| Literature DB >> 9326599 |
K Murakami1, J T Owens, T A Belyaeva, C F Meares, S J Busby, A Ishihama.
Abstract
Interactions between the cAMP receptor protein (CRP) and the carboxy-terminal regulatory domain (CTD) of Escherichia coli RNA polymerase alpha subunit were analyzed at promoters carrying tandem DNA sites for CRP binding using a chemical nuclease covalently attached to alpha. Each CRP dimer was found to direct the positioning of one of the two alpha subunit CTDs. Thus, the function of RNA polymerase may be subject to regulation through protein-protein interactions between the two alpha subunits and two different species of transcription factors.Entities:
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Year: 1997 PMID: 9326599 PMCID: PMC23438 DOI: 10.1073/pnas.94.21.11274
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205