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pubmed-article:9079929pubmed:abstractTextTranscription 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:9079929pubmed:authorpubmed-author:JohnsonR CRClld:pubmed
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pubmed-article:9079929pubmed:dateRevised2009-11-18lld:pubmed
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pubmed-article:9079929pubmed:articleTitleCyclic AMP receptor protein functions as a repressor of the osmotically inducible promoter proP P1 in Escherichia coli.lld:pubmed
pubmed-article:9079929pubmed:affiliationDepartment of Biological Chemistry, UCLA School of Medicine, Los Angeles, California 90095-1737, USA.lld:pubmed
pubmed-article:9079929pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9079929pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:9079929pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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