The Molecular Basis of Translational Control

被引:15
作者
Fraser, Christopher S. [1 ]
机构
[1] Univ Calif Davis, Dept Mol & Cellular Biol, Davis, CA 95616 USA
来源
TRANSLATIONAL CONTROL IN HEALTH AND DISEASE | 2009年 / 90卷
关键词
GUANINE-NUCLEOTIDE EXCHANGE; CAP-BINDING-PROTEIN; INITIATION-FACTOR; 3; MESSENGER-RNA STRUCTURE; 40S RIBOSOMAL-SUBUNIT; SACCHAROMYCES-CEREVISIAE HOMOLOG; STOP CODON RECOGNITION; START-SITE SELECTION; C-TERMINAL DOMAIN; FACTOR; EIF5;
D O I
10.1016/S1877-1173(09)90001-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Our current understanding of eukaryotic protein synthesis has emerged from many years of biochemical, genetic and biophysical approaches. Significant insight into the molecular details of the mechanism has been obtained, although there are clearly many aspects of the process that remain to be resolved. Importantly, our understanding of the mechanism has identified a number of key stages in the pathway that contribute to the regulation of general and gene-specific translation. Not surprisingly, translational control is now widely accepted to play a role in aspects of cell stress, growth, development, synaptic function, aging, and disease. This chapter reviews the mechanism of eukaryotic protein synthesis and its relevance to translational control.
引用
收藏
页码:1 / 51
页数:51
相关论文
共 314 条
[1]  
ABRAMSON RD, 1987, J BIOL CHEM, V262, P3826
[2]  
ABRAMSON RD, 1988, J BIOL CHEM, V263, P5462
[3]   Interaction between eukaryotic initiation factors 1A and 5B is required for efficient ribosomal subunit joining [J].
Acker, MG ;
Shin, BS ;
Dever, TE ;
Lorsch, JR .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (13) :8469-8475
[4]   Mechanism of ribosomal subunit joining during eukaryotic translation initiation [J].
Acker, Michael G. ;
Lorsch, Jon R. .
BIOCHEMICAL SOCIETY TRANSACTIONS, 2008, 36 :653-657
[5]   Pi release from elF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation [J].
Algire, MA ;
Maag, D ;
Lorsch, JR .
MOLECULAR CELL, 2005, 20 (02) :251-262
[6]   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
[7]   In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3 [J].
Alkalaeva, Elena Z. ;
Pisarev, Andrey V. ;
Frolova, Lyudmila Y. ;
Kisselev, Lev L. ;
Pestova, Tatyana V. .
CELL, 2006, 125 (06) :1125-1136
[8]   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
[9]   A SACCHAROMYCES-CEREVISIAE HOMOLOG OF MAMMALIAN TRANSLATION INITIATION FACTOR-4B CONTRIBUTES TO RNA HELICASE ACTIVITY [J].
ALTMANN, M ;
MULLER, PP ;
WITTMER, B ;
RUCHTI, F ;
LANKER, S ;
TRACHSEL, H .
EMBO JOURNAL, 1993, 12 (10) :3997-4003
[10]   Translation factors promote the formation of two states of the closed-loop mRNP [J].
Amrani, Nadia ;
Ghosh, Shubhendu ;
Mangus, David A. ;
Jacobson, Allan .
NATURE, 2008, 453 (7199) :1276-U85