Publications
2003
Sauter C, Basquin J, Suck D
Sm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coli Journal Article
In: Nucleic Acids Res, vol. 31, no. 14, pp. 4091-4098, 2003, ISBN: 12853626, (1362-4962 Journal Article).
Abstract | Links | BibTeX | Tags: Amino Acid Support, Amino Acid Sequence Bacteria/*genetics Crystallography, FRUGIER, Molecular Host Factor 1 Protein/chemistry/*genetics Molecular Sequence Data Protein Conformation Protein Structure, Non-U.S. Gov't, SAUTER, Secondary Ribonucleoproteins, Small Nuclear/chemistry/*genetics Sequence Alignment Sequence Homology, Unité ARN, X-Ray Dimerization Escherichia coli Proteins/chemistry/*genetics Evolution
@article{,
title = {Sm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coli},
author = {C Sauter and J Basquin and D Suck},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12853626},
isbn = {12853626},
year = {2003},
date = {2003-01-01},
journal = {Nucleic Acids Res},
volume = {31},
number = {14},
pages = {4091-4098},
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.},
note = {1362-4962
Journal Article},
keywords = {Amino Acid Support, Amino Acid Sequence Bacteria/*genetics Crystallography, FRUGIER, Molecular Host Factor 1 Protein/chemistry/*genetics Molecular Sequence Data Protein Conformation Protein Structure, Non-U.S. Gov't, SAUTER, Secondary Ribonucleoproteins, Small Nuclear/chemistry/*genetics Sequence Alignment Sequence Homology, Unité ARN, X-Ray Dimerization Escherichia coli Proteins/chemistry/*genetics Evolution},
pubstate = {published},
tppubtype = {article}
}
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.