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RNA-protein distance patterns in ribosomes reveal the mechanism of translational attenuation.
MedLine Citation:
PMID:  25326828     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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.
Authors:
DongMei Yu; Chao Zhang; PeiWu Qin; Peter V Cornish; Dong Xu
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2014-10-18
Journal Detail:
Title:  Science China. Life sciences     Volume:  -     ISSN:  1869-1889     ISO Abbreviation:  Sci China Life Sci     Publication Date:  2014 Oct 
Date Detail:
Created Date:  2014-10-19     Completed Date:  -     Revised Date:  2014-10-20    
Medline Journal Info:
Nlm Unique ID:  101529880     Medline TA:  Sci China Life Sci     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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