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PMID: 20192783 Published · ppublish English Journal Article Review

Single ribosome dynamics and the mechanism of translation.

Annual review of biophysics ·Vol. 39 ·2010-00-00 ·Pages 491-513

Aitken CE, Petrov A, Puglisi JD

Abstract

Our current understanding of the mechanism of translation is based on nearly fifty years of biochemical and biophysical studies. This mechanism, which requires the ribosome to manipulate tRNA and step repetitively along the mRNA, implies movement. High-resolution structures of the ribosome and its ligands have recently described translation in atomic detail, capturing the endpoints of large-scale rearrangements of the ribosome. Direct observation of the dynamic events that underlie the mechanism of translation is challenged by ensemble averaging in bulk solutions. Single-molecule methods, which eliminate these averaging effects, have emerged as powerful tools to probe the mechanism of translation. Single-molecule fluorescence experiments have described the dynamic motion of the ribosome and tRNA. Single-molecule force measurements have directly probed the forces stabilizing ribosomal complexes. Recent developments have allowed real-time observation of ribosome movement and dynamics during translation. This review covers the contributions of single-molecule studies to our understanding of the dynamic nature of translation.

MeSH Terms
Eukaryotic Cells/metabolism Fluorescence Models, Biological Prokaryotic Cells/metabolism Protein Biosynthesis RNA, Messenger/metabolism RNA, Transfer/metabolism Ribosomes/chemistry,metabolism
Chemicals
RNA, Messenger RNA, Transfer
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Aitken Colin Echeverría
Biophysics Program, Stanford University, Stanford, California 94305-5126, USA. [email protected]
Petrov Alexey
Puglisi Joseph D
Article Info
Journal
Annual review of biophysics
Abbr.
Annu Rev Biophys
ISSN
1936-1238
Published
2010-00-00
Pages
491-513
Language
English
Region
United States
NLM ID
101469708
Subset
IM
Grants
NIGMS NIH HHS · R01 GM051266 · United States
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