Distinct eRF3 requirements suggest alternate eRF1 conformations mediate peptide release during eukaryotic translation termination

被引：58

作者：

Fan-Minogue, Hua ^{[1
]}

Du, Ming ^{[1
]}

Pisarev, Andrey V. ^{[2
]}

Kallmeyer, Adam K. ^{[1
]}

Salas-Marco, Joe ^{[1
]}

Keeling, Kim M. ^{[1
]}

Thompson, Sunnie R. ^{[1
]}

Pestova, Tatyana V. ^{[2
]}

Bedwell, David M. ^{[1
]}

机构：

[1] Univ Alabama, Dept Microbiol, Birmingham, AL 35294 USA

[2] Suny Downstate Med Ctr, Dept Microbiol & Immunol, Brooklyn, NY 11203 USA

来源：

MOLECULAR CELL | 2008年 / 30卷 / 05期

关键词：

D O I：

10.1016/j.molcel.2008.03.020

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：

Organisms that use the standard genetic code recognize UAA, UAG, and UGA as stop codons, whereas variant code species frequently alter this pattern of stop codon recognition. We previously demonstrated that a hybrid eRF1 carrying the Euplotes octocarinatus domain 1 fused to Saccharomyces cerevisiae domains 2 and 3 (Eo/Sc eRF1) recognized UAA and UAG, but not UGA, as stop codons. In the current study, we identified mutations in Eo/Sc eRF1 that restore UGA recognition and define distinct roles for the TASNIKS and YxCxxxF motifs in eRF1 function. Mutations in or near the YxCxxxF motif support the cavity model for stop codon recognition by eRF1. Mutations in the TASNIKS motif eliminated the eRF3 requirement for peptide release at UAA and UAG codons, but not UGA codons. These results suggest that the TASNIKS motif and eRF3 function together to trigger eRF1 conformational changes that couple stop codon recognition and peptide release during eukaryotic translation termination.

引用

页码：599 / 609

页数：11

共 31 条

[1] In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3 [J].