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PMID: 22370051 Published · ppublish English Journal Article Review

Multiple activities of RNA-binding proteins S1 and Hfq.

Biochimie ·Vol. 94 ·No. 7 ·2012-07-00 ·Pages 1544-53

Hajnsdorf E, Boni IV

Abstract

In all organisms, RNA-binding proteins participate in modulating all the steps in the life cycle of RNA, including transcription, folding, translation and turnover. In bacteria, RNA-binding proteins may be specific for a few RNA targets (e.g., several ribosomal proteins that recognize both rRNA during ribosome assembly and their own mRNAs when acting as highly specific autogenous repressors) or function as global regulators implicated in numerous regulatory networks. Some RNA-binding proteins combine all these features, and this particularly concerns the ribosomal protein S1 and the Sm-like protein Hfq. S1 is a key mRNA-binding protein in gram-negative bacteria; it recognizes mRNA leaders and provides binding of diverse mRNAs to the ribosome at the initiation step of translation. Moreover, S1 is a highly specific autogenous repressor that is able to distinguish its own mRNA from all the others. Hfq is recognized as a global regulator that facilitates small RNA-mRNA interactions in bacteria; it thereby controls the expression of many mRNAs either positively or negatively. In addition, these two proteins were reported to affect transcription, RNA degradation and other processes. Although they have no sequence specificity, Hfq and S1 preferentially bind A/U-rich single-stranded RNA regions; despite this, they nevertheless carry out very different tasks in the cell. This review is focused on the diversity of functions that can be performed by these abundant RNA-binding bacterial proteins.

MeSH Terms
Bacterial Proteins/chemistry,metabolism Gene Expression Regulation Host Factor 1 Protein/chemistry,metabolism Humans Ribosomal Proteins/chemistry,metabolism
Chemicals
Bacterial Proteins Host Factor 1 Protein Ribosomal Proteins ribosomal protein S1
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hajnsdorf Eliane
CNRS UPR9073, Associated with University Paris Diderot, Sorbonne Paris Cité, Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France. Eliane.Hajnsdorf@ibpc.fr
Boni Irina V
Article Info
Journal
Biochimie
Abbr.
Biochimie
ISSN
1638-6183
Published
2012-07-00
Epub
2012-00-18
Pages
1544-53
Language
English
Region
France
NLM ID
1264604
Subset
IM
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