12 MG1655, Untreated (40 min), rep. 4no treatment control-0.289.220.40Laubacher ME and Ades SE (2008) 
E. coli K-12 BW25113 ymgB755(del)::FRT-kan-FRT, 24 h biofilmBiofilm + Mutant-0.277.000.97Lee J, et al. (2007)Gene Profile
E. coli K-12 MG1655 + 60 ug/ml Cefsulodin (-5 min), rep. 1Cefsulodin-0.039.340.10Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 60 ug/ml Cefsulodin (-5 min), rep. 2Cefsulodin0.179.450.48Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 60 ug/ml Cefsulodin (5 min), rep. 1Cefsulodin0.059.390.29Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 60 ug/ml Cefsulodin (5 min), rep. 2Cefsulodin0.089.400.35Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 60 ug/ml Cefsulodin (20 min), rep. 1Cefsulodin-0.219.260.33Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 60 ug/ml Cefsulodin (20 min), rep. 2Cefsulodin-0.439.150.57Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 60 ug/ml Cefsulodin (40 min), rep. 1Cefsulodin0.029.370.27Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 60 ug/ml Cefsulodin (40 min), rep. 2Cefsulodin0.029.370.33Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 60 ug/ml Cefsulodin (40 min), rep. 3Cefsulodin-0.049.340.02Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam (-5 min), rep. 1Mecillinam0.029.370.17Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam (-5 min), rep. 2Mecillinam0.329.520.76Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam (5 min), rep. 1Mecillinam0.039.380.10Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam (5 min), rep. 2Mecillinam0.149.430.50Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam (20 min), rep. 1Mecillinam0.059.390.22Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam (20 min), rep. 2Mecillinam0.079.390.21Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam (40 min), rep. 1Mecillinam-0.189.270.22Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam (40 min), rep. 2Mecillinam-0.089.320.15Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam (40 min), rep. 3Mecillinam-0.089.320.02Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam and 60 ug/ml Cefsulodin (-5 min), rep. 1Cefsulodin + Mecillinam0.159.430.30Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam and 60 ug/ml Cefsulodin (-5 min), rep. 2Cefsulodin + Mecillinam0.249.480.48Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam and 60 ug/ml Cefsulodin (-5 min), rep. 3Cefsulodin + Mecillinam0.219.470.44Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam and 60 ug/ml Cefsulodin (5 min), rep. 1Cefsulodin + Mecillinam0.189.450.46Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam and 60 ug/ml Cefsulodin (5 min), rep. 2Cefsulodin + Mecillinam0.189.450.41Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam and 60 ug/ml Cefsulodin (5 min), rep. 3Cefsulodin + Mecillinam0.129.420.28Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam and 60 ug/ml Cefsulodin (20 min), rep. 1Cefsulodin + Mecillinam-0.129.300.02Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam and 60 ug/ml Cefsulodin (20 min), rep. 2Cefsulodin + Mecillinam-0.069.330.08Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam and 60 ug/ml Cefsulodin (20 min), rep. 3Cefsulodin + Mecillinam0.009.360.30Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam and 60 ug/ml Cefsulodin (40 min), rep. 1Cefsulodin + Mecillinam0.039.380.30Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam and 60 ug/ml Cefsulodin (40 min), rep. 2Cefsulodin + Mecillinam-0.049.340.11Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam and 60 ug/ml Cefsulodin (40 min), rep. 3Cefsulodin + Mecillinam-0.249.240.44Laubacher ME and Ades SE (2008) 
E. coli K-12 MG1655 + 0.3 ug/ml Mecillinam and 60 ug/ml Cefsulodin (40 min), rep. 4Cefsulodin + Mecillinam-0.758.991.16Laubacher ME and Ades SE (2008) 
K-12 B178 groLS(del)::cam + pOFX-HSP60(wt)-HSP10(wt) + pBAD/His A-HSP60(wt)-HSP10(wt)Overexpression0.027.480.09Bross P, et al. (2008)Gene Profile
E. coli K-12 MG1655, M63 Glucose, Exponential Phase, rep. 3Exponential phase-0.0910.580.46Dong T and Schellhorn HE (2009)Gene Profile
K-12 B178 groLS(del)::cam + pOFX-HSP60(wt)-HSP10(wt) + pBAD/His A-HSP60(Val98Ile)-HSP10(wt)Overexpression-0.027.460.19Bross P, et al. (2008)Gene Profile
E. coli K-12 MG1655, M63 Glucose, Stationary Phase, rep. 1Stationary phase0.0010.620.18Dong T, et al. (2008)Gene Profile
E. coli K-12 MG1655, M63 Glucose, Stationary Phase, rep. 2Stationary phase-0.0110.610.11Dong T and Schellhorn HE (2009)Gene Profile
E. coli K-12 MG1655, M63 Glucose, Stationary Phase, rep. 3Stationary phase0.1110.680.43Dong T, et al. (2008)Gene Profile
E. coli K-12 MG1655 rpoS(del)::FRT, M63 Glucose, Exponential Phase, rep. 1Exponential phase0.0010.620.17Dong T, et al. (2008)Gene Profile
E. coli K-12 MG1655 rpoS(del)::FRT, M63 Glucose, Exponential Phase, rep. 2Exponential phase-0.2010.520.82Dong T and Schellhorn HE (2009)Gene Profile
E. coli K-12 MG1655 rpoS(del)::FRT, M63 Glucose, Exponential Phase, rep. 3Exponential phase-0.0610.590.49Dong T, et al. (2008)Gene Profile
E. coli K-12 MG1655 rpoS(del)::FRT, M63 Glucose, Stationary Phase, rep. 1Stationary phase-0.0210.610.30Dong T, et al. (2008)Gene Profile
E. coli K-12 MG1655 plus pTN9 (paeR7I r+m+), 0 h, rep 1DNA damage-0.219.530.22Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 rpoS(del)::FRT, M63 Glucose, Stationary Phase, rep. 2Stationary phase0.0410.640.46Dong T and Schellhorn HE (2009)Gene Profile
E. coli K-12 MG1655 plus pTN9 (paeR7I r+m+), 0 h, rep 2DNA damage-0.149.560.05Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 rpoS(del)::FRT, M63 Glucose, Stationary Phase, rep. 3Stationary phase0.2810.760.93Dong T and Schellhorn HE (2009)Gene Profile
E. coli K-12 MG1655 plus pTN11 (paeR7I r-m+), 0 h, rep 1DNA damage0.409.840.72Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655, M63 Glucose, Exponential Phase, rep. 1Exponential phase-0.1010.570.54Dong T and Schellhorn HE (2009)Gene Profile
E. coli K-12 MG1655 plus pTN11 (paeR7I r-m+), 0 h, rep 2DNA damage0.449.860.81Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655, M63 Glucose, Exponential Phase, rep. 2Exponential phase-0.0110.620.04Dong T and Schellhorn HE (2009)Gene Profile
E. coli K-12 MG1655 plus pHSG415 (vector control), 0 h, rep 1DNA damage - control0.019.640.22Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 plus pHSG415 (vector control), 0 h, rep 2DNA damage - control0.119.690.33Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 plus pTN9 (paeR7I r+m+), 1 h, rep 1DNA damage-0.169.550.20Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 plus pTN9 (paeR7I r+m+), 1 h, rep 2DNA damage-0.199.540.14Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 plus pTN11 (paeR7I r-m+), 1 h, rep 1DNA damage-0.329.480.45Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 plus pTN11 (paeR7I r-m+), 1 h, rep 2DNA damage-0.169.550.14Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 plus pHSG415 (vector control), 1 h, rep 1DNA damage - control-0.169.550.15Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 plus pHSG415 (vector control), 1 h, rep 2DNA damage - control-0.319.480.42Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 plus pTN9 (paeR7I r+m+), 1 h 50 min, rep 1DNA damage0.299.780.59Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 plus pTN9 (paeR7I r+m+), 1 h 50 min, rep 2DNA damage0.299.780.67Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 plus pTN11 (paeR7I r-m+), 1 h 50 min, rep 1DNA damage0.159.710.53Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 plus pTN11 (paeR7I r-m+), 1 h 50 min, rep 2DNA damage0.149.700.43Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 plus pHSG415 (vector control), 1 h 50 min, rep 1DNA damage - control0.289.780.70Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 plus pHSG415 (vector control), 1 h 50 min, rep 2DNA damage - control0.149.710.54Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 plus pTN9 (paeR7I r+m+), 3 h, rep 1DNA damage-0.209.530.13Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 plus pTN9 (paeR7I r+m+), 3 h, rep 2DNA damage-0.299.490.50Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 plus pTN11 (paeR7I r-m+), 3 h, rep 1DNA damage-0.089.590.11Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 plus pTN11 (paeR7I r-m+), 3 h, rep 2DNA damage-0.399.440.63Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 plus pHSG415 (vector control), 3 h, rep 1DNA damage - control0.019.640.26Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 MG1655 plus pHSG415 (vector control), 3 h, rep 2DNA damage - control-0.139.570.07Asakura Y and Kobayashi I (2009)Gene Profile
E. coli K-12 C600, Exponential Phase in LB, rep. 1Wild type vs Mutant-0.017.800.17Oberto J, et al. (2009)Gene Profile
E. coli K-12 C600, Exponential Phase in LB, rep. 2Wild type vs Mutant0.127.860.49Oberto J, et al. (2009)Gene Profile
E. coli K-12 C600, Transition Phase in LBWild type vs Mutant-0.067.780.25Oberto J, et al. (2009)Gene Profile
E. coli K-12 C600, Stationary Phase in LB, rep. 1Wild type vs Mutant0.237.920.77Oberto J, et al. (2009)Gene Profile
E. coli K-12 C600, Stationary Phase in LB, rep. 2Wild type vs Mutant-0.027.790.26Oberto J, et al. (2009)Gene Profile
E. coli K-12 C600 hupA::Cm, Exponential Phase in LBWild type vs Mutant0.087.840.34Oberto J, et al. (2009)Gene Profile
E. coli K-12 C600 hupA::Cm, Transition Phase in LBWild type vs Mutant0.137.870.54Oberto J, et al. (2009)Gene Profile
E. coli K-12 C600 hupA::Cm, Stationary Phase in LBWild type vs Mutant-0.037.790.34Oberto J, et al. (2009)Gene Profile
E. coli K-12 C600 hupB::Km, Exponential Phase in LBWild type vs Mutant-0.177.720.02Oberto J, et al. (2009)Gene Profile
E. coli K-12 C600 hupB::Km, Transition Phase in LBWild type vs Mutant-0.017.800.23Oberto J, et al. (2009)Gene Profile
E. coli K-12 C600 hupB::Km, Stationary Phase in LBWild type vs Mutant-0.447.580.26Oberto J, et al. (2009)Gene Profile
E. coli K-12 C600 hupA::Cm hupB::Km, Exponential Phase in LB, rep. 1Wild type vs Mutant-0.107.750.06Oberto J, et al. (2009)Gene Profile
E. coli K-12 C600 hupA::Cm hupB::Km, Exponential Phase in LB, rep. 2Wild type vs Mutant0.057.830.34Oberto J, et al. (2009)Gene Profile
E. coli K-12 C600 hupA::Cm hupB::Km, Transition Phase in LBWild type vs Mutant0.077.840.46Oberto J, et al. (2009)Gene Profile
E. coli K-12 C600 hupA::Cm hupB::Km, Stationary Phase in LB, rep. 1Wild type vs Mutant-0.097.760.19Oberto J, et al. (2009)Gene Profile
K-12 C600 hupA::Cm hupB::Km, Stationary Phase in LB, rep. 2Wild type vs Mutant-0.147.730.06Oberto J, et al. (2009)Gene Profile
E. coli K-12 C600 rpoS, Stationary Phase in LBWild type vs Mutant-0.027.790.37Oberto J, et al. (2009)Gene Profile
E. coli K-12 C600, Exponential Phase in M9 glucoseWild type vs Mutant-0.557.530.64Oberto J, et al. (2009)Gene Profile
E. coli K-12 ATCC 25404, 24 h biofilmBiofilm-0.128.190.20Yang X, et al. (2008) 
E. coli K-12 C600, Exponential Phase in M9 glycerolWild type vs Mutant-0.257.680.23Oberto J, et al. (2009)Gene Profile
E. coli K-12 ATCC 25404 + R1drd19 Plasmid, 24 h biofilmBiofilm0.078.290.62Yang X, et al. (2008) 
E. coli K-12 C600, Stationary Phase in M9 glucoseWild type vs Mutant0.067.830.40Oberto J, et al. (2009)Gene Profile
E. coli K-12 MG1655, 24 h biofilmBiofilm0.078.280.39Yang X, et al. (2008) 
E. coli K-12 C600, Stationary Phase in M9 glycerolWild type vs Mutant0.277.940.56Oberto J, et al. (2009)Gene Profile
E. coli K-12 MG1655 + Plasmid R1drd19, 24 h biofilmBiofilm-0.028.240.05Yang X, et al. (2008) 
E. coli K-12 C600 hupA::Cm hupB::Km, Exponential Phase in M9 glucoseWild type vs Mutant-0.207.700.11Oberto J, et al. (2009)Gene Profile
E. coli K-12 BW25113 + Plasmid R1drd19, 24 h biofilm, time courseBiofilm + Time course0.458.471.94Yang X, et al. (2008) 
E. coli K-12 C600 hupA::Cm hupB::Km, Exponential Phase in M9 glycerolWild type vs Mutant0.267.930.56Oberto J, et al. (2009)Gene Profile
E. coli K-12 BW25113 + Plasmid R1drd19, 15 h biofilm, time courseBiofilm + Time course-0.228.140.86Yang X, et al. (2008) 
E. coli K-12 C600 hupA::Cm hupB::Km, Stationary Phase in M9 glucoseWild type vs Mutant0.087.840.43Oberto J, et al. (2009)Gene Profile
E. coli K-12 BW25113 + Plasmid R1drd19, 7 h biofilm, time courseBiofilm + Time course-0.028.240.49Yang X, et al. (2008) 
E. coli K-12 C600 hupA::Cm hupB::Km, Stationary Phase in M9 glycerolWild type vs Mutant0.398.000.95Oberto J, et al. (2009)Gene Profile
E. coli K-12 BW25113, 15 h biofilm, time courseBiofilm + Time course0.058.270.50Yang X, et al. (2008) 
E. coli K-12 BW25113, 24 h biofilm, time courseBiofilm + Time course-0.088.210.18Yang X, et al. (2008) 
E. coli K-12 BW25113, 7 h biofilm, time courseBiofilm + Time course-0.328.091.13Yang X, et al. (2008) 
E. coli K-12 MG1655, Aerobic 2.5 h, rep. 1Aerobic growth0.637.230.99Unpublished Experiment Set: 4780 
E. coli K-12 MG1655, Aerobic 2.5 h, rep. 2Aerobic growth0.447.140.87Reigstad CS, et al. (2007)Gene Profile
E. coli K-12 MG1655, Aerobic 5 h, rep. 1Aerobic growth-0.226.800.01Unpublished Experiment Set: 4780 
E. coli K-12 MG1655, Aerobic 5 h, rep. 2Aerobic growth-0.386.730.29Reigstad CS, et al. (2007)Gene Profile
E. coli K-12 MG1655, Aerobic 8 h, rep. 1Aerobic growth-0.146.840.06Reigstad CS, et al. (2007)Gene Profile
E. coli K-12 MG1655, Aerobic 8 h, rep. 2Aerobic growth-0.326.750.32Unpublished Experiment Set: 4780 
E. coli K-12 MG1655, Aerobic 12 h, rep. 1Aerobic growth-0.046.890.29Reigstad CS, et al. (2007)Gene Profile
E. coli K-12 MG1655, Aerobic 12 h, rep. 2Aerobic growth-0.016.910.35Reigstad CS, et al. (2007)Gene Profile
E. coli K-12 MG1655, Aerobic 18 h, rep. 1Aerobic growth-0.146.850.03Reigstad CS, et al. (2007)Gene Profile
E. coli K-12 MG1655, Aerobic 18 h, rep. 2Aerobic growth-0.236.800.12Reigstad CS, et al. (2007)Gene Profile
E. coli K-12 MG1655, Aerobic 26 h, rep. 1Aerobic growth0.076.950.42Reigstad CS, et al. (2007)Gene Profile
E. coli UTI89, Aerobic 2.5 h, rep. 1Aerobic growth-0.036.900.12Reigstad CS, et al. (2007)Gene Profile
E. coli UTI89, Aerobic 2.5 h, rep. 2Aerobic growth-0.346.750.38Unpublished Experiment Set: 4780 
E. coli UTI89, Aerobic 5 h, rep. 1Aerobic growth-0.106.870.02Reigstad CS, et al. (2007)Gene Profile
