Structure of the mammalian ribosomal pre-termination complex associated with eRF1•eRF3•GDPNP

被引：55

作者：

des Georges, Amedee ^{[1
,2
]}

Hashem, Yaser ^{[1
,2
]}

Unbehaun, Anett ^{[3
]}

Grassucci, Robert A. ^{[1
,2
]}

Taylor, Derek ^{[4
]}

Hellen, Christopher U. T. ^{[3
]}

Pestova, Tatyana V. ^{[3
]}

Frank, Joachim ^{[1
,2
,5
]}

机构：

[1] Howard Hughes Med Inst, Chevy Chase, MD 20815 USA

[2] Columbia Univ, Dept Biochem & Mol Biophys, New York, NY USA

[3] Suny Downstate Med Ctr, Dept Cell Biol, Brooklyn, NY 11203 USA

[4] Case Western Reserve Univ, Dept Pharmacol, Cleveland, OH 44106 USA

[5] Columbia Univ, Dept Biol Sci, New York, NY 10027 USA

来源：

NUCLEIC ACIDS RESEARCH | 2014年 / 42卷 / 05期

关键词：

STOP CODON RECOGNITION; EUKARYOTIC TRANSLATION TERMINATION; TRANSFER-RNA HYDROLYSIS; RELEASE FACTOR ERF1; CRYO-EM STRUCTURE; AMINOACYL-TRANSFER-RNA; CRYSTAL-STRUCTURE; SACCHAROMYCES-CEREVISIAE; MOLECULAR-DYNAMICS; GTP HYDROLYSIS;

D O I：

10.1093/nar/gkt1279

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：

Eukaryotic translation termination results from the complex functional interplay between two release factors, eRF1 and eRF3, in which GTP hydrolysis by eRF3 couples codon recognition with peptidyl-tRNA hydrolysis by eRF1. Here, we present a cryoelectron microscopy structure of pre-termination complexes associated with eRF1 center dot eRF3 center dot GDPNP at 9.7-angstrom resolution, which corresponds to the initial pre-GTP hydrolysis stage of factor attachment and stop codon recognition. It reveals the ribosomal positions of eRFs and provides insights into the mechanisms of stop codon recognition and triggering of eRF3's GTPase activity.

引用

页码：3409 / 3418

页数：10

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