The molecular structure of the left-handed supra-molecular helix of eukaryotic polyribosomes

被引:38
|
作者
Myasnikov, Alexander G. [1 ,2 ,3 ,4 ]
Afonina, Zhanna A. [5 ]
Menetret, Jean-Francois [1 ,2 ,3 ,4 ]
Shirokov, Vladimir A. [5 ]
Spirin, Alexander S. [5 ]
Klaholz, Bruno P. [1 ,2 ,3 ,4 ]
机构
[1] IGBMC Inst Genet & Mol & Cellular Biol, Dept Integrated Struct Biol, Ctr Integrat Biol CBI, F-67404 Illkirch Graffenstaden, France
[2] CNRS, UMR 7104, F-67404 Illkirch Graffenstaden, France
[3] INSERM, F-67404 Illkirch Graffenstaden, France
[4] Univ Strasbourg, F-67400 Strasbourg, France
[5] Russian Acad Sci, Inst Prot Res, Moscow 142290, Russia
来源
NATURE COMMUNICATIONS | 2014年 / 5卷
基金
欧洲研究理事会; 俄罗斯基础研究基金会;
关键词
DOUBLE-ROW POLYRIBOSOMES; MESSENGER-RNA; ENDOPLASMIC-RETICULUM; TRANSMISSION ELECTRON; 80S RIBOSOME; CELLS; PROTEIN; VISUALIZATION; ORGANIZATION; TRANSLATION;
D O I
10.1038/ncomms6294
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
During protein synthesis, several ribosomes bind to a single messenger RNA (mRNA) forming large macromolecular assemblies called polyribosomes. Here we report the detailed molecular structure of a 100 MDa eukaryotic poly-ribosome complex derived from cryo electron tomography, sub-tomogram averaging and pseudo-atomic modelling by crystal structure fitting. The structure allowed the visualization of the three functional parts of the polysome assembly, the central core region that forms a rather compact left-handed supra-molecular helix, and the more open regions that harbour the initiation and termination sites at either ends. The helical region forms a continuous mRNA channel where the mRNA strand bridges neighbouring exit and entry sites of the ribosomes and prevents mRNA looping between ribosomes. This structure provides unprecedented insights into protein-and RNA-mediated inter-ribosome contacts that involve conserved sites through 40S subunits and long protruding RNA expansion segments, suggesting a role in stabilizing the overall polyribosomal assembly.
引用
收藏
页数:8
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