Source:http://linkedlifedata.com/resource/pubmed/id/19843227
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2009-11-27
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pubmed:abstractText |
StpA is a paralogue of the nucleoid-associated protein H-NS that is conserved in a range of enteric bacteria and had no known function in Salmonella Typhimurium. We show that 5% of the Salmonella genome is regulated by StpA, which contrasts with the situation in Escherichia coli where deletion of stpA only had minor effects on gene expression. The StpA-dependent genes of S. Typhimurium are a specific subset of the H-NS regulon that are predominantly under the positive control of sigma(38) (RpoS), CRP-cAMP and PhoP. Regulation by StpA varied with growth phase; StpA controlled sigma(38) levels at mid-exponential phase by preventing inappropriate activation of sigma(38) during rapid bacterial growth. In contrast, StpA only activated the CRP-cAMP regulon during late exponential phase. ChIP-chip analysis revealed that StpA binds to PhoP-dependent genes but not to most genes of the CRP-cAMP and sigma(38) regulons. In fact, StpA indirectly regulates sigma(38)-dependent genes by enhancing sigma(38) turnover by repressing the anti-adaptor protein rssC. We discovered that StpA is essential for the dynamic regulation of sigma(38) in response to increased glucose levels. Our findings identify StpA as a novel growth phase-specific regulator that plays an important physiological role by linking sigma(38) levels to nutrient availability.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Sigma Factor,
http://linkedlifedata.com/resource/pubmed/chemical/StpA protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/sigma factor KatF protein, Bacteria
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1365-2958
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
74
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1169-86
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pubmed:dateRevised |
2010-5-10
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pubmed:meshHeading |
pubmed-meshheading:19843227-Amino Acid Sequence,
pubmed-meshheading:19843227-Bacterial Proteins,
pubmed-meshheading:19843227-Cell Wall,
pubmed-meshheading:19843227-Cloning, Molecular,
pubmed-meshheading:19843227-DNA-Binding Proteins,
pubmed-meshheading:19843227-Escherichia coli,
pubmed-meshheading:19843227-Escherichia coli Proteins,
pubmed-meshheading:19843227-Gene Expression Regulation, Bacterial,
pubmed-meshheading:19843227-Glucose,
pubmed-meshheading:19843227-Molecular Chaperones,
pubmed-meshheading:19843227-Protein Stability,
pubmed-meshheading:19843227-Regulon,
pubmed-meshheading:19843227-Salmonella typhimurium,
pubmed-meshheading:19843227-Sigma Factor
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pubmed:year |
2009
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pubmed:articleTitle |
The H-NS-like protein StpA represses the RpoS (sigma 38) regulon during exponential growth of Salmonella Typhimurium.
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pubmed:affiliation |
Institute of Food Research, Colney Lane, Norwich, NR4 7UA, UK. sacha.lucchini@bbsrc.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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