Quantitative studies of ribosome conformational dynamics

Christopher S. Fraser, Jennifer A. Doudna

Research output: Contribution to journalArticle

9 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)163-189
Number of pages27
JournalQuarterly Reviews of Biophysics
Volume40
Issue number2
DOIs
StatePublished - May 2007

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Ribosomes
Peptide Initiation Factors
Proteins
X-Ray Emission Spectrometry
Cryoelectron Microscopy
Initiator Codon
X Ray Crystallography
Molecular Dynamics Simulation
Eukaryota
Bacteria
Messenger RNA

ASJC Scopus subject areas

  • Biophysics

Cite this

Quantitative studies of ribosome conformational dynamics. / Fraser, Christopher S.; Doudna, Jennifer A.

In: Quarterly Reviews of Biophysics, Vol. 40, No. 2, 05.2007, p. 163-189.

Research output: Contribution to journalArticle

Fraser, Christopher S. ; Doudna, Jennifer A. / Quantitative studies of ribosome conformational dynamics. In: Quarterly Reviews of Biophysics. 2007 ; Vol. 40, No. 2. pp. 163-189.
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