| pubmed-article:3306410 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3306410 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:3306410 | lifeskim:mentions | umls-concept:C0086045 | lld:lifeskim |
| pubmed-article:3306410 | lifeskim:mentions | umls-concept:C0282498 | lld:lifeskim |
| pubmed-article:3306410 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:3306410 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:3306410 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:3306410 | pubmed:issue | 6137 | lld:pubmed |
| pubmed-article:3306410 | pubmed:dateCreated | 1987-10-22 | lld:pubmed |
| pubmed-article:3306410 | pubmed:abstractText | Cells subjected to a heat shock, or a variety of other stresses increase the synthesis of a set of proteins, known as heat shock proteins. This response is apparently universal, occurring in the entire range from bacterial to mammalian cells. In Escherichia coli heat shock protein synthesis transiently increases following a shift from 30 degrees C to 42 degrees C as a result of changes in transcription initiation at heat shock promoters. Heat shock promoters are recognized by RNA polymerase containing a sigma factor of relative molecular mass (Mr) 32,000 (32K) E sigma 32 and not E sigma 70, the major form of RNA polymerase holoenzyme. To determine whether changes in the concentration of sigma 32 regulate this response, we measured the amount of sigma 32 before and after shift to high temperature and found that it increased transiently during heat shock as a result of changes in sigma 32 synthesis and stability. Our results indicate that sigma 32 is directly responsible for regulation of the heat shock response. | lld:pubmed |
| pubmed-article:3306410 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3306410 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3306410 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3306410 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3306410 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:3306410 | pubmed:author | pubmed-author:StrausD BDB | lld:pubmed |
| pubmed-article:3306410 | pubmed:author | pubmed-author:GrossC ACA | lld:pubmed |
| pubmed-article:3306410 | pubmed:author | pubmed-author:WalterW AWA | lld:pubmed |
| pubmed-article:3306410 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3306410 | pubmed:volume | 329 | lld:pubmed |
| pubmed-article:3306410 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3306410 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3306410 | pubmed:pagination | 348-51 | lld:pubmed |
| pubmed-article:3306410 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:3306410 | pubmed:articleTitle | The heat shock response of E. coli is regulated by changes in the concentration of sigma 32. | lld:pubmed |
| pubmed-article:3306410 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3306410 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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