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Quantitative studies of ribosome conformational dynamics

Published online by Cambridge University Press:  12 December 2007

Christopher S. Fraser  and
Jennifer A. Doudna
Christopher S. Fraser
Affiliation:
Department of Molecular and Cell Biology & Department of Chemistry, Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA, USA
Jennifer A. Doudna*
Affiliation:
Department of Molecular and Cell Biology & Department of Chemistry, Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA, USA
*
*Author for correspondence: Dr J. A. Doudna, Department of Molecular and Cell Biology & Department of Chemistry, Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, CA, USA. Tel.: (510) 643-0225; Fax: (510) 643-0080; Email: doudna@berkeley.edu
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Abstract

The ribosome is a dynamic machine that undergoes many conformational rearrangements during the initiation of protein synthesis. Significant differences exist between the process of protein synthesis initiation in eubacteria and eukaryotes. In particular, the initiation of eukaryotic protein synthesis requires roughly an order of magnitude more initiation factors to promote efficient mRNA recruitment and ribosomal recognition of the start codon than are needed for eubacterial initiation. The mechanisms by which these initiation factors promote ribosome conformational changes during stages of initiation have been studied using cross-linking, footprinting, site-directed probing, cryo-electron microscopy, X-ray crystallography, fluorescence spectroscopy and single-molecule techniques. Here, we review how the results of these different approaches have begun to converge to yield a detailed molecular understanding of the dynamic motions that the eukaryotic ribosome cycles through during the initiation of protein synthesis.

Type
Review Article
Information
Quarterly Reviews of Biophysics , Volume 40 , Issue 2 , May 2007 , pp. 163 - 189
Copyright
Copyright © Cambridge University Press 2007

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