E. coli UTI89, Aerobic 8 h, rep. 1Aerobic growth-0.136.850.03Unpublished Experiment Set: 4780 
E. coli UTI89, Aerobic 8 h, rep. 2Aerobic growth-0.246.800.25Reigstad CS, et al. (2007)Gene Profile
E. coli UTI89, Aerobic 12 h, rep. 1Aerobic growth-0.276.780.33Reigstad CS, et al. (2007)Gene Profile
E. coli UTI89, Aerobic 19.5 h, rep. 1Aerobic growth0.187.010.47Reigstad CS, et al. (2007)Gene Profile
E. coli UTI89, Aerobic 19.5 h, rep. 2Aerobic growth0.116.970.39Unpublished Experiment Set: 4780 
E. coli K-12 MG1655, Anaerobic 2.5 h, rep. 1Anaerobic growth0.156.990.44Unpublished Experiment Set: 4780 
E. coli K-12 MG1655, Anaerobic 2.5 h, rep. 2Anaerobic growth-0.066.890.20Reigstad CS, et al. (2007)Gene Profile
E. coli K-12 MG1655, Anaerobic 3 h, rep. 1Anaerobic growth0.187.000.84Unpublished Experiment Set: 4780 
E. coli K-12 MG1655, Anaerobic 3 h, rep. 2Anaerobic growth0.126.970.70Unpublished Experiment Set: 4780 
E. coli K-12 MG1655, Anaerobic 3.75 h, rep. 1Anaerobic growth-0.286.780.11Reigstad CS, et al. (2007)Gene Profile
E. coli K-12 MG1655, Anaerobic 3.75 h, rep. 2Anaerobic growth-0.076.880.30Unpublished Experiment Set: 4780 
E. coli K-12 MG1655, Anaerobic 4.5 h, rep. 1Anaerobic growth-0.226.810.02Unpublished Experiment Set: 4780 
E. coli K-12 MG1655, Anaerobic 4.5 h, rep. 2Anaerobic growth-0.096.870.30Reigstad CS, et al. (2007)Gene Profile
E. coli K-12 MG1655, Anaerobic 6.75 h, rep. 1Anaerobic growth-0.086.870.21Unpublished Experiment Set: 4780 
E. coli K-12 MG1655, Anaerobic 6.75 h, rep. 2Anaerobic growth0.046.930.50Reigstad CS, et al. (2007)Gene Profile
E. coli UTI89, Anaerobic 2.5 h, rep. 1Anaerobic growth-0.086.880.01Unpublished Experiment Set: 4780 
E. coli UTI89, Anaerobic 2.5 h, rep. 2Anaerobic growth-0.286.780.25Unpublished Experiment Set: 4780 
E. coli UTI89, Anaerobic 3 h, rep. 1Anaerobic growth-0.256.790.26Unpublished Experiment Set: 4780 
E. coli UTI89, Anaerobic 3 h, rep. 2Anaerobic growth-0.116.860.02Unpublished Experiment Set: 4780 
K-12 W3110, pH 5.0, Aerobic, rep. 1Acidic medium0.199.590.12Maurer LM, et al. (2005)Gene Profile
K-12 W3110, pH 5.0, Aerobic, rep. 2Acidic medium-0.129.440.01Maurer LM, et al. (2005)Gene Profile
K-12 W3110, pH 5.0, Aerobic, rep. 3Acidic medium0.079.530.26Maurer LM, et al. (2005)Gene Profile
K-12 W3110, pH 5.0, Aerobic, rep. 4Acidic medium0.019.500.03Maurer LM, et al. (2005)Gene Profile
K-12 W3110, pH 5.0, Aerobic, rep. 5Acidic medium0.069.530.24Maurer LM, et al. (2005)Gene Profile
K-12 W3110, pH 7.0, Aerobic, rep. 1Neutral medium0.069.530.52Maurer LM, et al. (2005)Gene Profile
K-12 W3110, pH 7.0, Aerobic, rep. 2Neutral medium0.019.500.17Maurer LM, et al. (2005)Gene Profile
K-12 W3110, pH 7.0, Aerobic, rep. 3Neutral medium0.019.500.23Maurer LM, et al. (2005)Gene Profile
K-12 W3110, pH 7.0, Aerobic, rep. 4Neutral medium0.019.500.28Maurer LM, et al. (2005)Gene Profile
K-12 W3110, pH 7.0, Aerobic, rep. 5Neutral medium-0.119.440.03Maurer LM, et al. (2005)Gene Profile
K-12 W3110, pH 8.7, Aerobic, rep. 1Alkaline medium0.059.520.37Maurer LM, et al. (2005)Gene Profile
K-12 W3110, pH 8.7, Aerobic, rep. 2Alkaline medium0.069.530.21Maurer LM, et al. (2005)Gene Profile
K-12 W3110, pH 8.7, Aerobic, rep. 3Alkaline medium-0.059.470.08Maurer LM, et al. (2005)Gene Profile
K-12 W3110, pH 8.7, Aerobic, rep. 4Alkaline medium-0.249.380.55Maurer LM, et al. (2005)Gene Profile
K-12 W3110, pH 8.7, Aerobic, rep. 5Alkaline medium-0.059.470.07Maurer LM, et al. (2005)Gene Profile
K-12 MG1655 + pPROEx-CAT, high cell density, no IPTG, t=0 h, rep. 1High cell density-0.219.150.92Harcum SW and Haddadin FT (2006)Gene Profile
K-12 MG1655 + pPROEx-CAT, high cell density, no IPTG, t=0 h, rep. 2High cell density-0.149.180.77Harcum SW and Haddadin FT (2006)Gene Profile
K-12 MG1655 + pPROEx-CAT, high cell density, no IPTG, t=0 h, rep. 3High cell density-0.269.130.98Harcum SW and Haddadin FT (2006)Gene Profile
K-12 MG1655 + pPROEx-CAT, high cell density, no IPTG, t=1 h, rep. 1High cell density-0.279.120.90Harcum SW and Haddadin FT (2006)Gene Profile
K-12 MG1655 + pPROEx-CAT, high cell density, no IPTG, t=1 h, rep. 2High cell density-0.269.120.84Harcum SW and Haddadin FT (2006)Gene Profile
K-12 MG1655 + pPROEx-CAT, high cell density, no IPTG, t=1 h, rep. 3High cell density-0.219.150.75Harcum SW and Haddadin FT (2006)Gene Profile
K-12 MG1655 + pPROEx-CAT, high cell density, no IPTG, t=4 h, rep. 1High cell density0.179.340.78Harcum SW and Haddadin FT (2006)Gene Profile
K-12 MG1655 + pPROEx-CAT, high cell density, no IPTG, t=4 h, rep. 2High cell density0.189.350.80Harcum SW and Haddadin FT (2006)Gene Profile
K-12 MG1655 + pPROEx-CAT, high cell density, no IPTG, t=4 h, rep. 3High cell density0.239.370.72Harcum SW and Haddadin FT (2006)Gene Profile
K-12 MG1655 + pPROEx-CAT, high cell density + IPTG, t=1 h, rep. 1High cell density + Overexpression0.399.450.95Harcum SW and Haddadin FT (2006)Gene Profile
K-12 MG1655 + pPROEx-CAT, high cell density + IPTG, t=1 h, rep. 2High cell density + Overexpression0.319.411.03Harcum SW and Haddadin FT (2006)Gene Profile
K-12 MG1655 + pPROEx-CAT, high cell density + IPTG, t=1 h, rep. 3High cell density + Overexpression0.109.300.56Harcum SW and Haddadin FT (2006)Gene Profile
K-12 MG1655 + pPROEx-CAT, high cell density + IPTG, t=4 h, rep. 1High cell density + Overexpression-0.029.250.12Haddadin FT and Harcum SW (2005)Gene Profile
K-12 MG1655 + pPROEx-CAT, high cell density + IPTG, t=4 h, rep. 2High cell density + Overexpression0.099.300.35Haddadin FT and Harcum SW (2005)Gene Profile
K-12 MG1655 + pPROEx-CAT, high cell density + IPTG, t=4 h, rep. 3High cell density + Overexpression0.019.260.21Haddadin FT and Harcum SW (2005)Gene Profile
K-12 MG1655, high cell density, no IPTG, t=0 h, rep. 1High cell density0.129.320.85Haddadin FT and Harcum SW (2005)Gene Profile
K-12 MG1655, high cell density, no IPTG, t=0 h, rep. 2High cell density0.119.311.06Haddadin FT and Harcum SW (2005)Gene Profile
K-12 MG1655, high cell density, no IPTG, t=0 h, rep. 3High cell density-0.019.250.59Haddadin FT and Harcum SW (2005)Gene Profile
K-12 MG1655, high cell density, no IPTG, t=1 h, rep. 1High cell density-0.029.250.15Haddadin FT and Harcum SW (2005)Gene Profile
K-12 MG1655, high cell density, no IPTG, t=1 h, rep. 2High cell density0.089.290.63Haddadin FT and Harcum SW (2005)Gene Profile
K-12 MG1655, high cell density, no IPTG, t=1 h, rep. 3High cell density-0.089.210.20Haddadin FT and Harcum SW (2005)Gene Profile
K-12 MG1655, high cell density, no IPTG, t=4 h, rep. 1High cell density-0.419.051.29Haddadin FT and Harcum SW (2005)Gene Profile
K-12 W3110, pH 5.7, Anaerobic, rep. 1Acidic medium-0.228.640.51Hayes ET, et al. (2006)Gene Profile
K-12 W3110, pH 5.7, Anaerobic, rep. 2Acidic medium-0.348.580.74Hayes ET, et al. (2006)Gene Profile
K-12 MG1655, high cell density, no IPTG, t=4 h, rep. 3High cell density-0.209.150.74Haddadin FT and Harcum SW (2005)Gene Profile
K-12 W3110, pH 5.7, Anaerobic, rep. 3Acidic medium-0.278.620.53Hayes ET, et al. (2006)Gene Profile
K-12 MG1655, high cell density + IPTG, t=1 h, rep. 1High cell density-0.049.240.27Haddadin FT and Harcum SW (2005)Gene Profile
K-12 W3110, pH 5.7, Anaerobic, rep. 4Acidic medium-0.418.551.05Hayes ET, et al. (2006)Gene Profile
K-12 MG1655, high cell density + IPTG, t=1 h, rep. 2High cell density0.209.351.35Haddadin FT and Harcum SW (2005)Gene Profile
K-12 W3110, pH 5.7, Anaerobic, rep. 5Acidic medium-0.418.550.85Hayes ET, et al. (2006)Gene Profile
K-12 MG1655, high cell density + IPTG, t=1 h, rep. 3High cell density-0.079.220.12Haddadin FT and Harcum SW (2005)Gene Profile
K-12 W3110, pH 7.0, Anaerobic, rep. 1Neutral medium0.188.840.61Hayes ET, et al. (2006)Gene Profile
K-12 MG1655, high cell density + IPTG, t=4 h, rep. 1High cell density-0.119.200.03Haddadin FT and Harcum SW (2005)Gene Profile
K-12 W3110, pH 7.0, Anaerobic, rep. 2Neutral medium0.358.930.93Hayes ET, et al. (2006)Gene Profile
K-12 MG1655, high cell density + IPTG, t=4 h, rep. 2High cell density-0.049.230.01Haddadin FT and Harcum SW (2005)Gene Profile
K-12 W3110, pH 7.0, Anaerobic, rep. 3Neutral medium0.539.021.45Hayes ET, et al. (2006)Gene Profile
K-12 MG1655, high cell density + IPTG, t=4 h, rep. 3High cell density0.029.260.37Haddadin FT and Harcum SW (2005)Gene Profile
K-12 W3110, pH 7.0, Anaerobic, rep. 4Neutral medium0.318.910.92Hayes ET, et al. (2006)Gene Profile
K-12 W3110, pH 7.0, Anaerobic, rep. 5Neutral medium0.358.931.03Hayes ET, et al. (2006)Gene Profile
K-12 W3110, pH 8.5, Anaerobic, rep. 1Alkaline medium-0.088.710.12Hayes ET, et al. (2006)Gene Profile
K-12 W3110, pH 8.5, Anaerobic, rep. 2Alkaline medium-0.038.740.04Hayes ET, et al. (2006)Gene Profile
K-12 W3110, pH 8.5, Anaerobic, rep. 3Alkaline medium-0.058.730.00Hayes ET, et al. (2006)Gene Profile
K-12 W3110, pH 8.5, Anaerobic, rep. 4Alkaline medium-0.138.680.27Hayes ET, et al. (2006)Gene Profile
K-12 W3110, pH 8.5, Anaerobic, rep. 5Alkaline medium-0.248.630.53Hayes ET, et al. (2006)Gene Profile
K-12 BW13711, no Tannins, rep. 2Tannins - control-0.1710.180.72Zoetendal EG, et al. (2008)Gene Profile
K-12 BW13711, no Tannins, rep. 8Tannins - control0.0010.270.47Zoetendal EG, et al. (2008)Gene Profile
K-12 BW13711 + Tannins (1% wattle tannin extract), rep. 3Tannins0.1410.340.91Zoetendal EG, et al. (2008)Gene Profile
K-12 BW13711 + Tannins (1% wattle tannin extract), rep. 5Tannins0.0110.280.35Zoetendal EG, et al. (2008)Gene Profile
E. coli K-12 BW25113 WTWild type vs Mutant-0.0513.140.29Wang X, et al. (2009)Gene Profile
E. coli K-12 BW25113 CP4-57(excised)Wild type vs Mutant0.0513.180.38Wang X, et al. (2009)Gene Profile
K-12 BW25113 ldhA+ pflB+Microaerobic growth0.106.010.51Singh A, et al. (2010)Gene Profile
K-12 BW25113 ldhA(del)::FRT, pflB(del)::FRT in Microaerobic growthMicroaerobic growth-0.105.910.31Singh A, et al. (2010)Gene Profile
K-12 MG1655 + DMSO, rep. 3CHIR-090 - Mock treatment0.281.960.88Zhu K, et al. (2009)Gene Profile
K-12 MG1655 + CHIR-090, rep. 2CHIR-090-0.111.760.40Zhu K, et al. (2009)Gene Profile
K-12 MG1655 + CHIR-090, rep. 3CHIR-090-0.221.710.87Zhu K, et al. (2009)Gene Profile
K-12 MG1655 pAZ3 (empty vector) rep. 1Overexpression - control-0.0911.290.34Durand S and Storz G (2010)Gene Profile
K-12 MG1655 pAZ3-FnrS rep. 1Overexpression0.2011.430.50Durand S and Storz G (2010)Gene Profile
K-12 MG1655 pAZ3 (empty vector) rep. 2Overexpression - control0.1811.420.70Durand S and Storz G (2010)Gene Profile
K-12 MG1655 pAZ3-FnrS rep. 2Overexpression-0.1311.260.15Durand S and Storz G (2010)Gene Profile
K-12 MG1655 pAZ3 (empty vector) rep. 3Overexpression - control-0.0711.290.01Durand S and Storz G (2010)Gene Profile
K-12 MG1655 pAZ3-FnrS rep. 3Overexpression-0.1311.260.21Durand S and Storz G (2010)Gene Profile
600 nM Zn Cy3 vs. 0.2 mM Zn Cy5Zinc0.3711.020.35Lee LJ, et al. (2005) 
0.2 mM Zn Cy3 vs. 600 nM Zn Cy5Zinc-0.5910.350.62Lee LJ, et al. (2005) 
600 nM Zn Cy3 vs. 0.2 mM Zn Cy5 (rep)Zinc0.0511.690.04Lee LJ, et al. (2005) 
0.2 mM Zn Cy3 vs. 600 nM Zn Cy5 (rep)Zinc-0.639.860.72Lee LJ, et al. (2005) 
600 nM Zn Cy3 vs. 0.2 mM Zn Cy5 (rep1)Zinc0.159.500.05Lee LJ, et al. (2005) 
0.2 mM Zn Cy3 vs. 600 nM Zn Cy5 (rep1)Zinc-0.109.900.17Lee LJ, et al. (2005) 
O157:H7 isolate 486/99 + reference poolGenome comparison1.0413.280.59Wu G, et al. (2008) 
O157:H7 isolate 665/99 + reference poolGenome comparison-0.9212.310.25Wu G, et al. (2008) 
O157:H7 isolate 665/99 + reference pool rep1Genome comparison-3.4411.041.04Wu G, et al. (2008) 
O157:H7 isolate 665/99 + reference pool rep2Genome comparison-1.4012.070.46Wu G, et al. (2008) 
O157:H7 isolate 1176/00 + reference poolGenome comparison-0.4512.540.54Wu G, et al. (2008) 
O157:H7 isolate 1176/00 + reference pool rep1Genome comparison1.9013.711.36Wu G, et al. (2008) 
O157:H7 isolate 1458/00 + reference poolGenome comparison0.3212.920.24Wu G, et al. (2008) 
O157:H7 isolate 1460/00 + reference poolGenome comparison-0.9512.290.72Wu G, et al. (2008) 
O157:H7 isolate 1460/00 + reference pool rep1Genome comparison-0.2112.660.51Wu G, et al. (2008) 
O157:H7 isolate 1461/00 + reference poolGenome comparison-0.6712.430.46Wu G, et al. (2008) 
O157:H7 isolate 1461/00 + reference pool rep1Genome comparison-0.1112.710.55Wu G, et al. (2008) 
O157:H7 isolate 1462/00 + reference poolGenome comparison-0.7412.390.38Wu G, et al. (2008) 
O157:H7 isolate 1462/00 + reference pool rep1Genome comparison0.1712.850.07Wu G, et al. (2008) 
O157:H7 isolate 1466/00 + reference poolGenome comparison-0.1012.720.03Wu G, et al. (2008) 
O157:H7 isolate 1466/00 + reference pool rep1Genome comparison-0.6212.450.05Wu G, et al. (2008) 
O157:H7 isolate 1583/00 + reference poolGenome comparison0.1312.830.06Wu G, et al. (2008) 
O157:H7 isolate 1583/00 + reference pool rep1Genome comparison-0.1912.670.15Wu G, et al. (2008) 
K-12 NCM3722 + 30C, no NaCl, no glycine betaine, rep 1Hyperosmotic - control0.039.970.24Gunasekera TS, et al. (2008)Gene Profile
K-12 NCM3722 + 30C, 0.3 M NaCl, no glycine betaine, rep 1Hyperosmotic0.1710.040.33Gunasekera TS, et al. (2008)Gene Profile
K-12 NCM3722 + 30C, 0.3 M NaCl, 1 mM glycine betaine, rep. 1Hyperosmotic-0.109.900.06Gunasekera TS, et al. (2008)Gene Profile
K-12 NCM3722 + 43C, no NaCl, no glycine betaine, rep 1Hyperosmotic - control0.3310.120.64Gunasekera TS, et al. (2008)Gene Profile
K-12 NCM3722 + 43C, 0.3 M NaCl, no glycine betaine, rep 1Hyperosmotic0.049.970.29Gunasekera TS, et al. (2008)Gene Profile
K-12 NCM3722 + 43C, 0.3 M NaCl, 1 mM glycine betaine, rep 1Hyperosmotic-0.099.900.05Gunasekera TS, et al. (2008)Gene Profile
K-12 NCM3722 + 30C, no NaCl, no glycine betaine, rep 2Hyperosmotic - control0.079.990.37Gunasekera TS, et al. (2008)Gene Profile
K-12 NCM3722 + 30C, 0.3 M NaCl, no glycine betaine, rep 2Hyperosmotic-0.509.700.85Gunasekera TS, et al. (2008)Gene Profile
K-12 NCM3722 + 30C, 0.3 M NaCl, 1 mM glycine betaine, rep 2Hyperosmotic-0.369.770.48Gunasekera TS, et al. (2008)Gene Profile
K-12 NCM3722 + 43C, no NaCl, no glycine betaine, rep 2Hyperosmotic - control-0.269.820.23Gunasekera TS, et al. (2008)Gene Profile
K-12 NCM3722 + 43C, 0.3 M NaCl, no glycine betaine, rep 2Hyperosmotic-0.329.790.34Gunasekera TS, et al. (2008)Gene Profile
