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PMID: 12093755 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Structures of the pleiotropic translational regulator Hfq and an Hfq-RNA complex: a bacterial Sm-like protein.

The EMBO journal ·Vol. 21 ·No. 13 ·2002-07-01 ·Pages 3546-56

Schumacher MA, Pearson RF, Møller T, Valentin-Hansen P, Brennan RG

Abstract

In prokaryotes, Hfq regulates translation by modulating the structure of numerous RNA molecules by binding preferentially to A/U-rich sequences. To elucidate the mechanisms of target recognition and translation regulation by Hfq, we determined the crystal structures of the Staphylococcus aureus Hfq and an Hfq-RNA complex to 1.55 and 2.71 A resolution, respectively. The structures reveal that Hfq possesses the Sm-fold previously observed only in eukaryotes and archaea. However, unlike these heptameric Sm proteins, Hfq forms a homo-hexameric ring. The Hfq-RNA structure reveals that the single-stranded hepta-oligoribonucleotide binds in a circular conformation around a central basic cleft, whereby Tyr42 residues from adjacent subunits stack with six of the bases, and Gln8, outside the Sm motif, provides key protein-base contacts. Such binding suggests a mechanism for Hfq function.

MeSH Terms
Amino Acid Motifs Amino Acid Sequence Carrier Proteins/chemistry,metabolism,ultrastructure Cryoelectron Microscopy Crystallography, X-Ray Gene Expression Regulation, Bacterial Host Factor 1 Protein Integration Host Factors Macromolecular Substances Models, Molecular Molecular Sequence Data Nucleic Acid Conformation Protein Binding Protein Biosynthesis Protein Conformation Protein Structure, Tertiary RNA, Bacterial/chemistry,metabolism,ultrastructure RNA, Messenger/chemistry,metabolism,ultrastructure Recombinant Fusion Proteins/chemistry Sequence Alignment Sequence Homology, Amino Acid Staphylococcus aureus/chemistry Substrate Specificity
Chemicals
Carrier Proteins Host Factor 1 Protein Integration Host Factors Macromolecular Substances RNA, Bacterial RNA, Messenger Recombinant Fusion Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Schumacher Maria A
Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, OR 97201-3098, USA.
Pearson Robert F
Møller Thorleif
Valentin-Hansen Poul
Brennan Richard G
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
DOI
10.1093/emboj/cdf322
Published
2002-07-01
Pages
3546-56
Language
English
Region
England
NLM ID
8208664
PMCID
PMC126077
Subset
IM
Grants
NIGMS NIH HHS · GM 49244 · United States
Databases
PDB
1QK1, 1QK2
External Links
PubMed source DOI: 10.1093/emboj/cdf322 PMC Full Text View journal details
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