pubmed-article:9079929 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9079929 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
pubmed-article:9079929 | lifeskim:mentions | umls-concept:C0007364 | lld:lifeskim |
pubmed-article:9079929 | lifeskim:mentions | umls-concept:C1336789 | lld:lifeskim |
pubmed-article:9079929 | lifeskim:mentions | umls-concept:C0086860 | lld:lifeskim |
pubmed-article:9079929 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
pubmed-article:9079929 | lifeskim:mentions | umls-concept:C1527118 | lld:lifeskim |
pubmed-article:9079929 | pubmed:issue | 7 | lld:pubmed |
pubmed-article:9079929 | pubmed:dateCreated | 1997-4-29 | lld:pubmed |
pubmed-article:9079929 | pubmed:abstractText | Transcription of the proP gene, encoding a transporter of the osmoprotectants proline and glycine betaine, is controlled from two promoters, P1 and P2, that respond primarily to osmotic and stationary-phase signals, respectively. The P1 promoter is normally expressed at a very low level under low or normal medium osmolarity. We demonstrate that the binding of the cyclic AMP (cAMP) receptor protein (CRP) to a site centered at -34.5 within the promoter is responsible for the low promoter activity under these conditions. A brief period of reduced CRP binding in early log phase corresponds to a transient burst of P1 transcription upon resumption of growth in Luria-Bertani broth. A CRP binding-site mutation or the absence of a functional crp gene leads to high constitutive expression of P1. We show that the binding of CRP-cAMP inhibits transcription by purified RNA polymerase in vitro at P1, but this repression is relieved at moderately high potassium glutamate concentrations. Likewise, open-complex formation at P1 in vivo is inhibited by the presence of CRP under low-osmolarity conditions. Because P1 expression can be further induced by osmotic upshifts in a delta crp strain or in the presence of the CRP binding-site mutation, additional controls exist to osmotically regulate P1 expression. | lld:pubmed |
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pubmed-article:9079929 | pubmed:language | eng | lld:pubmed |
pubmed-article:9079929 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9079929 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:9079929 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9079929 | pubmed:month | Apr | lld:pubmed |
pubmed-article:9079929 | pubmed:issn | 0021-9193 | lld:pubmed |
pubmed-article:9079929 | pubmed:author | pubmed-author:JohnsonR CRC | lld:pubmed |
pubmed-article:9079929 | pubmed:author | pubmed-author:XuJJ | lld:pubmed |
pubmed-article:9079929 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9079929 | pubmed:volume | 179 | lld:pubmed |
pubmed-article:9079929 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9079929 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9079929 | pubmed:pagination | 2410-7 | lld:pubmed |
pubmed-article:9079929 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:9079929 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9079929 | pubmed:articleTitle | Cyclic AMP receptor protein functions as a repressor of the osmotically inducible promoter proP P1 in Escherichia coli. | lld:pubmed |
pubmed-article:9079929 | pubmed:affiliation | Department of Biological Chemistry, UCLA School of Medicine, Los Angeles, California 90095-1737, USA. | lld:pubmed |
pubmed-article:9079929 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9079929 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9079929 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:948626 | entrezgene:pubmed | pubmed-article:9079929 | lld:entrezgene |
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