RNA remodeling by bacterial global regulator CsrA promotes Rho-dependent transcription termination

RNA-binding protein CsrA is a key regulator of a variety of cellular processes in bacteria, including carbon and stationary phase metabolism, biofilm formation, quorum sensing, and virulence gene expression in pathogens. CsrA binds to bipartite sequence elements at or near the ribosome loading site...

Full description

Saved in:
Bibliographic Details
Published inGenes & development Vol. 28; no. 11; pp. 1239 - 1251
Main Authors Figueroa-Bossi, Nara, Schwartz, Annie, Guillemardet, Benoit, D'Heygère, François, Bossi, Lionello, Boudvillain, Marc
Format Journal Article
LanguageEnglish
Published United States Cold Spring Harbor Laboratory Press 01.06.2014
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:RNA-binding protein CsrA is a key regulator of a variety of cellular processes in bacteria, including carbon and stationary phase metabolism, biofilm formation, quorum sensing, and virulence gene expression in pathogens. CsrA binds to bipartite sequence elements at or near the ribosome loading site in messenger RNA (mRNA), most often inhibiting translation initiation. Here we describe an alternative novel mechanism through which CsrA achieves negative regulation. We show that CsrA binding to the upstream portion of the 5' untranslated region of Escherichia coli pgaA mRNA-encoding a polysaccharide adhesin export protein-unfolds a secondary structure that sequesters an entry site for transcription termination factor Rho, resulting in the premature stop of transcription. These findings establish a new paradigm for bacterial gene regulation in which remodeling of the nascent transcript by a regulatory protein promotes Rho-dependent transcription attenuation.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
PMCID: PMC4052769
ISSN:0890-9369
1549-5477
DOI:10.1101/gad.240192.114