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J Bacteriol. 2005 May;187(10):3496-501.

Solution structure of the carbon storage regulator protein CsrA from Escherichia coli.

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1
Department of Biochemistry, McGill University, 3655 Promenade Sir William Osler, Montreal, Quebec, Canada H3G 1Y6.

Abstract

The carbon storage regulator A (CsrA) is a protein responsible for the repression of a variety of stationary-phase genes in bacteria. In this work, we describe the nuclear magnetic resonance (NMR)-based structure of the CsrA dimer and its RNA-binding properties. CsrA is a dimer of two identical subunits, each composed of five strands, a small alpha-helix and a flexible C terminus. NMR titration experiments suggest that the beta1-beta2 and beta3-beta4 loops and the C-terminal helix are important elements in RNA binding. Even though the beta3-beta4 loop contains a highly conserved RNA-binding motif, GxxG, typical of KH domains, our structure excludes CsrA from being a member of this protein family, as previously suggested. A mechanism for the recognition of mRNAs downregulated by CsrA is proposed.

PMID:
15866937
PMCID:
PMC1112004
DOI:
10.1128/JB.187.10.3496-3501.2005
[Indexed for MEDLINE]
Free PMC Article
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