| Literature DB >> 25376914 |
Alexander G Myasnikov1, Zhanna A Afonina2, Jean-François Ménétret1, Vladimir A Shirokov2, Alexander S Spirin2, Bruno P Klaholz1.
Abstract
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.Mesh:
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Year: 2014 PMID: 25376914 DOI: 10.1038/ncomms6294
Source DB: PubMed Journal: Nat Commun ISSN: 2041-1723 Impact factor: 14.919