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J. Biol. Chem., Vol. 279, Issue 19, 19540-19550, May 7, 2004
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Crl, a Low Temperature-induced Protein in Escherichia coli That Binds Directly to the Stationary Phase 
Subunit of RNA Polymerase*
From the Laboratoire Adaptation et Pathogénie des Micro-organismes, Université Joseph Fourier, CNRS UMR 5163, F-38041 Grenoble Cedex 9, France
The alternative sigma factor 
S (RpoS) of Escherichia coli RNA polymerase regulates the expression of stationary phase and stress-response genes. S is also required for the transcription of the cryptic genes csgBA that encode the subunits of the curli proteins. The expression of the csgBA genes is regulated in response to a multitude of physiological signals. In stationary phase, these genes are transcribed by the S factor, and expression of the operon is enhanced by the small protein Crl. It has been shown that Crl stimulates the activity of S, leading to an increased transcription rate of a subset of genes of the rpoS regulon in stationary phase. However, the underlying molecular mechanism has remained elusive. We show here that Crl interacts directly with S and that this interaction promotes binding of the S holoenzyme (ES) to the csgBA promoter. Expression of Crl is increased during the transition from growing to stationary phase. Crl accumulates in stationary phase cells at low temperature (30 °C) but not at 37 °C. We therefore propose that Crl is a second thermosensor, besides DsrA, controlling S activity.
Received for publication, December 24, 2003 , and in revised form, February 13, 2004.
* The costs of publication of this article were defrayed in part by the payment of page charges. This 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: Laboratoire Adaptation et Pathogénie des Micro-organismes, Université Joseph Fourier, BP53, F-38041 Grenoble Cedex 9, France. Tel.: 33-4-76-51-40-28; Fax: 33-4-76-63-56-63; E-mail: cecile.lelong{at}ujf-grenoble.fr.
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