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RNA-protein distance patterns in ribosomes reveal the mechanism of translational attenuation.

Authors
  • Yu, DongMei
  • Zhang, Chao
  • Qin, PeiWu
  • Cornish, Peter V
  • Xu, Dong
Type
Published Article
Journal
Science China. Life sciences
Publication Date
Nov 01, 2014
Volume
57
Issue
11
Pages
1131–1139
Identifiers
DOI: 10.1007/s11427-014-4753-8
PMID: 25326828
Source
Medline
License
Unknown

Abstract

Elucidating protein translational regulation is crucial for understanding cellular function and drug development. A key molecule in protein translation is ribosome, which is a super-molecular complex extensively studied for more than a half century. The structure and dynamics of ribosome complexes were resolved recently thanks to the development of X-ray crystallography, Cryo-EM, and single molecule biophysics. Current studies of the ribosome have shown multiple functional states, each with a unique conformation. In this study, we analyzed the RNA-protein distances of ribosome (2.5 MDa) complexes and compared these changes among different ribosome complexes. We found that the RNA-protein distance is significantly correlated with the ribosomal functional state. Thus, the analysis of RNA-protein binding distances at important functional sites can distinguish ribosomal functional states and help understand ribosome functions. In particular, the mechanism of translational attenuation by nascent peptides and antibiotics was revealed by the conformational changes of local functional sites.

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