4.5 Article

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

Journal

RNA BIOLOGY
Volume 10, Issue 4, Pages 610-618

Publisher

TAYLOR & FRANCIS INC
DOI: 10.4161/rna.24201

Keywords

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

Funding

  1. German Research Foundation Priority Program SPP1258 Sensory and Regulatory RNAs in Prokaryotes
  2. International PhD Program Tubingen

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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.

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