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Nucleic Acids Research, 2003, Vol. 31, No. 14 4091-4098
© 2003 Oxford University Press

Sm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coli

Claude Sauter, Jérôme Basquin and Dietrich Suck*

European Molecular Biology Laboratory, Structural and Computational Biology Programme, Meyerhofstrasse 1, D-69117 Heidelberg, Germany

*To whom correspondence should be addressed. Tel: +49 6221 387 307; Fax: +49 6221 387 306; Email: suck{at}embl.de
Present address:
Claude Sauter, UPR 9002—CNRS, Institut de Biologie Moléculaire et Cellulaire, 15 Rue René Descartes, F-67084 Strasbourg, France

The Hfq protein was discovered in Escherichia coli in the early seventies as a host factor for the Qß 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.


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