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 language | English (US) |
|---|---|
| Pages (from-to) | 163-189 |
| Number of pages | 27 |
| Journal | Quarterly Reviews of Biophysics |
| Volume | 40 |
| Issue number | 2 |
| DOIs | |
| State | Published - May 2007 |
Fingerprint
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 journal › Article
}
TY - JOUR
T1 - Quantitative studies of ribosome conformational dynamics
AU - Fraser, Christopher S.
AU - Doudna, Jennifer A.
PY - 2007/5
Y1 - 2007/5
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=37149010437&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=37149010437&partnerID=8YFLogxK
U2 - 10.1017/S0033583507004647
DO - 10.1017/S0033583507004647
M3 - Article
C2 - 18072984
AN - SCOPUS:37149010437
VL - 40
SP - 163
EP - 189
JO - Quarterly Reviews of Biophysics
JF - Quarterly Reviews of Biophysics
SN - 0033-5835
IS - 2
ER -