K-12 NCM3722 + 43C, 0.3 M NaCl, 1 mM glycine betaine, rep 2Hyperosmotic-0.699.610.85Gunasekera TS, et al. (2008)Gene Profile
K-12 NCM3722 + 30C, no NaCl, no glycine betaine, rep 3Hyperosmotic - control0.2510.080.55Gunasekera TS, et al. (2008)Gene Profile
K-12 NCM3722 + 30C, 0.3 M NaCl, no glycine betaine, rep 3Hyperosmotic0.1010.000.16Gunasekera TS, et al. (2008)Gene Profile
K-12 NCM3722 + 30C, 0.3 M NaCl, 1 mM glycine betaine, rep 3Hyperosmotic0.2610.080.47Gunasekera TS, et al. (2008)Gene Profile
K-12 NCM3722 + 43C, no NaCl, no glycine betaine, rep 3Hyperosmotic - control-0.029.940.12Gunasekera TS, et al. (2008)Gene Profile
K-12 NCM3722 + 43C, 0.3 M NaCl, no glycine betaine, rep 3Hyperosmotic0.049.970.17Gunasekera TS, et al. (2008)Gene Profile
K-12 NCM3722 + 43C, 0.3 M NaCl, 1 mM glycine betaine, rep 3Hyperosmotic0.5010.200.75Gunasekera TS, et al. (2008)Gene Profile
O157:H7 EDL933 TUV93-0 treated with ME0052 rep1Type III secretion (TTS) inhibitors-0.568.730.56Tree JJ, et al. (2009) 
O157:H7 EDL933 TUV93-0 treated with ME0052 rep2Type III secretion (TTS) inhibitors-0.498.860.40Tree JJ, et al. (2009) 
O157:H7 EDL933 TUV93-0 treated with ME0052 rep3Type III secretion (TTS) inhibitors-0.468.480.38Tree JJ, et al. (2009) 
O157:H7 EDL933 TUV93-0 treated with ME0053 rep1Type III secretion (TTS) inhibitors-0.189.640.18Tree JJ, et al. (2009) 
O157:H7 EDL933 TUV93-0 treated with ME0053 rep2Type III secretion (TTS) inhibitors-0.549.130.59Tree JJ, et al. (2009) 
O157:H7 EDL933 TUV93-0 treated with ME0053 rep3Type III secretion (TTS) inhibitors-0.489.020.58Tree JJ, et al. (2009) 
O157:H7 EDL933 TUV93-0 treated with ME0054 rep1Type III secretion (TTS) inhibitors-0.219.090.26Tree JJ, et al. (2009) 
O157:H7 EDL933 TUV93-0 treated with ME0054 rep2Type III secretion (TTS) inhibitors-0.499.490.26Tree JJ, et al. (2009) 
O157:H7 EDL933 TUV93-0 treated with ME0054 rep3Type III secretion (TTS) inhibitors-0.299.380.34Tree JJ, et al. (2009) 
O157:H7 EDL933 TUV93-0 treated with ME0055 rep1Type III secretion (TTS) inhibitors0.0612.250.01Tree JJ, et al. (2009) 
O157:H7 EDL933 TUV93-0 treated with ME0055 rep2Type III secretion (TTS) inhibitors0.1412.970.01Tree JJ, et al. (2009) 
O157:H7 EDL933 TUV93-0 treated with ME0055 rep3Type III secretion (TTS) inhibitors0.1411.950.14Tree JJ, et al. (2009) 
K-12 BW25113 + Amp for 2 hAmpicillin-0.063.511.52Unpublished Experiment Set: 5635 
K-12 BW25113 hfq(del)::FRT-kan-FRT + Amp for 2 hAmpicillin0.053.571.42Kim Y and Wood TK (2010) 
K-12 MG1655 -CO, Anaerobic, rep. 2Carbon monoxide - control0.029.600.14Nobre LS, et al. (2009)Gene Profile
K-12 MG1655 +CO, Anaerobic, rep. 2Carbon monoxide-0.429.380.42Nobre LS, et al. (2009)Gene Profile
K-12 MG1655 -CO, Anaerobic, rep. 1Carbon monoxide - control-0.259.470.14Nobre LS, et al. (2009)Gene Profile
K-12 MG1655 +CO, Anaerobic, rep. 1Carbon monoxide-0.599.300.61Nobre LS, et al. (2009)Gene Profile
K-12 MG1655 -CO, Aerobic, rep. 2Carbon monoxide - control0.299.740.47Nobre LS, et al. (2009)Gene Profile
K-12 MG1655 +CO, Aerobic, rep. 2Carbon monoxide0.309.740.77Nobre LS, et al. (2009)Gene Profile
K-12 MG1655 -CO, Aerobic, rep. 1Carbon monoxide - control0.089.630.20Nobre LS, et al. (2009)Gene Profile
K-12 MG1655 +CO, Aerobic, rep. 1Carbon monoxide0.289.730.67Nobre LS, et al. (2009)Gene Profile
K-12 W3110 (is crp+), LB + Glu, expo. phase, rep. 1Wild type vs Mutant-0.8810.340.91Khankal R, et al. (2009)Gene Profile
K-12 W3110 (is crp+), LB + Glu, expo. phase, rep. 2Wild type vs Mutant0.0710.810.16Khankal R, et al. (2009)Gene Profile
K-12 W3110 (is crp+), LB + Glu, expo. phase, rep. 3Wild type vs Mutant0.0710.810.16Khankal R, et al. (2009)Gene Profile
K-12 W3110 (is crp+), LB, expo. phase, rep. 1Wild type vs Mutant0.6611.111.07Khankal R, et al. (2009)Gene Profile
K-12 W3110 (is crp+), LB, expo. phase, rep. 2Wild type vs Mutant0.4711.010.82Khankal R, et al. (2009)Gene Profile
K-12 W3110 (is crp+), LB, expo. phase, rep. 3Wild type vs Mutant0.0310.790.12Khankal R, et al. (2009)Gene Profile
K-12 W3110 crp*-Tn10, LB + Glu, expo. phase, rep. 1Wild type vs Mutant0.5611.060.89Khankal R, et al. (2009)Gene Profile
K-12 W3110 crp*-Tn10, LB + Glu, expo. phase, rep. 2Wild type vs Mutant-0.2910.630.36Khankal R, et al. (2009)Gene Profile
K-12 W3110 crp*-Tn10, LB + Glu, expo. phase, rep. 3Wild type vs Mutant-0.0810.740.01Khankal R, et al. (2009)Gene Profile
K-12 W3110 crp*-Tn10, LB + Glu, expo. phase, rep. 4Wild type vs Mutant-0.8310.361.47Khankal R, et al. (2009)Gene Profile
K-12 W3110 crp*-Tn10, LB + Glu, expo. phase, rep. 5Wild type vs Mutant-0.6010.481.13Khankal R, et al. (2009)Gene Profile
K-12 W3110 crp*-Tn10, LB, expo. phase, rep. 1Wild type vs Mutant-0.1310.710.12Khankal R, et al. (2009)Gene Profile
K-12 W3110 crp*-Tn10, LB, expo. phase, rep. 2Wild type vs Mutant-0.0610.750.05Khankal R, et al. (2009)Gene Profile
K-12 W3110 crp*-Tn10, LB, expo. phase, rep. 3Wild type vs Mutant0.0710.810.30Khankal R, et al. (2009)Gene Profile
K-12 BW25113 ompA(del)::kan + pCA24N (vector)Overexpression - control-0.2811.041.35Ma Q and Wood TK (2009) 
K-12 BW25113 ompA(del)::kan + pCA24N-ompA+Overexpression0.2511.310.99Ma Q and Wood TK (2009) 
K-12 BW25113 ompA(del)::kan, 15 h biofilm (polystyrene), rep. 1Biofilm + Mutant0.0011.190.30Ma Q and Wood TK (2009) 
K-12 BW25113, 15 h biofilm (polystyrene), rep. 1Biofilm + Parental strain-0.0211.170.09Ma Q and Wood TK (2009) 
K-12 BW25113 ompA(del)::kan, 15 h biofilm (glass wool)Biofilm + Mutant-0.078.350.10Ma Q and Wood TK (2009) 
K-12 MG1655 fnr-267(del) dinI overexpressed + Norfloxacin (25 ng/ml), rep. 1DNA damage0.149.040.24Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) dinI overexpressed + Norfloxacin (25 ng/ml), rep. 2DNA damage0.239.080.48Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) dinI overexpressed + Norfloxacin (25 ng/ml), rep. 3DNA damage0.219.070.52Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) dinP overexpressed + Norfloxacin (25 ng/ml), rep. 1DNA damage0.299.110.71Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) dinP overexpressed + Norfloxacin (25 ng/ml), rep. 2DNA damage0.309.110.68Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) dinP overexpressed + Norfloxacin (25 ng/ml), rep. 3DNA damage0.179.050.41Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) lexA overexpressed + Norfloxacin (25 ng/ml), rep. 1DNA damage0.339.130.72Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) lexA overexpressed + Norfloxacin (25 ng/ml), rep. 2DNA damage0.249.080.50Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) lexA overexpressed + Norfloxacin (25 ng/ml), rep. 3DNA damage0.229.080.53Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) lon overexpressed + Norfloxacin (25 ng/ml), rep. 1DNA damage0.299.110.60Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) lon overexpressed + Norfloxacin (25 ng/ml), rep. 2DNA damage0.109.010.30Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) lon overexpressed + Norfloxacin (25 ng/ml), rep. 3DNA damage0.179.050.35Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) luc overexpressed + Norfloxacin (25 ng/ml), rep. 1DNA damage0.289.100.58Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) luc overexpressed + Norfloxacin (25 ng/ml), rep. 2DNA damage0.369.140.92Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) luc overexpressed + Norfloxacin (25 ng/ml), rep. 3DNA damage0.119.020.27Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) mazF overexpressed + Norfloxacin (25 ng/ml), rep. 1DNA damage-0.148.900.24Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) mazF overexpressed + Norfloxacin (25 ng/ml), rep. 2DNA damage-0.018.960.04Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) mazF overexpressed + Norfloxacin (25 ng/ml), rep. 3DNA damage-0.028.960.06Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) recA overexpressed + Norfloxacin (25 ng/ml), rep. 1DNA damage0.149.030.33Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) recA overexpressed + Norfloxacin (25 ng/ml), rep. 2DNA damage0.179.050.46Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) recA overexpressed + Norfloxacin (25 ng/ml), rep. 3DNA damage0.189.050.41Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) relE overexpressed + Norfloxacin (25 ng/ml), rep. 1DNA damage-0.068.940.10Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) relE overexpressed + Norfloxacin (25 ng/ml), rep. 2DNA damage-0.058.940.04Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) relE overexpressed + Norfloxacin (25 ng/ml), rep. 3DNA damage-0.248.840.32Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) ruvA overexpressed + Norfloxacin (25 ng/ml), rep. 1DNA damage0.249.080.48Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) ruvA overexpressed + Norfloxacin (25 ng/ml), rep. 2DNA damage0.279.100.59Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) ruvA overexpressed + Norfloxacin (25 ng/ml), rep. 3DNA damage0.209.070.51Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) sulA overexpressed + Norfloxacin (25 ng/ml), rep. 1DNA damage0.129.020.29Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) sulA overexpressed + Norfloxacin (25 ng/ml), rep. 2DNA damage0.249.090.57Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) sulA overexpressed + Norfloxacin (25 ng/ml), rep. 3DNA damage0.329.120.73Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) umuD overexpressed + Norfloxacin (25 ng/ml), rep. 1DNA damage0.099.010.24Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) umuD overexpressed + Norfloxacin (25 ng/ml), rep. 2DNA damage0.089.000.21Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) umuD overexpressed + Norfloxacin (25 ng/ml), rep. 3DNA damage0.229.070.50Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) uvrA overexpressed + Norfloxacin (25 ng/ml), rep. 1DNA damage0.099.010.19Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) uvrA overexpressed + Norfloxacin (25 ng/ml), rep. 2DNA damage0.199.060.42Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) uvrA overexpressed + Norfloxacin (25 ng/ml), rep. 3DNA damage0.119.020.20Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) yebF overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage0.068.990.63Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) yebF overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.269.090.78Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) yebF overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.098.920.19Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) luc overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage0.048.980.38Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) luc overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.038.950.01Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) luc overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.068.930.04Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) zipA overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage0.179.050.76Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) zipA overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.058.990.19Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) zipA overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.078.930.13Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) luc overexpressed, rep. 1DNA damage - control0.259.090.35Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) luc overexpressed, rep. 2DNA damage - control0.319.120.57Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) luc overexpressed, rep. 3DNA damage - control0.129.020.19Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) yfjF overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.168.880.15Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) yfjF overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.159.040.55Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) yfjF overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.178.880.12Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) bcp overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.108.910.09Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) bcp overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.028.950.24Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) bcp overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.108.910.05Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) cpxR overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.198.870.21Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) cpxR overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.648.641.13Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) cpxR overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.048.940.25Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) crcB overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.138.900.05Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) crcB overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.448.740.88Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) crcB overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage0.129.030.58Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) crp overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.138.900.11Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) crp overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.028.970.35Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) crp overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage0.008.970.33Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) cspF overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage0.018.970.12Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) cspF overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.159.040.62Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) cspF overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage0.069.000.41Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) dam overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage0.079.000.45Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) dam overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.159.040.74Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) dam overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage0.038.980.08Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) dnaA overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.118.910.02Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) dnaA overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-1.088.421.86Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) dnaA overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage0.028.980.40Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) dnaN overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.048.940.09Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) dnaN overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.018.960.04Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) dnaN overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.138.900.05Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) dnaT overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.048.940.26Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) dnaT overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.248.840.67Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) dnaT overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage0.008.960.31Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) emrA overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage0.169.040.42Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) emrA overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.048.950.13Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) era overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.108.910.02Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) era overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.108.920.09Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) era overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.018.960.23Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) fis overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.048.950.18Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) fis overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.218.860.51Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) fis overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.168.880.13Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) fklB overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.208.870.09Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) fklB overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.008.970.28Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) fklB overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.138.900.01Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) folA overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.108.910.03Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) folA overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.028.970.39Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) folA overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage0.069.000.39Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) galF overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.078.930.24Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) galF overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.028.980.24Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) galF overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage0.038.980.38Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) gcvR overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage0.018.970.41Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) gcvR overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.028.950.14Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) gcvR overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage0.119.020.57Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) gyrA overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.098.920.03Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) gyrA overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.298.820.60Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) gyrA overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.088.920.11Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) gyrI overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.338.800.60Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) gyrI overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.089.000.52Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) gyrI overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage0.038.980.38Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) skp overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage0.048.980.38Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) skp overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.089.010.26Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) skp overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage0.119.020.70Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) holD overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.108.920.15Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) holD overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.018.960.05Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) holD overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.028.950.16Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) hscA overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.168.890.42Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) hscA overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.058.990.17Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) hscA overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.298.820.75Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) ihfA overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.018.960.07Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) ihfA overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.538.701.61Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) ldrA overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.388.770.83Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) ldrA overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.099.010.34Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) ldrA overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.938.501.72Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) mcrB overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.258.840.25Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) mcrB overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.038.950.25Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) mcrB overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.048.940.14Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) mcrC overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.178.880.06Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) mcrC overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.038.950.23Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) mcrC overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.048.940.10Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) menB overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.318.810.56Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) menB overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.068.930.22Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) menB overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage0.058.990.51Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) menC overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage0.028.970.48Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) menC overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.028.980.41Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) menC overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage0.219.070.82Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) minD overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.858.542.48Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) minD overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.068.930.35Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) minD overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage0.099.010.50Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) minE overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage0.139.030.55Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) minE overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.068.930.05Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) minE overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.028.960.25Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) murI overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage0.129.030.60Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) murI overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.068.990.32Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) murI overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage0.028.980.30Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) yoeB overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.158.890.17Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) yoeB overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.038.980.09Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) yoeB overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.048.940.09Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) nrdA overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage0.068.990.17Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) nrdA overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.048.990.24Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) nrdA overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage0.028.980.09Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) nrdB overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage0.229.080.53Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) nrdB overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage0.069.000.00Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) nupC overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.158.890.21Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) nupC overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.219.070.70Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) nupC overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.618.661.56Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) pyrC overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.158.890.02Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) pyrC overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.068.990.39Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) pyrC overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.178.880.00Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) rimI overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.018.960.32Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) rimI overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.008.960.30Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) rimI overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage0.058.990.41Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) rstB overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.368.780.64Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) rstB overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.048.950.04Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) rstB overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.028.960.23Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) ruvC overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage0.079.000.17Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) ruvC overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.119.020.33Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) ruvC overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.008.960.29Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) sbcB overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.158.890.02Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) sbcB overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.048.990.29Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) sbcB overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage0.028.970.41Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) uspA overexpressed + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.098.920.06Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) uspA overexpressed + Norfloxacin (75 ng/ml), rep. 2DNA damage0.079.000.49Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) uspA overexpressed + Norfloxacin (75 ng/ml), rep. 3DNA damage-0.018.960.41Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del), rep. 1DNA damage - control-0.598.670.24Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del), rep. 2DNA damage - control-1.028.451.19Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), rep. 1DNA damage-0.208.860.34Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), rep. 2DNA damage-0.028.950.41Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (50 ng/ml), rep. 1DNA damage-0.428.750.26Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (50 ng/ml), rep. 2DNA damage-0.388.780.04Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (75 ng/ml), rep. 1DNA damage-0.208.870.19Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (75 ng/ml), rep. 2DNA damage-0.208.860.20Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) recA(del), rep. 1DNA damage - control-0.228.850.23Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) recA(del), rep. 2DNA damage - control-0.308.810.24Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) recA(del) + Norfloxacin (50 ng/ml), rep. 1DNA damage-0.158.890.08Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) recA(del) + Norfloxacin (50 ng/ml), rep. 2DNA damage0.119.020.41Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) recA(del) + Norfloxacin (0.1 ug/ml), rep. 1DNA