Structural basis for ribosome recycling by RRF and tRNA.

Structural basis for ribosome recycling by RRF and tRNA.
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RRF 和 tRNA 回收核糖体的结构基础

DOI:
10.1038/s41594-019-0350-7
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发表时间:
2020-01
影响因子:
16.8
通讯作者:
Gagnon, Matthieu G.
Gagnon, Matthieu G.
中科院分区:
生物学1区
文献类型:
--
作者:
Zhou, Dejian;Tanzawa, Takehito;Lin, Jinzhong;Gagnon, Matthieu G.

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细菌核糖体通过两种保守蛋白质——延伸因子G(EF - G)和核糖体循环因子(RRF)被循环为亚基。RRF和EF - G进行核糖体循环的分子基础仍不清楚。在此,我们报道了分辨率为3.5 Å的终止后嗜热栖热菌70S核糖体与EF - G、RRF以及两种tRNA形成的复合物的晶体结构。P位点的去酰化tRNA移动到一种之前未被发现的结合状态(肽酰/循环;p/R),该状态类似于起始过程中所观察到的状态。p/R - tRNA的末端与50S亚基形成不利的接触,同时RRF楔入中央亚基间桥附近,这阐明了tRNA和RRF在核糖体亚基解离中的积极作用。该结构揭示了tRNA在P位点和E位点之间转移时缺失的一个瞬间状态,为核糖体循环和tRNA易位的机制提供了见解。
The bacterial ribosome is recycled into subunits by two conserved proteins, elongation factor G (EF-G) and the ribosome recycling factor (RRF). The molecular basis for ribosome recycling by RRF and EF-G remains unclear. Here, we report the crystal structure of a postterminationThermus thermophilus70S ribosome complexed with EF-G, RRF and two transfer RNAs at a resolution of 3.5 Å. The deacylated tRNA in the peptidyl (P) site moves into a previously unsuspected state of binding (peptidyl/recycling, p/R) that is analogous to that seen during initiation. The terminal end of the p/R-tRNA forms nonfavorable contacts with the 50S subunit while RRF wedges next to central inter-subunit bridges, illuminating the active roles of tRNA and RRF in dissociation of ribosomal subunits. The structure uncovers a missing snapshot of tRNA as it transits between the P and exit (E) sites, providing insights into the mechanisms of ribosome recycling and tRNA translocation.
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发表时间: 2013-11-15
期刊: Science (New York, N.Y.)
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