| pubmed-article:3023348 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3023348 | lifeskim:mentions | umls-concept:C0007364 | lld:lifeskim |
| pubmed-article:3023348 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:3023348 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:3023348 | pubmed:issue | 35 | lld:pubmed |
| pubmed-article:3023348 | pubmed:dateCreated | 1987-1-12 | lld:pubmed |
| pubmed-article:3023348 | pubmed:abstractText | cAMP receptor protein (CRP)-dependent operon expression in Escherichia coli requires the CRP X cAMP complex form of wild-type CRP. One class of crp mutants (crp*) activates CRP-dependent promoters in strains (cya) incapable of endogenous cAMP synthesis. Of fundamental interest is the difference in regulatory properties exhibited by crp* mutant strains, some of which exhibit glucose-mediated repression of beta-galactosidase synthesis, some of which do not. To gain a better understanding of the mechanisms of cAMP-independent promoter activation and repression we have: determined through cloning and DNA sequence analysis the primary structure of three CRP* forms of CRP; purified the mutant proteins; characterized the effect of these mutations on CRP secondary structure; and studied CRP*-activated lac promoter regulation in a purified in vitro transcription system. The results of this study provide strong evidence that mutations in crp alter the conformation of CRP and result in cAMP-independent activation of CRP-dependent promoters in vitro. In addition, a CRP allele-specific inhibition of CRP* activity by spermidine was observed in vitro that parallels crp* strain-specific sensitivity to glucose-mediated repression of CRP-dependent enzyme synthesis in vivo. This observation provides evidence that catabolite repression in cells lacking cAMP may be mediated through a mechanism that inhibits CRP* activity. | lld:pubmed |
| pubmed-article:3023348 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3023348 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3023348 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3023348 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3023348 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:3023348 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3023348 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3023348 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:3023348 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:3023348 | pubmed:author | pubmed-author:PeterkofskyAA | lld:pubmed |
| pubmed-article:3023348 | pubmed:author | pubmed-author:HarmanJ GJG | lld:pubmed |
| pubmed-article:3023348 | pubmed:author | pubmed-author:McKenneyKK | lld:pubmed |
| pubmed-article:3023348 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3023348 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:3023348 | pubmed:volume | 261 | lld:pubmed |
| pubmed-article:3023348 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3023348 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3023348 | pubmed:pagination | 16332-9 | lld:pubmed |
| pubmed-article:3023348 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:3023348 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:3023348 | pubmed:articleTitle | Structure-function analysis of three cAMP-independent forms of the cAMP receptor protein. | lld:pubmed |
| pubmed-article:3023348 | pubmed:publicationType | Journal Article | lld:pubmed |
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