Structural and functional studies revealed key mechanisms underlying elongation step of protein translation

被引:4
|
作者
Zhang, Ling [1 ]
Wang, Yinghui [1 ]
Dai, Hong [1 ]
Zhou, Jie [1 ]
机构
[1] Zhejiang Univ, Life Sci Inst, Hangzhou 310058, Peoples R China
基金
浙江省自然科学基金;
关键词
ribosome; elongation; translocation; LARGE RIBOSOMAL-SUBUNIT; PEPTIDE-BOND FORMATION; AMINOACYL-TRANSFER-RNA; MESSENGER-RNA; CRYSTAL-STRUCTURE; INTERSUBUNIT MOVEMENT; CODING SPECIFICITY; DECODING CENTER; INDUCED-FIT; FACTOR TU;
D O I
10.1093/abbs/gmaa046
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The ribosome is an ancient and universally conserved macromolecular machine that synthesizes proteins in all organisms. Since the discovery of the ribosome by electron microscopy in the mid-1950s, rapid progress has been made in research on it, regarding its architecture and functions. As a machine that synthesizes polypeptides, the sequential addition of amino acids to a growing polypeptide chain occurs during a phase called the elongation cycle. This is the core step of protein translation and is highly conserved between bacteria and eukarya. The elongation cycle involves codon recognition by aminoacyl tRNAs, catalysis of peptide bond formation, and the most complex operation of translation-translocation. In this review, we discuss the fundamental results from structural and functional studies over the past decades that have led to understanding of the three key questions underlying translation.
引用
收藏
页码:749 / 756
页数:8
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