Crystal structures of the ribosome in complex with release factors RF1 and RF2 bound to a cognate stop codon

被引：201

作者：

Petry, S ^{[1
]}

Brodersen, DE ^{[1
]}

Murphy, FV ^{[1
]}

Dunham, CM ^{[1
]}

Selmer, M ^{[1
]}

Tarry, MJ ^{[1
]}

Kelley, AC ^{[1
]}

Ramakrishnan, V ^{[1
]}

机构：

[1] MRC, Mol Biol Lab, Cambridge CB2 2QH, England

来源：

CELL | 2005年 / 123卷 / 07期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1016/j.cell.2005.09.039

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：

During protein synthesis, translational release factors catalyze the release of the polypeptide chain when a stop codon on the mRNA reaches the A site of the ribosome. The detailed mechanism of this process is currently unknown. We present here the crystal structures of the ribosome from Thermus thermophilus with RF1 and RF2 bound to their cognate stop codons, at resolutions of 5.9 angstrom and 6.7 angstrom, respectively. The structures reveal details of interactions of the factors with the ribosome and mRNA, including elements previously implicated in decoding and peptide release. They also shed light on conformational changes both in the factors and in the ribosome during termination. Differences seen in the interaction of RF1 and RF2 with the RF1 region of the ribosome allow us to rationalize previous biochemical data. Finally, this work demonstrates the feasibility of crystallizing ribosomes with bound factors at a defined state along the translational pathway.

引用

页码：1255 / 1266

页数：12

共 56 条

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