damage-0.698.620.93Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) recA(del) + Norfloxacin (0.1 ug/ml), rep. 2DNA damage-0.678.630.84Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (0.1 ug/ml), rep. 1DNA damage-0.488.720.34Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (0.1 ug/ml), rep. 2DNA damage-0.468.740.32Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) luc overexpressed + Norfloxacin (25 ng/ml), rep. 4DNA damage-0.318.810.18Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) luc overexpressed + Norfloxacin (25 ng/ml), rep. 5DNA damage0.209.070.53Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) luc overexpressed, rep. 4DNA damage - control0.018.970.48Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) luc overexpressed, rep. 5DNA damage - control0.079.000.32Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), t=0, rep. 1DNA damage - control0.359.140.71Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), t=0, rep. 2DNA damage - control0.399.160.78Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), t=0, rep. 3DNA damage - control0.419.170.76Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), t=12 min, rep. 1DNA damage-0.048.940.14Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), t=12 min, rep. 2DNA damage0.189.050.39Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), t=12 min, rep. 3DNA damage0.119.020.32Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), t=24 min, rep. 1DNA damage0.339.130.51Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), t=24 min, rep. 2DNA damage0.389.160.57Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), t=24 min, rep. 3DNA damage0.429.170.61Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + untreated, t=24 min, rep. 1DNA damage - control-0.048.940.09Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + untreated, t=24 min, rep. 2DNA damage - control0.008.970.00Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + untreated, t=24 min, rep. 3DNA damage - control-0.238.850.42Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), t=36 min, rep. 1DNA damage0.169.050.33Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), t=36 min, rep. 2DNA damage0.319.120.47Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), t=36 min, rep. 3DNA damage0.249.080.40Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), t=48 min, rep. 1DNA damage-0.008.960.22Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), t=48 min, rep. 2DNA damage-0.038.950.15Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), t=48 min, rep. 3DNA damage0.199.060.39Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), t=60 min, rep. 1DNA damage-0.088.920.22Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), t=60 min, rep. 2DNA damage0.058.990.35Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + Norfloxacin (25 ng/ml), t=60 min, rep. 3DNA damage0.058.990.29Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + untreated, t=60 min, rep. 1DNA damage - control-0.568.690.82Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + untreated, t=60 min, rep. 2DNA damage - control-0.258.840.35Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + untreated, t=60 min, rep. 3DNA damage - control-0.238.850.28Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + ccdB induction, t=0DNA damage0.038.980.03Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + ccdB induction, t=30 minDNA damage0.079.000.23Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + ccdB induction, t=60 minDNA damage-0.288.820.38Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + ccdB induction, t=90 minDNA damage-0.518.710.64Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + ccdB induction, t=120 minDNA damage-0.578.680.76Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + lacZ induction, t=0Overexpression0.058.990.03Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + lacZ induction, t=30Overexpression-0.058.940.02Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + lacZ induction, t=60Overexpression-0.098.920.13Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + lacZ induction, t=90Overexpression0.179.050.45Faith JJ, et al. (2007) 
K-12 MG1655 fnr-267(del) + lacZ induction, t=120Overexpression0.139.030.43Faith JJ, et al. (2007) 
K-12 MG1063 (is recA56) + lacZ induction, t=0 min, rep. 1Overexpression0.309.120.48Faith JJ, et al. (2007) 
K-12 MG1063 (is recA56) + lacZ induction, t=0 min, rep. 2Overexpression0.139.030.13Faith JJ, et al. (2007) 
K-12 MG1063 (is recA56) + lacZ induction, t=30 min, rep. 1Overexpression0.119.020.28Faith JJ, et al. (2007) 
K-12 MG1063 (is recA56) + lacZ induction, t=30 min, rep. 2Overexpression0.139.030.20Faith JJ, et al. (2007) 
K-12 MG1063 (is recA56) + lacZ induction, t=60 min, rep. 1Overexpression0.018.970.18Faith JJ, et al. (2007) 
K-12 MG1063 (is recA56) + lacZ induction, t=60 min, rep. 2Overexpression0.089.000.16Faith JJ, et al. (2007) 
K-12 MG1063 (is recA56) + lacZ induction, t=90 min, rep. 1Overexpression-0.028.950.11Faith JJ, et al. (2007) 
K-12 MG1063 (is recA56) + lacZ induction, t=90 min, rep. 2DNA damage - control-0.128.900.10Faith JJ, et al. (2007) 
K-12 MG1063 (is recA56) + ccdB induction, t=0 min, rep. 1DNA damage0.359.140.49Faith JJ, et al. (2007) 
K-12 MG1063 (is recA56) + ccdB induction, t=0 min, rep. 2DNA damage0.289.100.38Faith JJ, et al. (2007) 
K-12 MG1063 (is recA56) + ccdB induction, t=30 min, rep. 1DNA damage0.229.080.38Faith JJ, et al. (2007) 
K-12 MG1063 (is recA56) + ccdB induction, t=30 min, rep. 2DNA damage0.169.050.24Faith JJ, et al. (2007) 
K-12 MG1063 (is recA56) + ccdB induction, t=60 min, rep. 1DNA damage0.259.090.44Faith JJ, et al. (2007) 
K-12 MG1063 (is recA56) + ccdB induction, t=60 min, rep. 2DNA damage0.259.090.39Faith JJ, et al. (2007) 
K-12 MG1063 (is recA56) + ccdB induction, t=90 min, rep. 1DNA damage0.149.030.44Faith JJ, et al. (2007) 
K-12 MG1063 (is recA56) + ccdB induction, t=90 min, rep. 2DNA damage0.018.970.27Faith JJ, et al. (2007) 
K-12 W1863 (is recA+) + lacZ induction, t=0 minOverexpression0.289.100.55Faith JJ, et al. (2007) 
K-12 W1863 (is recA+) + lacZ induction, t=30 minOverexpression0.089.010.22Faith JJ, et al. (2007) 
K-12 W1863 (is recA+) + lacZ induction, t=60 minOverexpression-0.118.910.04Faith JJ, et al. (2007) 
K-12 W1863 (is recA+) + lacZ induction, t=90 minOverexpression-0.268.830.20Faith JJ, et al. (2007) 
K-12 W1863 (is recA+) + ccdB induction, t=0 minDNA damage0.159.040.23Faith JJ, et al. (2007) 
K-12 W1863 (is recA+) + ccdB induction, t=30 minDNA damage-0.058.940.00Faith JJ, et al. (2007) 
K-12 W1863 (is recA+) + ccdB induction, t=60 minDNA damage-0.228.860.16Faith JJ, et al. (2007) 
K-12 W1863 (is recA+) + ccdB induction, t=90 minDNA damage-0.208.870.07Faith JJ, et al. (2007) 
K-12 MG1063 (is recA56) + lacZ induction, t=120 minOverexpression-0.078.930.01Faith JJ, et al. (2007) 
K-12 MG1063 (is recA56) + ccdB induction, t=120 minDNA damage-0.308.820.06Faith JJ, et al. (2007) 
K-12 EMG2, LB Glucose (0.2%), t=2.5 hr post-inoc., rep. 1LB Glucose0.209.060.31Faith JJ, et al. (2007) 
K-12 EMG2, LB Glucose (0.2%), t=3.0 hr post-inoc., rep. 1LB Glucose0.169.040.12Faith JJ, et al. (2007) 
K-12 EMG2, LB Glucose (0.2%), t=3.5 hr post-inoc., rep. 1LB Glucose0.249.090.30Faith JJ, et al. (2007) 
K-12 EMG2, LB Glucose (0.2%), t=4.0 hr post-inoc., rep. 1LB Glucose0.199.060.26Faith JJ, et al. (2007) 
K-12 EMG2, LB Glucose (0.2%), t=4.5 hr post-inoc., rep. 1LB Glucose0.339.130.50Faith JJ, et al. (2007) 
K-12 EMG2, LB Glucose (0.2%), t=5.0 hr post-inoc., rep. 1LB Glucose-0.168.890.07Faith JJ, et al. (2007) 
K-12 EMG2, LB Glucose (0.2%), t=5.5 hr post-inoc., rep. 1LB Glucose-0.288.820.41Faith JJ, et al. (2007) 
K-12 EMG2, LB Glucose (0.2%), t=6.0 hr post-inoc., rep. 1LB Glucose-0.188.880.17Faith JJ, et al. (2007) 
K-12 EMG2, LB Glucose (0.2%), t=8.0 hr post-inoc., rep. 1LB Glucose-0.138.900.10Faith JJ, et al. (2007) 
K-12 EMG2, LB Glucose (0.4%), t=2.5 hr post-inoc., rep. 1LB Glucose0.309.110.49Faith JJ, et al. (2007) 
K-12 EMG2, LB Glucose (0.4%), t=3.0 hr post-inoc., rep. 1LB Glucose0.149.040.42Faith JJ, et al. (2007) 
K-12 EMG2, LB Glucose (0.4%), t=3.5 hr post-inoc., rep. 1LB Glucose0.439.180.73Faith JJ, et al. (2007) 
K-12 EMG2, LB Glucose (0.4%), t=4.0 hr post-inoc., rep. 1LB Glucose0.339.130.44Faith JJ, et al. (2007) 
K-12 EMG2, LB Glucose (0.4%), t=4.5 hr post-inoc., rep. 1LB Glucose0.079.000.03Faith JJ, et al. (2007) 
K-12 EMG2, LB Glucose (0.4%), t=5.0 hr post-inoc., rep. 1LB Glucose-0.428.750.55Faith JJ, et al. (2007) 
K-12 EMG2, LB Glucose (0.4%), t=5.5 hr post-inoc., rep. 1LB Glucose-0.308.820.42Faith JJ, et al. (2007) 
K-12 EMG2, LB Glucose (0.4%), t=6.0 hr post-inoc., rep. 1LB Glucose-0.348.800.49Faith JJ, et al. (2007) 
K-12 EMG2, LB Glucose (0.4%), t=8.0 hr post-inoc., rep. 1LB Glucose-0.498.720.52Faith JJ, et al. (2007) 
K-12 BW25113, 15 h biofilm (glass wool)Biofilm + Parental strain0.078.420.03Ma Q and Wood TK (2009) 
K-12 BW25113, 15 h biofilm (polystyrene), rep. 2Biofilm + Parental strain-0.0011.180.60Ma Q and Wood TK (2009) 
K-12 BW25113 ompA(del)::kan, 15 h biofilm (polystyrene), rep. 2Biofilm + Mutant0.0111.190.11Ma Q and Wood TK (2009) 
MG1655 wt, Ile starved, repl1Stringent response - control0.689.731.17Traxler MF, et al. (2008) 
MG1655 wt, Ile starved, repl2Stringent response - control0.569.660.96Unpublished Experiment Set: 5126 
MG1655 wt, Ile starved, 340 minStringent response - time course0.139.450.72Traxler MF, et al. (2011) 
MG1655 wt, Ile starved, 370 minStringent response - time course0.309.540.65Unpublished Experiment Set: 5126 
MG1655 wt, Ile starved, 380 minStringent response - time course0.109.440.28Traxler MF, et al. (2011) 
MG1655 wt, Ile starved, 390 minStringent response - time course-0.089.340.11Traxler MF, et al. (2008) 
MG1655 wt, Ile starved, 395 minStringent response - time course0.149.460.39Traxler MF, et al. (2011) 
MG1655 wt, Ile starved, 400 minStringent response - time course-0.059.360.34Traxler MF, et al. (2011) 
MG1655 wt, Ile starved, 410 minStringent response - time course0.059.410.40Traxler MF, et al. (2008) 
MG1655 wt, Ile starved, 420 minStringent response - time course-0.569.110.56Traxler MF, et al. (2011) 
MG1655 wt, Ile starved, 430 minStringent response - time course-0.229.270.24Traxler MF, et al. (2008) 
MG1655 wt, Ile starved, 445 minStringent response - time course-0.858.961.16Traxler MF, et al. (2008) 
K-12 W3110 RhsA overexpression control, t=0 h; biol. rep. 1, tech. rep. 1Overexpression - control0.2210.950.26Aggarwal K and Lee KH (2011) 
MG1655 wt, Ile starved, 460 minStringent response - time course-0.349.210.25Traxler MF, et al. (2011) 
K-12 W3110 RhsA overexpression control, t=0 h; biol. rep. 2, tech. rep. 1Overexpression - control0.1910.940.26Aggarwal K and Lee KH (2011) 
MG1655 wt, Ile starved, 493 minStringent response - time course-0.779.000.79Unpublished Experiment Set: 5126 
K-12 W3110 RhsA overexpression control, t=1.5 h; biol. rep. 1, tech. rep. 1Overexpression - control-0.2310.730.34Aggarwal K and Lee KH (2011) 
K-12 W3110 RhsA overexpression control, t=3.5 h; biol. rep. 1, tech. rep. 1Overexpression - control-0.0610.810.01Aggarwal K and Lee KH (2011) 
K-12 W3110 RhsA overexpression control, t=3.5 h; biol. rep. 2, tech. rep. 1Overexpression - control-0.2310.730.08Aggarwal K and Lee KH (2011) 
K-12 W3110 RhsA overexpression (low IPTG), t=1.5 h; biol. rep. 1, tech. rep. 1Overexpression-0.0810.800.22Aggarwal K and Lee KH (2011) 
K-12 W3110 RhsA overexpression (low IPTG), t=1.5 h; biol. rep. 2, tech. rep. 1Overexpression-0.0410.820.17Aggarwal K and Lee KH (2011) 
K-12 W3110 RhsA overexpression (low IPTG), t=3.5 h; biol. rep. 1, tech. rep. 1Overexpression-0.1710.760.32Aggarwal K and Lee KH (2011) 
K-12 W3110 RhsA overexpression (low IPTG), t=3.5 h; biol. rep. 2, tech. rep. 1Overexpression-0.0410.820.30Aggarwal K and Lee KH (2011) 
K-12 W3110 RhsA overexpression (high IPTG), t=1.5 h; biol. rep. 1, tech. rep. 1Overexpression-0.1610.760.34Aggarwal K and Lee KH (2011) 
K-12 W3110 RhsA overexpression (high IPTG), t=1.5 h; biol. rep. 2, tech. rep. 1Overexpression0.1810.930.46Aggarwal K and Lee KH (2011) 
K-12 W3110 RhsA overexpression (high IPTG), t=3.5 h; biol. rep. 1, tech. rep. 1Overexpression0.1210.900.10Aggarwal K and Lee KH (2011) 
K-12 W3110 RhsA overexpression (high IPTG), t=3.5 h; biol. rep. 2, tech. rep. 1Overexpression0.1710.930.51Aggarwal K and Lee KH (2011) 
K-12 MG1655, HCl added to stationary phase culture, t=3 h, rep. 1Acidic medium0.274.830.50King T, et al. (2010) 
K-12 MG1655, HCl added to stationary phase culture, t=0 h, rep. 1Acidic medium - Control-0.484.450.56King T, et al. (2010) 
K-12 MG1655, HCl added to stationary phase culture, t=3 h, rep. 4Acidic medium-0.354.520.65King T, et al. (2010) 
K-12 MG1655, Lactic Acid added to stationary phase culture, t=0 h, rep. 1Acidic medium - Control-0.564.420.62King T, et al. (2010) 
K-12 MG1655, Lactic Acid added to stationary phase culture, t=3 h, rep. 1Acidic medium-0.344.520.43King T, et al. (2010) 
K-12 MG1655, Lactic Acid added to stationary phase culture, t=3 h, rep. 2Acidic medium-0.404.490.84King T, et al. (2010) 
K-12 MG1655, Lactic Acid added to stationary phase culture, t=0 h, rep. 3Acidic medium - Control0.044.720.12King T, et al. (2010) 
K-12 MG1655, Lactic Acid added to stationary phase culture, t=3 h, rep. 3Acidic medium-0.184.600.22King T, et al. (2010) 
K-12 MG1655, Lactic Acid added to stationary phase culture, t=0 h, rep. 4Acidic medium - Control1.095.242.02King T, et al. (2010) 
K-12 MG1655, Lactic Acid added to stationary phase culture, t=3 h, rep. 4Acidic medium0.124.750.51King T, et al. (2010) 
K-12 MG1655, Acetic Acid added to stationary phase culture, t=0 h, rep. 2Acidic medium - Control-0.084.650.26King T, et al. (2010) 
K-12 MG1655(phage N15): linear genome-controlLinear chromosome - control-0.009.410.23Cui T, et al. (2007) 
K-12 MG1655 tos-kan: linear genome-controlLinear chromosome - control0.169.490.35Cui T, et al. (2007) 
K-12 MG1655(phage N15) tos-kan: linear genomeLinear chromosome-0.179.330.59Cui T, et al. (2007) 
K-12 F+ Lambda+, planktonic exponential phase, rep. 2Exponential phase0.326.560.79May T, et al. (2009)Gene Profile
