Quantitative studies of ribosome conformational dynamics

被引:7
作者
Fraser, Christopher S. [1 ,2 ]
Doudna, Jennifer A. [1 ,2 ]
机构
[1] Univ Calif Berkeley, Howard Hughes Med Inst, Dept Mol & Cell Biol, Berkeley, CA 94720 USA
[2] Univ Calif Berkeley, Howard Hughes Med Inst, Dept Chem, Berkeley, CA 94720 USA
关键词
D O I
10.1017/S0033583507004647
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
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.
引用
收藏
页码:163 / 189
页数:27
相关论文
共 169 条
[1]   Visualization of ribosome-recycling factor on the Escherichia coli 70S ribosome:: Functional implications [J].
Agrawal, RK ;
Sharma, MR ;
Kiel, MC ;
Hirokawa, G ;
Booth, TM ;
Spahn, CMT ;
Grassucci, RA ;
Kaji, A ;
Frank, J .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (24) :8900-8905
[2]   Direct visualization of A-, P-, and E-site transfer RNAs in the Escherichia coli ribosome [J].
Agrawal, RK ;
Penczek, P ;
Grassucci, RA ;
Li, YH ;
Leith, A ;
Nierhaus, KH ;
Frank, J .
SCIENCE, 1996, 271 (5251) :1000-1002
[3]   Visualization of elongation factor G on the Escherichia coli 70S ribosome:: The mechanism of translocation [J].
Agrawal, RK ;
Penczek, P ;
Grassucci, RA ;
Frank, J .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (11) :6134-6138
[4]   Development and characterization of a reconstituted yeast translation initiation system [J].
Algire, MA ;
Maag, D ;
Savio, P ;
Acker, MG ;
Tarun, SZ ;
Sachs, AB ;
Asano, K ;
Nielsen, KH ;
Olsen, DS ;
Phan, L ;
Hinnebusch, AG ;
Lorsch, JR .
RNA, 2002, 8 (03) :382-397
[5]   Structural insights on the translation initiation complex: ghosts of a universal initiation complex [J].
Allen, Gregory S. ;
Frank, Joachim .
MOLECULAR MICROBIOLOGY, 2007, 63 (04) :941-950
[6]   The cryo-EM structure of a translation initiation complex from Escherichia coli [J].
Allen, GS ;
Zavialov, A ;
Gursky, R ;
Ehrenberg, M ;
Frank, J .
CELL, 2005, 121 (05) :703-712
[7]   The roles of initiation factor 2 and guanosine triphosphate in initiation of protein synthesis [J].
Antoun, A ;
Pavlov, MY ;
Andersson, K ;
Tenson, T ;
Ehrenberg, M .
EMBO JOURNAL, 2003, 22 (20) :5593-5601
[8]   Ribosome formation from subunits studied by stopped-flow and Rayleigh light scattering [J].
Antoun A. ;
Pavlov M.Y. ;
Tenson T. ;
Ehrenberg M. .
Biological Procedures Online, 2004, 6 (1) :35-54
[9]  
BENNE R, 1978, J BIOL CHEM, V253, P3078
[10]  
Benne R, 1979, Methods Enzymol, V60, P15