Hfq-bridged ternary complex is important for translation activation of rpoS by DsrA.
Hfq-bridged ternary complex is important for translation activation of rpoS by DsrA.
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DOI：
10.1093/nar/gkt276
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发表时间：
2013-06
影响因子：
14.9
通讯作者：
Shi Y
中科院分区：
文献类型：
--
作者：
Wang W;Wang L;Wu J;Gong Q;Shi Y
rpoS mRNA编码一般应激反应的主调节因子σS，需要Hfq促进的碱基配对与DsrA小RNA在低温下有效翻译。最近有人提出，Hfq作用的一种机制是通过同时结合rpoS和DsrA来桥接瞬时三元复合物。然而，没有Hfq同时结合不同RNA的结构证据被报道。我们检测到Hfq的rpoS和DsrA片段的同时结合。AU 6A·Hfq·A7和Hfq·A7配合物的晶体结构分别用1.8和1.9 μ m分辨率分辨。三元配合物在溶液中得到了进一步的核磁共振证实。在体内，rpoS翻译的激活需要完整的Hfq，其能够将rpoS和DsrA同时桥接成三元复合物。该三元复合物可能对应于Hfq促进的小RNA-mRNA退火过程中的亚稳态过渡态。
The rpoS mRNA, which encodes the master regulator σS of general stress response, requires Hfq-facilitated base pairing with DsrA small RNA for efficient translation at low temperatures. It has recently been proposed that one mechanism underlying Hfq action is to bridge a transient ternary complex by simultaneously binding to rpoS and DsrA. However, no structural evidence of Hfq simultaneously bound to different RNAs has been reported. We detected simultaneous binding of Hfq to rpoS and DsrA fragments. Crystal structures of AU6A•Hfq•A7 and Hfq•A7 complexes were resolved using 1.8- and 1.9-Å resolution, respectively. Ternary complex has been further verified in solution by NMR. In vivo, activation of rpoS translation requires intact Hfq, which is capable of bridging rpoS and DsrA simultaneously into ternary complex. This ternary complex possibly corresponds to a meta-stable transition state in Hfq-facilitated small RNA–mRNA annealing process.
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