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RNA Biol. 2013 Apr;10(4):610-8. doi: 10.4161/rna.24201. Epub 2013 Mar 27.

Structure and RNA-binding properties of the bacterial LSm protein Hfq.

Author information

1
Biozentrum, University of Basel, Basel, Switzerland. evelyn.sauer@unibas.ch

Abstract

Over the past years, small non-coding RNAs (sRNAs) emerged as important modulators of gene expression in bacteria. Guided by partial sequence complementarity, these sRNAs interact with target mRNAs and eventually affect transcript stability and translation. The physiological function of sRNAs depends on the protein Hfq, which binds sRNAs in the cell and promotes the interaction with their mRNA targets. This important physiological function of Hfq as a central hub of sRNA-mediated regulation made it one of the most intensely studied proteins in bacteria. Recently, a new model for sRNA binding by Hfq has been proposed that involves the direct recognition of the sRNA 3' end and interactions of the sRNA body with the lateral RNA-binding surface of Hfq. This review summarizes the current understanding of the RNA binding properties of Hfq and its (s)RNA complexes. Moreover, the implications of the new binding model for sRNA-mediated regulation are discussed.

KEYWORDS:

3′ end recognition; LSm ring; RNA chaperone; RNA degradation; crystal structure; gene regulation; non-coding RNAs; prokaryotes

PMID:
23535768
PMCID:
PMC3710368
DOI:
10.4161/rna.24201
[Indexed for MEDLINE]
Free PMC Article
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