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Originally published In Press as doi:10.1074/jbc.M202881200 on May 16, 2002

J. Biol. Chem., Vol. 277, Issue 30, 27282-27287, July 26, 2002
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Interaction of the Conserved Region 4.2 of sigma E with the RseA Anti-sigma Factor*

Christina Tam, Bruno Collinet, Gary Lau, Satish RainaDagger , and Dominique Missiakas§

From the Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois 60637 and the Dagger  Departement de Biochimie Médicale, Centre Médical Universitaire, 1 Rue Michel Servet, 1211 Geneva 4, Switzerland

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.

* This work was supported by United States Public Health Service Grant GM58266.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, The University of Chicago, 920 East 58th St., Chicago IL 6063. Tel.: 773-834-8161; E-mail: dmissiak@bsd.uchicago.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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