K-12 F+ Lambda+, planktonic stationary phase, rep. 2Stationary phase0.066.430.34May T, et al. (2009)Gene Profile
K-12 MG1655, 48 h biofilm, rep. 1Biofilm-0.596.100.61May T, et al. (2009)Gene Profile
K-12 MG1655, 48 h biofilm, rep. 2Biofilm-0.636.090.08May T, et al. (2009)Gene Profile
K-12 TG1 expressing TOM-Green/IsoILR1/GSHI* + cis-DCE, rep. 1cis-DCE + Mutant-0.7910.020.62Lee J, et al. (2010)Gene Profile
K-12 MG1655, planktonic exponential phase, rep. 1Exponential phase0.056.430.16May T, et al. (2009)Gene Profile
K-12 TG1 with plasmid vectors + cis-DCE, rep. 1cis-DCE-0.929.960.88Lee J, et al. (2010)Gene Profile
K-12 TG1 expressing TOM-Green/EchA F108L/I219L/C248I + cis-DCEcis-DCE + Mutant0.025.220.10Lee J, et al. (2010)Gene Profile
K-12 MG1655, planktonic exponential phase, rep. 2Exponential phase0.396.600.80May T, et al. (2009)Gene Profile
K-12 TG1 expressing TOM-Green + cis-DCEcis-DCE + Mutant-0.025.200.01Lee J, et al. (2010)Gene Profile
K-12 MG1655, planktonic exponential phase, rep. 3Exponential phase0.426.610.79May T, et al. (2009)Gene Profile
K-12 BW25113 + waterHydrogen Peroxide - Control0.5510.690.87Lee J, et al. (2010)Gene Profile
K-12 MG1655 pBR322, 48 h biofilm, rep. 1Biofilm-0.216.300.12May T, et al. (2009)Gene Profile
K-12 BW25113 + H2O2Hydrogen Peroxide0.1210.470.27Lee J, et al. (2010)Gene Profile
K-12 MG1655 pBR322, 48 h biofilm, rep. 2Biofilm-0.056.370.24May T, et al. (2009)Gene Profile
K-12 BW25113 ygiW(del) + waterHydrogen Peroxide - Control0.6410.740.88Lee J, et al. (2010)Gene Profile
K-12 BW25113 ychH(del) + waterHydrogen Peroxide - Control0.1410.490.32Lee J, et al. (2010)Gene Profile
K-12 MG1655, planktonic stationary phase, rep. 1Stationary phase-0.196.300.04May T, et al. (2009)Gene Profile
K-12 BW25113 ygiW(del) + H2O2Hydrogen Peroxide0.1410.490.29Lee J, et al. (2010)Gene Profile
K-12 BW25113 ychH(del) + H2O2Hydrogen Peroxide-0.4310.200.41Lee J, et al. (2010)Gene Profile
K-12 TG1 expressing TOM-Green/IsoILR1/GSHI* + cis-DCE, rep. 2cis-DCE + Mutant-0.0610.390.33Lee J, et al. (2010)Gene Profile
K-12 TG1 with plasmid vectors + cis-DCE, rep. 2cis-DCE-0.2010.320.14Lee J, et al. (2010)Gene Profile
K-12 MG1655 lacIq + pBRplac (vector control), rep. 1Overexpression - control0.0710.180.44Beisel CL and Storz G (2011)Gene Profile
K-12 MG1655 lacIq + pBRplac-Spot42, rep. 1Overexpression0.2510.270.95Beisel CL and Storz G (2011)Gene Profile
K-12 MG1655 lacIq + pBRplac (vector control), rep. 2Overexpression - control-0.2410.030.79Beisel CL and Storz G (2011)Gene Profile
K-12 MG1655 lacIq + pBRplac-Spot42, rep. 2Overexpression-0.2310.040.37Beisel CL and Storz G (2011)Gene Profile
K-12 MG1655 lacIq + pBRplac (vector control), rep. 3Overexpression - control0.0510.180.22Beisel CL and Storz G (2011)Gene Profile
K-12 MG1655 lacIq + pBRplac-Spot42, rep. 3Overexpression0.0510.170.33Beisel CL and Storz G (2011)Gene Profile
BW25113, OD600=1.0 in DMEMWild type vs Mutant0.249.200.45Habdas BJ, et al. (2010) 
BW25113 qseD(del), OD600=1.0 in DMEMWild type vs Mutant0.089.120.30Habdas BJ, et al. (2010) 
BW25113, OD600=1.0 in LBWild type vs Mutant-0.868.650.63Habdas BJ, et al. (2010) 
BW25113 qseD(del), OD600=1.0 in LBWild type vs Mutant0.279.220.48Habdas BJ, et al. (2010) 
K-12 BW25113 hha(del) hns(del) + H-NS overexpressionBiofilm + Mutant-0.149.510.35Hong SH, et al. (2010) 
K-12 BW25113 hha(del) hns(del) + H-NS K57N overexpressionBiofilm + Mutant0.129.650.44Hong SH, et al. (2010) 
K-12 MG1655 rpoC(del 3132..3158), rep. 1Wild type vs Mutant0.149.010.52Conrad TM, et al. (2010) 
K-12 MG1655 rpoC(del 3132..3158), rep. 2Wild type vs Mutant0.169.020.55Conrad TM, et al. (2010) 
K-12 MG1655 rpoC(del 3132..3158), rep. 3Wild type vs Mutant0.309.090.63Conrad TM, et al. (2010) 
K-12 MG1655 rpoC(del 3120..3143), rep. 1Wild type vs Mutant-0.088.900.23Conrad TM, et al. (2010) 
K-12 MG1655 rpoC(del 3120..3143), rep. 2Wild type vs Mutant-0.178.850.08Conrad TM, et al. (2010) 
K-12 MG1655 rpoC(del 3120..3143), rep. 3Wild type vs Mutant0.249.060.60Conrad TM, et al. (2010) 
K-12 MG1655 rpoC(del 3611..3619), rep. 1Wild type vs Mutant-0.028.920.09Conrad TM, et al. (2010) 
K-12 MG1655 rpoC(del 3611..3619), rep. 2Wild type vs Mutant-0.088.900.00Conrad TM, et al. (2010) 
K-12 MG1655 rpoC(del 3611..3619), rep. 3Wild type vs Mutant-0.088.900.00Conrad TM, et al. (2010) 
K-12 MG1655, rep. 1Wild type vs Mutant-0.108.880.22Conrad TM, et al. (2010) 
K-12 MG1655, rep. 2Wild type vs Mutant-0.248.820.36Conrad TM, et al. (2010) 
K-12 MG1655, rep. 3Wild type vs Mutant-0.218.830.31Conrad TM, et al. (2010) 
K-12 MG1655, Biofilm-attachment stage, rep. 1Biofilm + Time course0.157.850.61Ito A, et al. (2009) 
K-12 MG1655, Biofilm-attachment stage, rep. 2Biofilm + Time course0.387.960.94Ito A, et al. (2009) 
K-12 MG1655, Biofilm-attachment stage, rep. 3Biofilm + Time course0.387.960.85Ito A, et al. (2009) 
K-12 MG1655, Biofilm-colony stage, rep. 1Biofilm + Time course0.147.840.48Ito A, et al. (2009) 
K-12 MG1655, Biofilm-colony stage, rep. 2Biofilm + Time course0.137.840.48Ito A, et al. (2009) 
K-12 MG1655, Biofilm-colony stage, rep. 3Biofilm + Time course0.167.850.55Ito A, et al. (2009) 
K-12 MG1655, Planktonic cells in exponential phase, rep. 1Exponential phase0.127.830.49Ito A, et al. (2009) 
K-12 MG1655, Planktonic cells in exponential phase, rep. 2Exponential phase-0.047.750.29Ito A, et al. (2009) 
O157:H7 CL56 after infection of HEp-2 epithelial cells, rep. 2Epithelial cell infection-0.045.020.71Jandu N, et al. (2009) 
K-12 MG1655, Planktonic cells in exponential phase, rep. 3Exponential phase-0.047.750.31Ito A, et al. (2009) 
K-12 MG1655, Biofilm-maturation stage, rep. 1Biofilm + Time course-0.667.440.84Ito A, et al. (2009) 
K-12 MG1655, Biofilm-maturation stage, rep. 2Biofilm + Time course-0.437.560.42Ito A, et al. (2009) 
K-12 MG1655, Biofilm-maturation stage, rep. 3Biofilm + Time course-0.807.370.85Ito A, et al. (2009) 
O157:H7 CL56 - minimal medium + CO2 (5%), rep. 4Minimal media0.045.060.08Jandu N, et al. (2009) 
K-12 BW25113 + Nalidixic acid (Nalidixic acid-0.0711.040.86Wang X, et al. (2010) 
K-12 BW25113 untreatedNalidixic acid, Azlocillin - control0.1311.131.22Wang X, et al. (2010) 
K-12 BW25113 + Azlocillin (Azlocillin-0.0711.040.94Wang X, et al. (2010) 
K-12 MG1655 ppGpp0 + overexpression control, rep. 1Overexpression - control0.276.390.62Vinella D, et al. (2012) 
K-12 MG1655 ppGpp0 + overexpression control, rep. 2Overexpression - control0.256.380.68Vinella D, et al. (2012) 
K-12 MG1655 ppGpp0 + GreA overexpression, rep. 1Overexpression0.216.360.52Vinella D, et al. (2012) 
K-12 MG1655 ppGpp0 + GreA overexpression, rep. 2Overexpression0.216.360.57Vinella D, et al. (2012) 
K-12 MG1655 ppGpp0 + GreB overexpression, rep. 1Overexpression0.306.410.88Vinella D, et al. (2012) 
K-12 MG1655 ppGpp0 + GreB overexpression, rep. 2Overexpression0.376.441.05Vinella D, et al. (2012) 
K-12 MG1655 ppGpp0 dksA(del)::kan + overexpression control, rep. 1Overexpression - control0.026.270.22Vinella D, et al. (2012) 
K-12 MG1655 ppGpp0 dksA(del)::kan + overexpression control, rep. 2Overexpression - control0.146.330.43Vinella D, et al. (2012) 
K-12 MG1655 ppGpp0 dksA(del)::kan + GreA overexpression, rep. 1Overexpression-0.855.831.44Vinella D, et al. (2012) 
K-12 MG1655 ppGpp0 dksA(del)::kan + GreA overexpression, rep. 2Overexpression-0.955.781.57Vinella D, et al. (2012) 
K-12 MG1655 ppGpp0 dksA(del)::kan + GreB overexpression, rep. 1Overexpression-0.216.150.40Vinella D, et al. (2012) 
K-12 MG1655 ppGpp0 dksA(del)::kan + GreB overexpression, rep. 2Overexpression-0.486.020.95Vinella D, et al. (2012) 
relA(del) 966 min, rep 1Diauxic shift - mutant0.017.720.07Traxler MF, et al. (2006)Gene Profile
relA(del) 966 min, rep 2Diauxic shift - mutant0.188.560.31Traxler MF, et al. (2006)Gene Profile
relA(del) 966 min, rep 3Diauxic shift - mutant-0.298.240.34Traxler MF, et al. (2006)Gene Profile
relA(del) 955 min, rep 1Diauxic shift - mutant-0.127.720.24Traxler MF, et al. (2006)Gene Profile
relA(del) 955 min, rep 2Diauxic shift - mutant0.138.390.05Traxler MF, et al. (2006)Gene Profile
relA(del) 955 min, rep 3Diauxic shift - mutant0.247.550.20Traxler MF, et al. (2006)Gene Profile
relA(del) 945 min, rep 1Diauxic shift - mutant-0.126.940.06Traxler MF, et al. (2006)Gene Profile
relA(del) 945 min, rep 2Diauxic shift - mutant-0.076.920.07Traxler MF, et al. (2006)Gene Profile
relA(del) 945 min, rep 3Diauxic shift - mutant-0.107.670.09Traxler MF, et al. (2006)Gene Profile
relA(del) 935 min, rep 1Diauxic shift - mutant-0.107.250.10Traxler MF, et al. (2006)Gene Profile
relA(del) 935 min, rep 2Diauxic shift - mutant0.347.710.43Traxler MF, et al. (2006)Gene Profile
relA(del) 935 min, rep 3Diauxic shift - mutant-0.425.340.18Traxler MF, et al. (2006)Gene Profile
relA(del) 925 min, rep 1Diauxic shift - mutant0.156.950.23Traxler MF, et al. (2006)Gene Profile
relA(del) 925 min, rep 2Diauxic shift - mutant0.047.350.09Traxler MF, et al. (2006)Gene Profile
relA(del) 925 min, rep 3Diauxic shift - mutant0.047.410.01Traxler MF, et al. (2006)Gene Profile
relA(del) 916 min, rep 1Diauxic shift - mutant-0.157.730.19Traxler MF, et al. (2006)Gene Profile
relA(del) 916 min, rep 2Diauxic shift - mutant0.387.880.55Traxler MF, et al. (2006)Gene Profile
relA(del) 916 min, rep 3Diauxic shift - mutant-0.036.520.09Traxler MF, et al. (2006)Gene Profile
relA(del) 909 min, rep 1Diauxic shift - mutant-0.606.780.69Traxler MF, et al. (2006)Gene Profile
relA(del) 909 min, rep 2Diauxic shift - mutant0.407.440.43Traxler MF, et al. (2006)Gene Profile
relA(del) 909 min, rep 3Diauxic shift - mutant0.087.490.13Traxler MF, et al. (2006)Gene Profile
relA(del) 896 min, rep 1Diauxic shift - mutant0.195.680.29Traxler MF, et al. (2006)Gene Profile
relA(del) 896 min, rep 2Diauxic shift - mutant0.138.790.21Traxler MF, et al. (2006)Gene Profile
relA(del) 896 min, rep 3Diauxic shift - mutant0.188.120.31Traxler MF, et al. (2006)Gene Profile
relA(del) 865 min, rep 1Diauxic shift - mutant0.228.970.40Traxler MF, et al. (2006)Gene Profile
relA(del) 865 min, rep 2Diauxic shift - mutant0.238.850.42Traxler MF, et al. (2006)Gene Profile
relA(del) 865 min, rep 3Diauxic shift - mutant0.156.930.23Traxler MF, et al. (2006)Gene Profile
relA(del) 832 min, rep 1Diauxic shift - mutant0.297.290.45Traxler MF, et al. (2006)Gene Profile
relA(del) 832 min, rep 2Diauxic shift - mutant-0.017.020.07Traxler MF, et al. (2006)Gene Profile
relA(del) 832 min, rep 3Diauxic shift - mutant-0.486.540.64Traxler MF, et al. (2006)Gene Profile
crp(del) 450 min, rep 1Diauxic shift - mutant0.155.690.20Traxler MF, et al. (2006)Gene Profile
crp(del) 450 min, rep 2Diauxic shift - mutant0.038.140.01Traxler MF, et al. (2006)Gene Profile
crp(del) 450 min, rep 3Diauxic shift - mutant0.287.930.47Traxler MF, et al. (2006)Gene Profile
crp(del) 450 min, rep 4Diauxic shift - mutant0.276.930.39Traxler MF, et al. (2006)Gene Profile
crp(del) 420 min, rep 1Diauxic shift - mutant0.536.150.79Traxler MF, et al. (2006)Gene Profile
crp(del) 420 min, rep 2Diauxic shift - mutant0.336.360.57Traxler MF, et al. (2006)Gene Profile
crp(del) 420 min, rep 3Diauxic shift - mutant0.567.190.78Traxler MF, et al. (2006)Gene Profile
crp(del) 420 min, rep 4Diauxic shift - mutant0.226.920.52Traxler MF, et al. (2006)Gene Profile
crp(del) 405 min, rep 1Diauxic shift - mutant0.216.570.40Traxler MF, et al. (2006)Gene Profile
crp(del) 405 min, rep 2Diauxic shift - mutant-0.076.010.12Traxler MF, et al. (2006)Gene Profile
crp(del) 405 min, rep 3Diauxic shift - mutant0.026.200.02Traxler MF, et al. (2006)Gene Profile
crp(del) 405 min, rep 4Diauxic shift - mutant-0.179.090.39Traxler MF, et al. (2006)Gene Profile
crp(del) 250 min, rep 1Diauxic shift - mutant-0.788.190.96Traxler MF, et al. (2006)Gene Profile
crp(del) 250 min, rep 2Diauxic shift - mutant-0.156.160.43Traxler MF, et al. (2006)Gene Profile
crp(del) 250 min, rep 3Diauxic shift - mutant0.107.210.20Traxler MF, et al. (2006)Gene Profile
crp(del) 250 min, rep 4Diauxic shift - mutant-0.317.560.55Traxler MF, et al. (2006)Gene Profile
rpoS(del) 330 min, rep 1Diauxic shift - mutant0.175.820.20Traxler MF, et al. (2006)Gene Profile
rpoS(del) 330 min, rep 2Diauxic shift - mutant0.506.350.43Traxler MF, et al. (2006)Gene Profile
rpoS(del) 330 min, rep 3Diauxic shift - mutant0.526.620.42Traxler MF, et al. (2006)Gene Profile
rpoS(del) 315 min, rep 1Diauxic shift - mutant0.586.051.09Traxler MF, et al. (2006)Gene Profile
rpoS(del) 315 min, rep 2Diauxic shift - mutant0.695.740.93Traxler MF, et al. (2006)Gene Profile
rpoS(del) 315 min, rep 3Diauxic shift - mutant0.115.000.29Traxler MF, et al. (2006)Gene Profile
rpoS(del) 290 min, rep 1Diauxic shift - mutant0.245.520.47Traxler MF, et al. (2006)Gene Profile
rpoS(del) 290 min, rep 2Diauxic shift - mutant0.255.830.50Traxler MF, et al. (2006)Gene Profile
rpoS(del) 290 min, rep 3Diauxic shift - mutant0.095.790.21Traxler MF, et al. (2006)Gene Profile
rpoS(del) 250 min, rep 1Diauxic shift - mutant0.285.470.60Traxler MF, et al. (2006)Gene Profile
rpoS(del) 250 min, rep 2Diauxic shift - mutant0.256.010.51Traxler MF, et al. (2006)Gene Profile
rpoS(del) 250 min, rep 3Diauxic shift - mutant0.265.330.55Traxler MF, et al. (2006)Gene Profile
rpoS(del) 220 min, rep 1Diauxic shift - mutant-0.045.270.01Traxler MF, et al. (2006)Gene Profile
rpoS(del) 220 min, rep 2Diauxic shift - mutant0.436.070.67Traxler MF, et al. (2006)Gene Profile
rpoS(del) 220 min, rep 3Diauxic shift - mutant0.305.510.53Traxler MF, et al. (2006)Gene Profile
rpoS(del) 210 min, rep 1Diauxic shift - mutant0.126.650.14Traxler MF, et al. (2006)Gene Profile
rpoS(del) 210 min, rep 2Diauxic shift - mutant0.235.670.39Traxler MF, et al. (2006)Gene Profile
rpoS(del) 210 min, rep 3Diauxic shift - mutant0.216.680.32Traxler MF, et al. (2006)Gene Profile
rpoS(del) 200 min, rep 1Diauxic shift - mutant-0.116.180.24Traxler MF, et al. (2006)Gene Profile
rpoS(del) 200 min, rep 2Diauxic shift - mutant0.055.930.05Traxler MF, et al. (2006)Gene Profile
rpoS(del) 200 min, rep 3Diauxic shift - mutant-0.256.870.50Traxler MF, et al. (2006)Gene Profile
rpoS(del) 190 min, rep 1Diauxic shift - mutant0.486.370.68Traxler MF, et al. (2006)Gene Profile
rpoS(del) 190 min, rep 2Diauxic shift - mutant0.055.750.02Traxler MF, et al. (2006)Gene Profile
