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

被引:350
作者
Schumacher, MA
Pearson, RF
Moller, T
Valentin-Hansen, P
Brennan, RG [1 ]
机构
[1] Oregon Hlth & Sci Univ, Dept Biochem & Mol Biol, Portland, OR 97201 USA
[2] Univ So Denmark, Dept Biochem & Mol Biol, DK-5230 Odense M, Denmark
关键词
Hfq; protein-RNA complex; RNA-binding protein; Sm; translation regulation;
D O I
10.1093/emboj/cdf322
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 Angstrom 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.
引用
收藏
页码:3546 / 3556
页数:11
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