Møller Thorleif, Franch Thomas, Højrup Peter, Keene Douglas R, Bächinger Hans Peter, Brennan Richard G, Valentin-Hansen Poul
Department of Biochemistry and Molecular Biology, University of Southern Denmark-Odense, Campusvej 55, DK-5230 M, Odense, Denmark.
Mol Cell. 2002 Jan;9(1):23-30. doi: 10.1016/s1097-2765(01)00436-1.
The bacterial Hfq protein modulates the stability or the translation of mRNAs and has recently been shown to interact with small regulatory RNAs in E. coli. Here we show that Hfq belongs to the large family of Sm and Sm-like proteins: it contains a conserved sequence motif, known as the Sm1 motif, forms a doughnut-shaped structure, and has RNA binding specificity very similar to the Sm proteins. Moreover, we provide evidence that Hfq strongly cooperates in intermolecular base pairing between the antisense regulator Spot 42 RNA and its target RNA. We speculate that Sm proteins in general cooperate in bimolecular RNA-RNA interaction and that protein-mediated complex formation permits small RNAs to interact with a broad range of target RNAs.
细菌Hfq蛋白可调节mRNA的稳定性或翻译，最近研究表明它能与大肠杆菌中的小调节RNA相互作用。我们在此表明，Hfq属于Sm和Sm样蛋白的大家族：它含有一个保守的序列基序，即Sm1基序，形成一种甜甜圈形状的结构，并且具有与Sm蛋白非常相似的RNA结合特异性。此外，我们提供的证据表明，Hfq在反义调节因子Spot 42 RNA与其靶RNA之间的分子间碱基配对中发挥着强有力的协同作用。我们推测，一般来说，Sm蛋白在双分子RNA-RNA相互作用中发挥协同作用，并且蛋白质介导的复合物形成使小RNA能够与广泛的靶RNA相互作用。