rpoS(del) 190 min, rep 3Diauxic shift - mutant-0.064.780.15Traxler MF, et al. (2006)Gene Profile
rpoS(del) 180 min, rep 1Diauxic shift - mutant0.235.610.38Traxler MF, et al. (2006)Gene Profile
rpoS(del) 180 min, rep 2Diauxic shift - mutant0.146.180.23Traxler MF, et al. (2006)Gene Profile
rpoS(del) 180 min, rep 3Diauxic shift - mutant0.305.280.47Traxler MF, et al. (2006)Gene Profile
rpoS(del) 170 min, rep 1Diauxic shift - mutant-0.206.630.37Traxler MF, et al. (2006)Gene Profile
rpoS(del) 170 min, rep 2Diauxic shift - mutant0.317.060.48Traxler MF, et al. (2006)Gene Profile
rpoS(del) 170 min, rep 3Diauxic shift - mutant0.496.430.79Traxler MF, et al. (2006)Gene Profile
rpoS(del) 160 min, rep 1Diauxic shift - mutant-0.496.490.57Traxler MF, et al. (2006)Gene Profile
rpoS(del) 160 min, rep 2Diauxic shift - mutant-0.085.740.13Traxler MF, et al. (2006)Gene Profile
rpoS(del) 160 min, rep 3Diauxic shift - mutant-0.016.310.02Traxler MF, et al. (2006)Gene Profile
rpoS(del) 150 min, rep 1Diauxic shift - mutant-0.015.210.11Traxler MF, et al. (2006)Gene Profile
rpoS(del) 150 min, rep 2Diauxic shift - mutant0.216.020.48Traxler MF, et al. (2006)Gene Profile
rpoS(del) 150 min, rep 3Diauxic shift - mutant0.136.260.25Traxler MF, et al. (2006)Gene Profile
rpoS(del) 120 min, rep 1Diauxic shift - mutant-0.246.480.57Traxler MF, et al. (2006)Gene Profile
rpoS(del) 120 min, rep 2Diauxic shift - mutant-0.116.170.32Traxler MF, et al. (2006)Gene Profile
rpoS(del) 120 min, rep 3Diauxic shift - mutant0.256.650.48Traxler MF, et al. (2006)Gene Profile
wt 1089 min, rep 1Diauxic shift - wt-0.474.410.54Traxler MF, et al. (2006)Gene Profile
wt 1089 min, rep 2Diauxic shift - wt0.096.700.17Traxler MF, et al. (2006)Gene Profile
wt 1089 min, rep 3Diauxic shift - wt-0.645.560.67Traxler MF, et al. (2006)Gene Profile
wt 1070 min, rep 1Diauxic shift - wt-0.104.580.11Traxler MF, et al. (2006)Gene Profile
wt 1070 min, rep 2Diauxic shift - wt0.155.040.15Traxler MF, et al. (2006)Gene Profile
wt 1070 min, rep 3Diauxic shift - wt0.614.900.45Traxler MF, et al. (2006)Gene Profile
wt 1049 min, rep 1Diauxic shift - wt-4.294.934.22Traxler MF, et al. (2006)Gene Profile
wt 1049 min, rep 2Diauxic shift - wt0.445.570.55Traxler MF, et al. (2006)Gene Profile
wt 1049 min, rep 3Diauxic shift - wt0.435.110.52Traxler MF, et al. (2006)Gene Profile
wt 1035 min, rep 1Diauxic shift - wt0.395.160.64Traxler MF, et al. (2006)Gene Profile
wt 1035 min, rep 2Diauxic shift - wt0.245.080.38Traxler MF, et al. (2006)Gene Profile
wt 1035 min, rep 3Diauxic shift - wt0.254.970.37Traxler MF, et al. (2006)Gene Profile
wt 999 min, rep 1Diauxic shift - wt0.065.430.10Traxler MF, et al. (2006)Gene Profile
wt 999 min, rep 2Diauxic shift - wt0.025.170.01Traxler MF, et al. (2006)Gene Profile
wt 999 min, rep 3Diauxic shift - wt0.285.900.55Traxler MF, et al. (2006)Gene Profile
wt 969 min, rep 1Diauxic shift - wt-0.194.750.44Traxler MF, et al. (2006)Gene Profile
wt 969 min, rep 2Diauxic shift - wt0.055.670.05Traxler MF, et al. (2006)Gene Profile
wt 969 min, rep 3Diauxic shift - wt0.556.811.13Traxler MF, et al. (2006)Gene Profile
wt 939 min, rep 1Diauxic shift - wt0.426.480.76Traxler MF, et al. (2006)Gene Profile
wt 939 min, rep 2Diauxic shift - wt0.427.830.81Traxler MF, et al. (2006)Gene Profile
wt 939 min, rep 3Diauxic shift - wt0.486.070.92Traxler MF, et al. (2006)Gene Profile
wt 929 min, rep 1Diauxic shift - wt-0.096.600.26Traxler MF, et al. (2006)Gene Profile
wt 929 min, rep 2Diauxic shift - wt0.156.420.26Traxler MF, et al. (2006)Gene Profile
wt 929 min, rep 3Diauxic shift - wt0.026.380.02Traxler MF, et al. (2006)Gene Profile
wt 919 min, rep 1Diauxic shift - wt-0.015.430.05Traxler MF, et al. (2006)Gene Profile
wt 919 min, rep 2Diauxic shift - wt-0.264.640.52Traxler MF, et al. (2006)Gene Profile
wt 919 min, rep 3Diauxic shift - wt0.055.360.01Traxler MF, et al. (2006)Gene Profile
wt 908 min, rep 1Diauxic shift - wt0.055.300.02Traxler MF, et al. (2006)Gene Profile
wt 908 min, rep 2Diauxic shift - wt-0.285.840.59Traxler MF, et al. (2006)Gene Profile
wt 908 min, rep 3Diauxic shift - wt-0.155.910.37Traxler MF, et al. (2006)Gene Profile
wt 898 min, rep 1Diauxic shift - wt-0.255.800.45Traxler MF, et al. (2006)Gene Profile
wt 898 min, rep 2Diauxic shift - wt-0.406.220.62Traxler MF, et al. (2006)Gene Profile
wt 898 min, rep 3Diauxic shift - wt0.046.520.02Traxler MF, et al. (2006)Gene Profile
wt 888 min, rep 1Diauxic shift - wt-0.135.550.16Traxler MF, et al. (2006)Gene Profile
wt 888 min, rep 2Diauxic shift - wt-0.335.530.41Traxler MF, et al. (2006)Gene Profile
wt 888 min, rep 3Diauxic shift - wt-0.234.580.23Traxler MF, et al. (2006)Gene Profile
wt 878 min, rep 1Diauxic shift - wt0.195.040.26Traxler MF, et al. (2006)Gene Profile
wt 878 min, rep 2Diauxic shift - wt0.155.540.15Traxler MF, et al. (2006)Gene Profile
wt 878 min, rep 3Diauxic shift - wt0.135.580.15Traxler MF, et al. (2006)Gene Profile
wt 869 min, rep 1Diauxic shift - wt0.235.440.43Traxler MF, et al. (2006)Gene Profile
wt 869 min, rep 2Diauxic shift - wt0.205.800.33Traxler MF, et al. (2006)Gene Profile
wt 869 min, rep 3Diauxic shift - wt0.695.671.06Traxler MF, et al. (2006)Gene Profile
wt 861 min, rep 1Diauxic shift - wt0.045.410.07Traxler MF, et al. (2006)Gene Profile
wt 861 min, rep 2Diauxic shift - wt0.306.040.61Traxler MF, et al. (2006)Gene Profile
wt 861 min, rep 3Diauxic shift - wt0.446.730.95Traxler MF, et al. (2006)Gene Profile
wt 830 min, rep 1Diauxic shift - wt0.195.950.39Traxler MF, et al. (2006)Gene Profile
wt 830 min, rep 2Diauxic shift - wt-0.056.140.14Traxler MF, et al. (2006)Gene Profile
wt 830 min, rep 3Diauxic shift - wt0.206.250.35Traxler MF, et al. (2006)Gene Profile
wt 780 min, rep 1Diauxic shift - wt0.206.310.22Traxler MF, et al. (2006)Gene Profile
wt 780 min, rep 2Diauxic shift - wt0.436.210.68Traxler MF, et al. (2006)Gene Profile
wt 780 min, rep 3Diauxic shift - wt0.105.600.13Traxler MF, et al. (2006)Gene Profile
K-12 MG1655 + MnCl2, 60 minMnCl20.089.730.30Waters LS, et al. (2011) 
K-12 MG1655 mntR(del)::FRT + MnCl2, 60 minMnCl2 + mntR(del)0.099.740.39Waters LS, et al. (2011) 
K-12 MG1655 + MnCl2, 10 minMnCl20.309.840.60Waters LS, et al. (2011) 
K-12 MG1655 mntR(del)::FRT + MnCl2, 10 minMnCl2 + mntR(del)-0.649.371.33Waters LS, et al. (2011) 
K-12 BW25113-pCA24N-ghoSOverexpression0.003.370.05Wang X, et al. (2012) 
K-12 BW25113-pCA24NOverexpression - control-0.003.370.03Wang X, et al. (2012) 
K-12 MG1655, exponential phase, rep. 1Methylthiolation - wt-0.013.410.34Strader MB, et al. (2011) 
K-12 MG1655, exponential phase, rep. 2Methylthiolation - wt-0.023.410.44Strader MB, et al. (2011) 
K-12 MG1655 cells rimO(del), exponential phase, rep. 1Methylthiolation - mutant0.003.420.01Strader MB, et al. (2011) 
K-12 MG1655 cells rimO(del), exponential phase, rep. 2Methylthiolation - mutant0.013.420.28Strader MB, et al. (2011) 
K-12 MG1655 cells rimO(del)::Tet, exponential phase, rep. 1Methylthiolation - mutant-0.013.410.39Strader MB, et al. (2011) 
K-12 MG1655 cells rimO(del)::Tet, exponential phase, rep. 2Methylthiolation - mutant0.013.420.19Strader MB, et al. (2011) 
K-12 MG1655 ycaO(del), exponential phase, rep. 1Methylthiolation - mutant0.013.420.27Strader MB, et al. (2011) 
K-12 MG1655 ycaO(del), exponential phase, rep. 2Methylthiolation - mutant0.013.420.28Strader MB, et al. (2011) 
K-12 DH5alpha irrE+ + furfural, rep. 3Furfural0.022.880.22Wang J, et al. (2012) 
K-12 DH5alpha irrE+ + furfural, rep. 2Furfural-0.002.870.04Wang J, et al. (2012) 
K-12 DH5alpha irrE+ + furfural, rep. 1Furfural0.032.890.20Wang J, et al. (2012) 
K-12 DH5alpha irrE furfural-tolerant mutant + furfural, rep. 3Furfural + furfural tolerant mutant-0.012.870.04Wang J, et al. (2012) 
K-12 DH5alpha irrE furfural-tolerant mutant + furfural, rep. 2Furfural + furfural tolerant mutant-0.022.860.15Wang J, et al. (2012) 
K-12 DH5alpha irrE furfural-tolerant mutant + furfural, rep. 1Furfural + furfural tolerant mutant-0.022.860.14Wang J, et al. (2012) 
K-12 BW25113 frdC(del), anaerobiosis in minimal glycerol mediumAnaerobic growth + Parental strain-0.043.210.06Hu H and Wood TK (2010) 
K-12 HW2 (evolved strain), anaerobiosis in minimal glycerol mediumAnaerobic growth + Mutant0.043.240.21Hu H and Wood TK (2010) 
K-12 BW25113 + Stationary phase + Amp (5 ug/ml) for 30 minPersister cells - Stationary phase control0.003.530.25Hong SH, et al. (2012) 
K-12 BW25113 persister cells (H2O2 pretreatment then 20 ug/ml Amp for 5 h)Persister cells0.013.530.51Hong SH, et al. (2012) 
K-12 BW25113 rpoS(del) persister cells (20 ug/ml Amp for 5 h)Persister cells - mutant-0.013.520.16Hong SH, et al. (2012) 
K-12 D31 + polymyxin B, t=60 min, rep. 3Polymyxin B-0.003.240.05Mensa B, et al. (2011) 
K-12 D31 + polymyxin B, t=60 min, rep. 2Polymyxin B0.013.250.22Mensa B, et al. (2011) 
K-12 D31 + polymyxin B, t=60 min, rep. 1Polymyxin B0.003.240.13Mensa B, et al. (2011) 
K-12 D31 + PMX 10070, t = 60 min, rep. 3PMX 100700.003.250.03Mensa B, et al. (2011) 
K-12 D31 + PMX 10070, t = 60 min, rep. 2PMX 10070-0.043.230.58Mensa B, et al. (2011) 
K-12 D31 + PMX 10070, t = 60 min, rep. 1PMX 10070-0.013.240.38Mensa B, et al. (2011) 
K-12 D31 no treatment, t=60 min, rep. 3No treatment-0.013.240.23Mensa B, et al. (2011) 
K-12 D31 no treatment, t=60 min, rep. 2No treatment-0.023.240.49Mensa B, et al. (2011) 
K-12 D31 no treatment, t=60 min, rep. 1No treatment-0.043.220.95Mensa B, et al. (2011) 
K-12 D31 + polymyxin B, t=20 min, rep. 3Polymyxin B0.013.250.18Mensa B, et al. (2011) 
K-12 D31 + polymyxin B, t=20 min, rep. 2Polymyxin B-0.003.240.07Mensa B, et al. (2011) 
K-12 D31 + polymyxin B, t=20 min, rep. 1Polymyxin B-0.013.240.25Mensa B, et al. (2011) 
K-12 D31 + PMX 10070, t = 20 min, rep. 3PMX 100700.013.250.00Mensa B, et al. (2011) 
K-12 D31 + PMX 10070, t = 20 min, rep. 2PMX 100700.003.250.09Mensa B, et al. (2011) 
K-12 D31 + PMX 10070, t = 20 min, rep. 1PMX 100700.013.250.26Mensa B, et al. (2011) 
K-12 D31 no treatment, t=20 min, rep. 3No treatment0.033.260.66Mensa B, et al. (2011) 
K-12 D31 no treatment, t=20 min, rep. 2No treatment0.033.260.53Mensa B, et al. (2011) 
K-12 D31 no treatment, t=20 min, rep. 1No treatment0.043.260.82Mensa B, et al. (2011) 
K-12 MG1655 (evolved), Minimal glycerol medium, rep. 3Minimal glycerol media + Mutant0.003.380.11Nam H, et al. (2012) 
K-12 MG1655 (evolved), Minimal glycerol medium, rep. 2Minimal glycerol media + Mutant-0.013.370.25Nam H, et al. (2012) 
K-12 MG1655 (evolved), Minimal glycerol medium, rep. 1Minimal glycerol media + Mutant0.023.380.04Nam H, et al. (2012) 
K-12 MG1655 (evolved), Minimal propylene glycol medium, rep. 3Minimal propylene glycol media + Mutant0.013.380.27Nam H, et al. (2012) 
K-12 MG1655 (evolved), Minimal propylene glycol medium, rep. 2Minimal propylene glycol media + Mutant-0.033.360.42Nam H, et al. (2012) 
K-12 MG1655 (evolved), Minimal propylene glycol medium, rep. 1Minimal propylene glycol media + Mutant0.003.380.18Nam H, et al. (2012) 
K-12 BW25113 + 10 um TPEN (Zn chelator), rep. 3Zinc chelator (TPEN)0.053.310.71Hensley MP, et al. (2012) 
K-12 BW25113 + 10 um TPEN (Zn chelator), rep. 2Zinc chelator (TPEN)-0.033.270.53Hensley MP, et al. (2012) 
K-12 BW25113 + 10 um TPEN (Zn chelator), rep. 1Zinc chelator (TPEN)-0.013.280.21Hensley MP, et al. (2012) 
K-12 BW25113 cells + no TPEN, rep. 3Zinc chelator (TPEN) - control-0.013.280.15Hensley MP, et al. (2012) 
K-12 BW25113 cells + no TPEN, rep. 2Zinc chelator (TPEN) - control0.033.300.54Hensley MP, et al. (2012) 
K-12 BW25113 cells + no TPEN, rep. 1Zinc chelator (TPEN) - control-0.033.270.53Hensley MP, et al. (2012) 
K-12 JM109 pUCA1501 + glyphosate (200 mM), rep. 3Glyphosphate-0.023.190.63Lu W, et al. (2013) 
K-12 JM109 pUCA1501 + glyphosate (200 mM), rep. 2Glyphosphate-0.063.171.18Lu W, et al. (2013) 
K-12 JM109 pUCA1501 + glyphosate (200 mM), rep. 1Glyphosphate0.003.200.08Lu W, et al. (2013) 
K-12 JM109 pUCA1501 + no glyphosate, rep. 3Glyphosate - control0.053.230.94Lu W, et al. (2013) 
K-12 JM109 pUCA1501 + no glyphosate, rep. 2Glyphosate - control0.013.210.48Lu W, et al. (2013) 
K-12 JM109 pUCA1501 + no glyphosate, rep. 1Glyphosate - control0.013.200.29Lu W, et al. (2013) 
K-12 BW25113 + biofilmBiofilm-0.013.490.49Ma Q, et al. (2011) 
K-12 BW25113 yjgI(del) + biofilmBiofilm + Mutant0.013.490.28Ma Q, et al. (2011) 
K-12 BW25113 in exponential phaseWild type vs Mutant0.033.530.28Kim Y, et al. (2010) 
K-12 BW25113 mqsR(del) in exponential phaseWild type vs Mutant0.033.530.21Kim Y, et al. (2010) 
K-12 BW25113 + msqR overexpression-controlOverexpression - control-0.083.480.90Kim Y, et al. (2010) 
K-12 BW25113 + msqR overexpression (3 h)Overexpression-0.033.500.77Kim Y, et al. (2010) 
K-12 BW25113 + msqR overexpression-control, (15 min)Overexpression - control0.033.530.48Kim Y, et al. (2010) 
K-12 BW25113 + mqsR overexpression (15 min)Overexpression0.023.530.60Kim Y, et al. (2010) 
ABU 83972, urine sample from patient 1, rep. 2urine, isolate-0.072.220.24Roos V and Klemm P (2006) 
ABU 83972, urine sample from patient 3, rep. 3urine, isolate0.072.290.93Roos V and Klemm P (2006) 
K-12 W3110 37C, rep. 1Heat shock - Control-0.003.590.38Murata M, et al. (2011) 
K-12 W3110 37C, rep. 2Heat shock - Control-0.013.590.50Murata M, et al. (2011) 
K-12 W3110 47C, rep. 1Heat shock0.013.600.30Murata M, et al. (2011) 
K-12 W3110 47C, rep. 2Heat shock-0.003.590.10Murata M, et al. (2011) 
K-12 MG1655 purR(del)::FRT, minimal medium + adenine, rep. 2Adenine + Mutant0.013.150.37Cho BK, et al. (2011) 
K-12 MG1655 purR(del)::FRT, minimal medium + adenine, rep. 1Adenine + Mutant-0.013.140.10Cho BK, et al. (2011) 
K-12 MG1655, minimal medium + adenine, rep. 2Adenine-0.013.150.09Cho BK, et al. (2011) 
K-12 MG1655, minimal medium + adenine, rep. 1Adenine0.003.150.12Cho BK, et al. (2011) 
K-12 MG1655 purR(del)::FRT, minimal medium - adenine, rep. 2Minimal media + Mutant0.013.150.07Cho BK, et al. (2011) 
K-12 MG1655 purR(del)::FRT, minimal medium - adenine, rep. 1Minimal media + Mutant0.043.170.41Cho BK, et al. (2011) 
K-12 MG1655, minimal medium - adenine, rep. 2Minimal media-0.033.130.67Cho BK, et al. (2011) 
K-12 MG1655, minimal medium - adenine, rep. 1Minimal media-0.013.140.35Cho BK, et al. (2011) 
