The hybrid state of tRNA binding is an authentic translation elongation intermediate

被引：100

作者：

Dorner, S ^{[1
]}

Brunelle, JL ^{[1
]}

Sharma, D ^{[1
]}

Green, R ^{[1
]}

机构：

[1] Johns Hopkins Univ, Sch Med, Dept Mol Biol & Genet, Howard Hughes Med Inst, Baltimore, MD 21205 USA

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2006年 / 13卷 / 03期

关键词：

D O I：

10.1038/nsmb1060

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 GTPase elongation factor ( EF)-G is responsible for promoting the translocation of the messenger RNA-transfer RNA complex on the ribosome, thus opening up the A site for the next aminoacyl-tRNA. Chemical modification and cryo-EM studies have indicated that tRNAs can bind the ribosome in an alternative 'hybrid' state after peptidyl transfer and before translocation, though the relevance of this state during translation elongation has been a subject of debate. Here, using pre-steady-state kinetic approaches and mutant analysis, we show that translocation by EF-G is most efficient when tRNAs are bound in a hybrid state, supporting the argument that this state is an authentic intermediate during translation.

引用

页码：234 / 241

页数：8

共 42 条

[1] Effect of buffer conditions on the position of tRNA on the 70 S ribosome as visualized by cryoelectron microscopy [J].