Structural basis for translation termination by archaeal RF1 and GTP-bound EF1α complex.

Structural basis for translation termination by archaeal RF1 and GTP-bound EF1α complex.
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DOI:
10.1093/nar/gks660
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发表时间:
2012-10
影响因子:
14.9
通讯作者:
Nureki O
Nureki O
中科院分区:
生物学2区
文献类型:
--
作者:
Kobayashi K;Saito K;Ishitani R;Ito K;Nureki O

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当终止密码子出现在核糖体A位点时,I类和II类释放因子(RF)终止翻译。在真核生物和古细菌中,I类和II类RF形成异二聚体复合物,并以GTP依赖的方式完成整个翻译终止过程。然而,I类和II类RF复合物的翻译终止的结构机制仍然没有得到解决。在古细菌中,古细菌延伸因子1 α(aEF 1 α)是tRNA的载体,通过与古细菌RF 1(aRF 1)形成异二聚体复合物而作为II类RF。我们报道了第一个活性I类和II类RF复合物aRF 1·aEF 1 α复合物的晶体结构。这种结构非常类似于tRNA·EF-Tu复合物,表明aRF 1通过模拟tRNA有效地传递到核糖体A位点。它提供了深入了解耦合GTP水解II类RF终止密码子识别和肽基-tRNA水解I类RF的机制。我们讨论了aEF 1 α识别aRF 1和aPelota(另一种aRF 1相关蛋白)的不同机制以及aEF 1 α三种功能的分子进化。
When a stop codon appears at the ribosomal A site, the class I and II release factors (RFs) terminate translation. In eukaryotes and archaea, the class I and II RFs form a heterodimeric complex, and complete the overall translation termination process in a GTP-dependent manner. However, the structural mechanism of the translation termination by the class I and II RF complex remains unresolved. In archaea, archaeal elongation factor 1 alpha (aEF1α), a carrier GTPase for tRNA, acts as a class II RF by forming a heterodimeric complex with archaeal RF1 (aRF1). We report the crystal structure of the aRF1·aEF1α complex, the first active class I and II RF complex. This structure remarkably resembles the tRNA·EF–Tu complex, suggesting that aRF1 is efficiently delivered to the ribosomal A site, by mimicking tRNA. It provides insights into the mechanism that couples GTP hydrolysis by the class II RF to stop codon recognition and peptidyl-tRNA hydrolysis by the class I RF. We discuss the different mechanisms by which aEF1α recognizes aRF1 and aPelota, another aRF1-related protein and molecular evolution of the three functions of aEF1α.
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