UTI 83972, biofilm grown in urine, rep. 3Urine + biofilm-0.042.450.28Hancock V, et al. (2010) 
UPEC CFT073 exponential phase in minimal glucose medium, rep. 2Minimal media-0.052.450.17Hancock V, et al. (2010) 
Nissle 1917 SmR, exponential phase in minimal glucose medium, rep. 1Minimal media0.092.521.32Hancock V, et al. (2010) 
K-12 YA027 (is lacZ::paeR71 r+m+ KmR, lacZ::CmR), rep. 1Parental strain0.043.170.39Asakura Y, et al. (2011) 
K-12 YA027 (is lacZ::paeR71 r+m+ KmR, lacZ::CmR), rep. 2Parental strain-0.103.100.74Asakura Y, et al. (2011) 
K-12 YA027 (is lacZ::paeR71 r+m+ KmR, lacZ::CmR), rep. 3Parental strain-0.033.140.23Asakura Y, et al. (2011) 
K-12 YA074 (is lacZ::paeR7I r-m+ KmR, lacZ::CmR), rep. 1Mutant-0.003.150.02Asakura Y, et al. (2011) 
K-12 YA074 (is lacZ::paeR7I r-m+ KmR, lacZ::CmR), rep. 2Mutant-0.043.130.39Asakura Y, et al. (2011) 
K-12 YA074 (is lacZ::paeR7I r-m+ KmR, lacZ::CmR), rep. 3Mutant-0.103.110.84Asakura Y, et al. (2011) 
K-12 YA105 (is lacZ::paeR7I r-m- KmR, lacZ::CmR), rep. 1Mutant-0.013.150.03Asakura Y, et al. (2011) 
K-12 YA105 (is lacZ::paeR7I r-m- KmR, lacZ::CmR), rep. 2Mutant-0.083.120.83Asakura Y, et al. (2011) 
K-12 YA105 (is lacZ::paeR7I r-m- KmR, lacZ::CmR), rep. 3Mutant-0.053.130.39Asakura Y, et al. (2011) 
K-12 YA027 after 11 serial passages (~70 generations) isolate 3-11-2, rep. 1Evolved strain0.053.180.81Asakura Y, et al. (2011) 
K-12 YA027 after 11 serial passages (~70 generations) isolate 3-11-2, rep. 2Evolved strain0.093.201.12Asakura Y, et al. (2011) 
K-12 YA027 after 11 serial passages (~70 generations) isolate 3-11-4, rep. 1Evolved strain0.083.201.01Asakura Y, et al. (2011) 
K-12 YA027 after 11 serial passages (~70 generations) isolate 3-11-4, rep. 2Evolved strain0.093.200.92Asakura Y, et al. (2011) 
K-12 YA027 after 11 serial passages (~70 generations) isolate 3-11-9, rep. 1Evolved strain0.043.170.35Asakura Y, et al. (2011) 
K-12 YA027 after 11 serial passages (~70 generations) isolate 3-11-9, rep. 2Evolved strain0.033.170.33Asakura Y, et al. (2011) 
K-12 YA027 after 11 serial passages (~70 generations) isolate 3-11-10, rep. 1Evolved strain0.063.180.45Asakura Y, et al. (2011) 
K-12 YA027 after 11 serial passages (~70 generations) isolate 3-11-10, rep. 2Evolved strain0.033.170.28Asakura Y, et al. (2011) 
K-12 YA027 after 84 serial passages (~500 generations) isolate 3-84-2, rep. 1Evolved strain-0.103.100.93Asakura Y, et al. (2011) 
K-12 YA027 after 84 serial passages (~500 generations) isolate 3-84-2, rep. 2Evolved strain-0.113.100.91Asakura Y, et al. (2011) 
K-12 YA027 after 84 serial passages (~500 generations) isolate 3-84-4, rep. 1Evolved strain0.053.180.62Asakura Y, et al. (2011) 
K-12 YA027 after 84 serial passages (~500 generations) isolate 3-84-4, rep. 2Evolved strain0.053.180.45Asakura Y, et al. (2011) 
K-12 YA027 after 84 serial passages (~500 generations) isolate 3-84-4, rep. 3Evolved strain0.013.160.20Asakura Y, et al. (2011) 
K-12 YA027 after 84 serial passages (~500 generations) isolate 3-84-6, rep. 1Evolved strain-0.033.140.35Asakura Y, et al. (2011) 
K-12 YA027 after 84 serial passages (~500 generations) isolate 3-84-6, rep. 2Evolved strain0.083.190.89Asakura Y, et al. (2011) 
K-12 YA027 after 84 serial passages (~500 generations) isolate 3-84-10, rep. 1Evolved strain-0.003.150.01Asakura Y, et al. (2011) 
K-12 YA027 after 84 serial passages (~500 generations) isolate 3-84-10, rep. 2Evolved strain0.043.170.38Asakura Y, et al. (2011) 
K-12 YA027 after 172 serial passages (~1,000 generations) isolate 3-172-1, rep. 1Evolved strain-0.013.150.25Asakura Y, et al. (2011) 
K-12 YA027 after 172 serial passages (~1,000 generations) isolate 3-172-1, rep. 2Evolved strain-0.023.140.37Asakura Y, et al. (2011) 
K-12 YA027 after 172 serial passages (~1,000 generations) isolate 3-172-1, rep. 3Evolved strain0.013.160.12Asakura Y, et al. (2011) 
K-12 YA027 after 172 serial passages (~1,000 generations) isolate 3-172-9, rep. 1Evolved strain-0.083.110.81Asakura Y, et al. (2011) 
K-12 YA027 after 172 serial passages (~1,000 generations) isolate 3-172-9, rep. 2Evolved strain-0.063.130.41Asakura Y, et al. (2011) 
K-12 YA027 after 172 serial passages (~1,000 generations) isolate 3-172-10, rep. 1Evolved strain0.003.160.08Asakura Y, et al. (2011) 
K-12 YA027 after 172 serial passages (~1,000 generations) isolate 3-172-10, rep. 2Evolved strain0.033.170.48Asakura Y, et al. (2011) 
K-12 MC4100 ycgE(del) vs. wt in stationary phase, rep. 1Wild type vs Mutant-0.589.920.54Tschowri N, et al. (2009)Gene Profile
K-12 MC4100 ycgE(del) vs. wt in stationary phase, rep. 2Wild type vs Mutant0.069.240.04Tschowri N, et al. (2009) 
ycgF dependent genes in blue light, rep1Blue-light irradiation0.479.970.69Tschowri N, et al. (2009) 
ycgF dependent genes in blue light, rep2Blue-light irradiation-0.349.260.65Tschowri N, et al. (2009)Gene Profile
K-12 MG1655 glycerol-evolved pop. 7 - day 44, rep. 3Evolution-0.052.890.48Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 7 - day 44, rep. 2Evolution-0.022.910.17Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 7 - day 44, rep. 1Evolution-0.012.920.02Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 6 - day 44, rep. 3Evolution0.082.960.53Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 6 - day 44, rep. 2Evolution0.062.950.57Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 6 - day 44, rep. 1Evolution0.072.950.61Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 6 - day 20, rep. 3Evolution0.082.960.55Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 6 - day 20, rep. 1Evolution-0.002.920.22Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 5 - day 44, rep. 3Evolution0.052.950.46Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 5 - day 44, rep. 2Evolution0.022.930.08Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 5 - day 44, rep. 1Evolution-0.012.910.14Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 5 - day 20, rep. 3Evolution0.052.950.51Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 5 - day 20, rep. 2Evolution0.002.920.06Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 4 - day 44, rep. 3Evolution-0.052.890.48Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 4 - day 44, rep. 2Evolution-0.072.880.64Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 4 - day 44, rep. 1Evolution-0.022.910.11Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 4 - day 20, rep. 3Evolution-0.082.880.27Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 4 - day 20, rep. 2Evolution0.012.930.23Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 3 - day 44, rep. 3Evolution0.012.930.09Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 3 - day 44, rep. 2Evolution0.042.940.41Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 3 - day 44, rep. 1Evolution-0.002.920.12Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 3 - day 20, rep. 2Evolution-0.042.900.15Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 3 - day 20, rep. 1Evolution0.072.961.00Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 1 - day 44, rep. 3Evolution-0.032.900.05Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 1 - day 44, rep. 2Evolution0.002.920.22Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 1 - day 44, rep. 1Evolution-0.022.910.14Fong SS, et al. (2005) 
K-12 MG1655 glycerol-evolved pop. 1 - day 20, rep. 3Evolution-0.112.860.35Fong SS, et al. (2005) 
K-12 MG1655 unevolved - growth on lactate, rep. 6Evolution - control-0.022.910.01Fong SS, et al. (2005) 
K-12 MG1655 unevolved - growth on lactate, rep. 5Evolution - control-0.052.900.51Fong SS, et al. (2005) 
K-12 MG1655 unevolved - growth on lactate, rep. 4Evolution - control-0.052.900.34Fong SS, et al. (2005) 
K-12 MG1655 unevolved - growth on lactate, rep. 3Evolution - control-0.022.910.22Fong SS, et al. (2005) 
K-12 MG1655 unevolved - growth on lactate, rep. 2Evolution - control-0.072.890.65Fong SS, et al. (2005) 
K-12 MG1655 unevolved - growth on lactate, rep. 1Evolution - control0.012.920.14Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 7 - day 60, rep. 3Evolution-0.022.910.25Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 7 - day 60, rep. 2Evolution0.082.960.91Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 7 - day 60, rep. 1Evolution-0.052.900.51Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 7 - day 20, rep. 3Evolution0.032.940.35Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 7 - day 20, rep. 2Evolution-0.032.900.10Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 7 - day 20, rep. 1Evolution0.052.950.76Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 6 - day 60, rep. 3Evolution-0.052.900.58Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 6 - day 60, rep. 2Evolution0.052.950.61Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 6 - day 60, rep. 1Evolution-0.012.910.23Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 6 - day 20, rep. 3Evolution-0.022.910.19Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 6 - day 20, rep. 2Evolution0.042.940.59Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 6 - day 20, rep. 1Evolution0.022.930.19Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 5 - day 60, rep. 3Evolution-0.062.890.54Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 5 - day 60, rep. 2Evolution0.012.920.12Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 5 - day 60, rep. 1Evolution-0.032.910.14Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 5 - day 20, rep. 3Evolution0.052.950.60Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 5 - day 20, rep. 2Evolution0.012.920.08Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 5 - day 20, rep. 1Evolution0.022.930.19Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 4 - day 60, rep. 3Evolution-0.032.910.06Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 4 - day 60, rep. 2Evolution0.042.940.67Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 4 - day 60, rep. 1Evolution0.022.930.50Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 4 - day 20, rep. 3Evolution0.022.930.30Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 4 - day 20, rep. 2Evolution-0.012.910.17Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 4 - day 20, rep. 1Evolution-0.022.910.20Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 3 - day 60, rep. 4Evolution0.032.940.26Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 3 - day 60, rep. 3Evolution-0.032.910.32Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 3 - day 60, rep. 2Evolution0.102.971.05Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 3 - day 60, rep. 1Evolution0.032.930.29Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 3 - day 20, rep. 2Evolution0.092.960.84Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 3 - day 20, rep. 1Evolution0.052.940.66Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 2 - day 60, rep. 3Evolution0.082.960.81Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 2 - day 60, rep. 2Evolution0.052.940.52Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 2 - day 60, rep. 1Evolution0.032.940.27Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 2 - day 20, rep. 3Evolution0.012.920.19Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 2 - day 20, rep. 2Evolution-0.022.910.20Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 2 - day 20, rep. 1Evolution-0.012.920.13Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 1 - day 60, rep. 3Evolution0.022.930.23Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 1 - day 60, rep. 2Evolution0.032.940.30Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 1 - day 60, rep. 1Evolution0.112.970.88Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 1 - day 20, rep. 3Evolution0.012.930.07Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 1 - day 20, rep. 2Evolution0.052.940.36Fong SS, et al. (2005) 
K-12 MG1655 lactate-evolved pop. 1 - day 20, rep. 1Evolution0.022.930.14Fong SS, et al. (2005) 
K-12 BW25113 rpoS + ethanol shock in expo. phase, rep. 1Ethanol - mutant0.063.290.42Lin M, Chen M, Yan Y, Zhang Y (unpublished) 
K-12 BW25113 rpoS + ethanol shock in expo. phase, rep. 2Ethanol - mutant-0.003.260.02Lin M, Chen M, Yan Y, Zhang Y (unpublished) 
K-12 BW25113 rpoS + ethanol shock in expo. phase, rep. 3Ethanol - mutant-0.023.250.19Lin M, Chen M, Yan Y, Zhang Y (unpublished) 
K-12 BW25113 rpoS + ethanol shock in stat. phase, rep. 1Ethanol - mutant-0.103.210.94Lin M, Chen M, Yan Y, Zhang Y (unpublished) 
K-12 BW25113 rpoS + ethanol shock in stat. phase, rep. 2Ethanol - mutant-0.083.220.64Lin M, Chen M, Yan Y, Zhang Y (unpublished) 
K-12 BW25113 rpoS + ethanol shock in stat. phase, rep. 3Ethanol - mutant-0.073.230.69Lin M, Chen M, Yan Y, Zhang Y (unpublished) 
K-12 BW25113 + ethanol shock in expo. phase, rep. 1Ethanol-0.043.240.49Lin M, Chen M, Yan Y, Zhang Y (unpublished) 
K-12 BW25113 + ethanol shock in expo. phase, rep. 2Ethanol-0.033.250.31Lin M, Chen M, Yan Y, Zhang Y (unpublished) 
K-12 BW25113 + ethanol shock in expo. phase, rep. 3Ethanol0.083.300.87Lin M, Chen M, Yan Y, Zhang Y (unpublished) 
K-12 BW25113 + ethanol shock in stat. phase, rep. 1Ethanol-0.053.240.43Lin M, Chen M, Yan Y, Zhang Y (unpublished) 
K-12 BW25113 + ethanol shock in stat. phase, rep. 2Ethanol-0.063.230.66Lin M, Chen M, Yan Y, Zhang Y (unpublished) 
K-12 BW25113 + ethanol shock in stat. phase, rep. 3Ethanol-0.053.240.46Lin M, Chen M, Yan Y, Zhang Y (unpublished) 
K-12 MG1655 nusB(del)Mutant-0.013.170.43Hashimoto C, et al. (2011) 
K-12 MG1655 (is nusB+) controlWild type0.013.180.30Hashimoto C, et al. (2011) 
K-12 DH5alpha pMG1-irrE+ + ethanol stress, rep. 3Ethanol-0.012.640.03Chen T, et al. (2012) 
K-12 DH5alpha pMG1-irrE+ + ethanol stress, rep. 2Ethanol0.042.660.29Chen T, et al. (2012) 
K-12 DH5alpha pMG1-irrE+ + ethanol stress, rep. 1Ethanol0.092.690.60Chen T, et al. (2012) 
K-12 DH5alpha pMG1-irrE(E1) + ethanol stress, rep. 3Ethanol + Mutant-0.062.620.25Chen T, et al. (2012) 
K-12 DH5alpha pMG1-irrE(E1) + ethanol stress, rep. 2Ethanol + Mutant-0.092.600.53Chen T, et al. (2012) 
K-12 DH5alpha pMG1-irrE(E1) + ethanol stress, rep. 1Ethanol + Mutant0.022.650.25Chen T, et al. (2012)