PMID:12853626

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Citation

Sauter, C, Basquin, J and Suck, D (2003) Sm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coli. Nucleic Acids Res. 31:4091-8

Abstract

The Hfq protein was discovered in Escherichia coli in the early seventies as a host factor for the Qbeta phage RNA replication. During the last decade, it was shown to be involved in many RNA processing events and remote sequence homology indicated a link to spliceosomal Sm proteins. We report the crystal structure of the E.coli Hfq protein showing that its monomer displays a characteristic Sm-fold and forms a homo-hexamer, in agreement with former biochemical data. Overall, the structure of the E.coli Hfq ring is similar to the one recently described for Staphylococcus aureus. This confirms that bacteria contain a hexameric Sm-like protein which is likely to be an ancient and less specialized form characterized by a relaxed RNA binding specificity. In addition, we identified an Hfq ortholog in the archaeon Methanococcus jannaschii which lacks a classical Sm/Lsm gene. Finally, a detailed structural comparison shows that the Sm-fold is remarkably well conserved in bacteria, Archaea and Eukarya, and represents a universal and modular building unit for oligomeric RNA binding proteins.

Links

PubMed PMC167641

Keywords

Amino Acid Sequence; Autoantigens; Bacteria/genetics; Crystallography, X-Ray; Dimerization; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Evolution, Molecular; Host Factor 1 Protein/chemistry; Host Factor 1 Protein/genetics; Molecular Sequence Data; Protein Conformation; Protein Structure, Secondary; Ribonucleoproteins, Small Nuclear/chemistry; Ribonucleoproteins, Small Nuclear/genetics; Sequence Alignment; Sequence Homology, Amino Acid; snRNP Core Proteins

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