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

被引:98
作者
Agirrezabala, Xabier [1 ]
Frank, Joachim [1 ,2 ]
机构
[1] Columbia Univ, Howard Hughes Med Inst, Dept Biochem & Mol Biophys, New York, NY 10032 USA
[2] Columbia Univ, Dept Biol Sci, New York, NY 10032 USA
关键词
AMINOACYL-TRANSFER-RNA; PEPTIDE-BOND FORMATION; LARGE CONFORMATIONAL-CHANGES; CODON-ANTICODON RECOGNITION; SITE-DIRECTED MUTAGENESIS; COLI 70S RIBOSOME; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; HYBRID-STATE; STRUCTURAL BASIS;
D O I
10.1017/S0033583509990060
中图分类号
Q6 [生物物理学];
学科分类号
071011 [生物物理学];
摘要
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,
引用
收藏
页码:159 / 200
页数:42
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