Starting the protein synthesis machine: eukaryotic translation initiation

被引:146
作者
Preiss, T
Hentze, MW
机构
[1] European Mol Biol Lab, Gene Express Programme, D-69117 Heidelberg, Germany
[2] VCCRI, Mol Genet Program, Sydney, NSW, Australia
关键词
D O I
10.1002/bies.10362
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
The final assembly of the protein synthesis machinery occurs during translation initiation. This delicate process involves both ends of eukaryotic messenger RNAs as well as multiple sequential protein-RNA and protein-protein interactions. As is expected from its critical position in the gene expression pathway between the transcriptome and the proteome, translation initiation is a selective and highly regulated process. This synopsis summarises the current status of the field and identifies intriguing open questions. (C) 2003 Wiley Periodicals, Inc.
引用
收藏
页码:1201 / 1211
页数:11
相关论文
共 99 条
[1]   Eukaryote-specific domains in translation initiation factors: Implications for translation regulation and evolution of the translation system [J].
Aravind, L ;
Koonin, EV .
GENOME RESEARCH, 2000, 10 (08) :1172-1184
[2]   A multifactor complex of eukaryotic initiation factors, eIE1, eIF2, eIF3, eIF5, and initiator tRNAMet is an important translation initiation intermediate in vivo [J].
Asano, K ;
Clayton, J ;
Shalev, A ;
Hinnebusch, AG .
GENES & DEVELOPMENT, 2000, 14 (19) :2534-2546
[3]   Conserved bipartite motifs in yeast eIF5 and eIF2Bε, GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2 [J].
Asano, K ;
Krishnamoorthy, T ;
Phan, L ;
Pavitt, GD ;
Hinnebusch, AG .
EMBO JOURNAL, 1999, 18 (06) :1673-1688
[4]   Multiple roles for the C-terminal domain of eIF5 in translation initiation complex assembly and GTPase activation [J].
Asano, K ;
Shalev, A ;
Phan, L ;
Nielsen, K ;
Clayton, J ;
Valásek, L ;
Donahue, TF ;
Hinnebusch, AG .
EMBO JOURNAL, 2001, 20 (09) :2326-2337
[5]   The eIF1A solution structure reveals a large RNA-binding surface important for scanning function [J].
Battiste, JL ;
Pestova, TV ;
Hellen, CUT ;
Wagner, G .
MOLECULAR CELL, 2000, 5 (01) :109-119
[6]   Picornavirus IRESes and the poly(A) tail jointly promote cap-independent translation in a mammalian cell-free system [J].
Bergamini, G ;
Preiss, T ;
Hentze, MW .
RNA, 2000, 6 (12) :1781-1790
[7]   Biochemical characterisation of cap-poly(A) synergy in rabbit reticulocyte lysates:: the eIF4G-PABP interaction increases the functional affinity of eIF4E for the capped mRNA 5′-end [J].
Borman, AM ;
Michel, YM ;
Kean, KM .
NUCLEIC ACIDS RESEARCH, 2000, 28 (21) :4068-4075
[8]   Free poly(A) stimulates capped mRNA translation in vitro through the eIF4G-poly(A)-binding protein interaction [J].
Borman, AM ;
Michel, YM ;
Malnou, CE ;
Kean, KM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (39) :36818-36824
[9]  
BRAKIERGINGRAS L, 2003, TRANSLATION MECH MOL
[10]   Unified nomenclature for the subunits of eukaryotic initiation factor 3 [J].
Browning, KS ;
Gallie, DR ;
Hershey, JWB ;
Hinnebusch, AG ;
Maitra, U ;
Merrick, WC ;
Norbury, C .
TRENDS IN BIOCHEMICAL SCIENCES, 2001, 26 (05) :284-284