| Literature DB >> 12016219 |
Christina Tam1, Bruno Collinet, Gary Lau, Satish Raina, Dominique Missiakas.
Abstract
Esigma(E) RNA polymerase transcribes a regulon of folding factors for the bacterial envelope and is induced by physical and chemical stresses. The RseA anti-sigma factor inhibits the activity of Esigma(E) RNA polymerase. It is shown here that the N-terminal portion of sigma(E), residues 1-153, binds core RNA polymerase. RseA interacts with residues 154-191 of sigma(E), a site that is homologous to region 4, the sigma factor binding site for promoter DNA. Mutations that reduce transcription of Esigma(E) RNA polymerase map to sigma(E) residues 178, 181, and 183. Variant sigma(E) proteins with amino acid substitutions at residues 178, 181, or 183 do not associate with RseA. A regulatory mechanism is proposed whereby RseA binds to a C-terminal peptide of sigma(E) and inhibits the transcription of Esigma(E) RNA polymerase by blocking promoter recognition.Entities:
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Year: 2002 PMID: 12016219 DOI: 10.1074/jbc.M202881200
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157