| pubmed-article:8550468 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8550468 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:8550468 | lifeskim:mentions | umls-concept:C0030946 | lld:lifeskim |
| pubmed-article:8550468 | lifeskim:mentions | umls-concept:C0037067 | lld:lifeskim |
| pubmed-article:8550468 | lifeskim:mentions | umls-concept:C0038187 | lld:lifeskim |
| pubmed-article:8550468 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:8550468 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:8550468 | pubmed:dateCreated | 1996-2-20 | lld:pubmed |
| pubmed-article:8550468 | pubmed:abstractText | In Escherichia coli, starvation (stationary-phase)-mediated differentiation involves 50 or more genes and is triggered by an increase in cellular sigma s levels. Western immunoblot analysis showed that in mutants lacking the protease ClpP or its cognate ATPase-containing subunit ClpX, sigma s levels of exponential-phase cells increased to those of stationary-phase wild-type cells. Lack of other potential partners of ClpP, i.e., ClpA or ClpB, or of Lon protease had no effect. In ClpXP-proficient cells, the stability of sigma s increased markedly in stationary-phase compared with exponential-phase cells, but in ClpP-deficient cells, sigma s became virtually completely stable in both phases. There was no decrease in ClpXP levels in stationary-phase wild-type cells. Thus, sigma s probably becomes more resistant to this protease in stationary phase. The reported sigma s-stabilizing effect of the hns mutation also was not due to decreased protease levels. Studies with translational fusions containing different lengths of sigma s coding region suggest that amino acid residues 173 to 188 of this sigma factor may directly or indirectly serve as at least part of the target for ClpXP protease. | lld:pubmed |
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| pubmed-article:8550468 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8550468 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8550468 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8550468 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8550468 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:8550468 | pubmed:author | pubmed-author:MatinAA | lld:pubmed |
| pubmed-article:8550468 | pubmed:author | pubmed-author:LeeK HKH | lld:pubmed |
| pubmed-article:8550468 | pubmed:author | pubmed-author:SchwederTT | lld:pubmed |
| pubmed-article:8550468 | pubmed:author | pubmed-author:LomovskayaOO | lld:pubmed |
| pubmed-article:8550468 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8550468 | pubmed:volume | 178 | lld:pubmed |
| pubmed-article:8550468 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8550468 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8550468 | pubmed:pagination | 470-6 | lld:pubmed |
| pubmed-article:8550468 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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