Science China Life Sciences

, Volume 57, Issue 11, pp 1131–1139

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

Open Access
Research Paper

DOI: 10.1007/s11427-014-4753-8

Cite this article as:
Yu, D., Zhang, C., Qin, P. et al. Sci. China Life Sci. (2014) 57: 1131. doi:10.1007/s11427-014-4753-8

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.

Keywords

ribosome protein translation antibiotics translocation RNA-protein interaction 

Copyright information

© The Author(s) 2014

Authors and Affiliations

  1. 1.Department of Biological EngineeringUniversity of MissouriColumbiaUSA
  2. 2.C.S. Bond Life Science CenterUniversity of MissouriColumbiaUSA
  3. 3.Department of Computer ScienceUniversity of MissouriColumbiaUSA
  4. 4.Department of BiochemistryUniversity of MissouriColumbiaUSA

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