Structural Insights into the Role of Diphthamide on Elongation Factor 2 in mRNA Reading-Frame Maintenance

被引：37
|
作者：
Pellegrino, Simone [1 ]
Demeshkina, Natalia [1 ,5 ]
Mancera-Martinez, Eder [2 ]
Melnikov, Sergey [1 ,6 ]
Simonetti, Angelita [2 ]
Myasnikov, Alexander [1 ]
Yusupov, Marat [1 ,3 ]
Yusupova, Gulnara [1 ]
Hashem, Yaser [4 ]
机构：
[1] Univ Strasbourg, Inst Genet & Mol & Cellular Biol, Dept Integrated Struct Biol, CNRS UMR710,INSERM U964, F-67000 Strasbourg, France
[2] Univ Strasbourg, Inst Mol & Cellular Biol, CNRS UPR9002, Architecture & React RNA, F-67084 Strasbourg, France
[3] Kazan Fed Univ, Inst Fundamental Med & Biol, Kazan 420008, Russia
[4] U1212 Univ Bordeaux, ARNA, IECB, INSERM, F-33600 Pessac, France
[5] NHLBI, Biochem & Biophys Ctr, Bldg 10, Bethesda, MD 20892 USA
[6] Yale Univ, Dept Mol Biophys & Biochem, POB 6666, New Haven, CT 06520 USA
来源：
JOURNAL OF MOLECULAR BIOLOGY | 2018年 / 430卷 / 17期
基金：
欧洲研究理事会;
关键词：
ribosome translocation; cryo-EM; eEF2; diphthamide; reading-frame maintenance; CRYO-EM; ELECTRON-MICROGRAPHS; FACTOR EEF2; RIBOSOME; TRANSLOCATION; TRANSLATION; MICROSCOPY; CRYSTALLOGRAPHY; VISUALIZATION; VALIDATION;
D O I：
10.1016/j.jmb.2018.06.006
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：
One of the most critical steps of protein biosynthesis is the coupled movement of mRNA, which encodes genetic information, with tRNAs on the ribosome. In eukaryotes, this process is catalyzed by a conserved G-protein, the elongation factor 2 (eEF2), which carries a unique post-translational modification, called diphthamide, found in all eukaryotic species. Here we present near-atomic resolution cryo-electron microscopy structures of yeast 80S ribosome complexes containing mRNA, tRNA and eEF2 trapped in different GTP-hydrolysis states which provide further structural insights into the role of diphthamide in the mechanism of translation fidelity in eukaryotes. (C) 2018 Elsevier Ltd. All rights reserved.
引用
收藏
页码：2677 / 2687
页数：11
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