| Characterization of the induction and cellular role of the BaeSR two-component envelope stress response of Escherichia coli. | |
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MedLine Citation:
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PMID: 21515766 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The bacterial cell envelope is the interface between a bacterium and its environment and is constantly exposed to environmental changes. The BaeSR two-component system regulates one of six envelope stress responses in Escherichia coli and is induced by spheroplasting, overexpression of the pilin subunit PapG, and exposure to indole. The known BaeR regulon is small, consisting of eight genes, mdtABCD-baeSR, acrD, and spy, two of which encode the BaeSR two-component system itself. In this study, we investigated the molecular nature of the BaeS-inducing cue and the cellular role of the BaeSR envelope stress response. We demonstrated that at least two flavonoids and sodium tungstate are novel inducers of the BaeSR response. Interestingly, flavonoids and sodium tungstate led to much stronger induction of the BaeSR response in an mdtA efflux pump mutant, while indole did not. These findings are consistent with the hypothesis that flavonoids and sodium tungstate are natural substrates of the MdtABC efflux pump. Indole has recently been implicated in cell-cell signaling and biofilm repression through a putative interaction with the LuxR homologue SdiA. Using genetic analyses, we found that induction of the BaeSR response by indole occurs via a pathway separate from the SdiA biofilm pathway. Further, we demonstrated that the BaeSR response does not influence biofilm formation, nor is it involved in indole-mediated inhibition of biofilm formation. We hypothesize that the main function of the Bae response is to upregulate efflux pump expression in response to specific envelope-damaging agents. |
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Authors:
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Shannon K D Leblanc; Christopher W Oates; Tracy L Raivio |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2011-04-22 |
Journal Detail:
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Title: Journal of bacteriology Volume: 193 ISSN: 1098-5530 ISO Abbreviation: J. Bacteriol. Publication Date: 2011 Jul |
Date Detail:
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Created Date: 2011-06-15 Completed Date: 2011-08-23 Revised Date: 2012-01-02 |
Medline Journal Info:
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Nlm Unique ID: 2985120R Medline TA: J Bacteriol Country: United States |
Other Details:
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Languages: eng Pagination: 3367-75 Citation Subset: IM |
Affiliation:
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Department of Biological Sciences, University of Alberta, Edmonton, Alberta, Canada. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Drug Resistance, Microbial Escherichia coli / genetics, metabolism, physiology* Escherichia coli Proteins / genetics, metabolism* Flavonoids / metabolism Gene Expression Regulation, Bacterial* Indoles / metabolism Membrane Transport Proteins / metabolism Multidrug Resistance-Associated Proteins / genetics, metabolism* Protein Kinases / genetics, metabolism* Signal Transduction* Trans-Activators / genetics, metabolism* Transcriptional Activation Tungsten Compounds / metabolism |
| Chemical | |
Reg. No./Substance:
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0/BaeR protein, E coli; 0/Escherichia coli Proteins; 0/Flavonoids; 0/Indoles; 0/Mdt-A protein, E coli; 0/MdtB protein, E coli; 0/MdtC protein, E coli; 0/Membrane Transport Proteins; 0/Multidrug Resistance-Associated Proteins; 0/Trans-Activators; 0/Tungsten Compounds; 120-72-9/indole; 13472-45-2/sodium tungstate(VI); EC 2.7.-/Protein Kinases; EC 2.7.3.-/protein-histidine kinase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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