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翻译延伸作为核糖体、tRNA 以及延伸因子 EF-G 和 EF-Tu 之间的动态相互作用。

Elongation in translation as a dynamic interaction among the ribosome, tRNA, and elongation factors EF-G and EF-Tu.

机构信息

The Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA.

出版信息

Q Rev Biophys. 2009 Aug;42(3):159-200. doi: 10.1017/S0033583509990060.

DOI:10.1017/S0033583509990060
PMID:20025795
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2832932/
Abstract

The ribosome is a complex macromolecular machine that translates the message encoded in the messenger RNA and synthesizes polypeptides by linking the individual amino acids carried by the cognate transfer RNAs (tRNAs). The protein elongation cycle, during which the tRNAs traverse the ribosome in a coordinated manner along a path of more than 100 A, is facilitated by large-scale rearrangements of the ribosome. These rearrangements go hand in hand with conformational changes of tRNA as well as elongation factors EF-Tu and EF-G - GTPases that catalyze tRNA delivery and translocation, respectively. This review focuses on the structural data related to the dynamics of the ribosomal machinery, which are the basis, in conjunction with existing biochemical, kinetic, and fluorescence resonance energy transfer data, of our knowledge of the decoding and translocation steps of protein elongation.

摘要

核糖体是一种复杂的大分子机器,通过连接携带相应转移 RNA(tRNA)的单个氨基酸,将信使 RNA 中编码的信息翻译成多肽。在蛋白质延伸循环中,tRNA 沿着超过 100Å 的路径以协调的方式穿过核糖体,这一过程由核糖体的大规模重排来促进。这些重排与 tRNA 的构象变化以及伸长因子 EF-Tu 和 EF-G-GTP 酶携手并进,分别催化 tRNA 的递呈和易位。本综述重点介绍与核糖体机制动力学相关的结构数据,这些数据与现有的生化、动力学和荧光共振能量转移数据一起,构成了我们对蛋白质延伸的解码和易位步骤的理解的基础。

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Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome.从完整70S核糖体肽基转移酶中心的快照中洞察底物稳定性。
Nat Struct Mol Biol. 2009 May;16(5):528-33. doi: 10.1038/nsmb.1577. Epub 2009 Apr 12.
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Fidelity at the molecular level: lessons from protein synthesis.分子水平的保真度:蛋白质合成的启示。
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