| pubmed-article:10485902 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10485902 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:10485902 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:10485902 | lifeskim:mentions | umls-concept:C0038952 | lld:lifeskim |
| pubmed-article:10485902 | lifeskim:mentions | umls-concept:C2350440 | lld:lifeskim |
| pubmed-article:10485902 | lifeskim:mentions | umls-concept:C0243127 | lld:lifeskim |
| pubmed-article:10485902 | lifeskim:mentions | umls-concept:C0443199 | lld:lifeskim |
| pubmed-article:10485902 | lifeskim:mentions | umls-concept:C1323631 | lld:lifeskim |
| pubmed-article:10485902 | lifeskim:mentions | umls-concept:C0443331 | lld:lifeskim |
| pubmed-article:10485902 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:10485902 | pubmed:dateCreated | 1999-10-14 | lld:pubmed |
| pubmed-article:10485902 | pubmed:abstractText | The Escherichia coli proteins H-NS is recognized as an important component among the major nucleoid-associated proteins. In studies of E. coli strains with defects in H-NS, we discovered a mutant that phenotypically restored stationary-phase viability (Rsv) of such strains. The Rsv phenotype was the result of a mutation that led to severalfold higher levels of the functionally and structurally related StpA protein. This mutation was a base pair change in the stpA structural gene, and the amino acid substitution in the StpA protein altered its turnover properties, suggesting a role for this residue in a cleavage site for proteolysis. We determined the stability of the StpA and the H-NS proteins and found that the StpA protein was degraded relatively rapidly in strains lacking functional H-NS, whereas H-NS remained stable irrespective of the presence/absence of StpA. Using protease-deficient mutants, we obtained evidence that the Lon protease was responsible for the degradation of StpA. The differential turnover of the nucleoid-associated proteins is suggested to contribute to the regulation of their stoichiometry and ratio in terms of homo- and heteromer formation. We conclude that StpA, in contrast to H-NS, is present mainly in heteromeric form in E. coli. | lld:pubmed |
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| pubmed-article:10485902 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10485902 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10485902 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10485902 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:10485902 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:10485902 | pubmed:author | pubmed-author:UhlinB EBE | lld:pubmed |
| pubmed-article:10485902 | pubmed:author | pubmed-author:JohanssonJJ | lld:pubmed |
| pubmed-article:10485902 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10485902 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:10485902 | pubmed:volume | 96 | lld:pubmed |
| pubmed-article:10485902 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10485902 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10485902 | pubmed:pagination | 10776-81 | lld:pubmed |
| pubmed-article:10485902 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:10485902 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10485902 | pubmed:articleTitle | Differential protease-mediated turnover of H-NS and StpA revealed by a mutation altering protein stability and stationary-phase survival of Escherichia coli. | lld:pubmed |
| pubmed-article:10485902 | pubmed:affiliation | Department of Microbiology, Umeâ University, S-90187 Umeâ, Sweden. | lld:pubmed |
| pubmed-article:10485902 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10485902 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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