The mechanism of eukaryotic translation initiation and principles of its regulation

被引:1943
作者
Jackson, Richard J. [1 ]
Hellen, Christopher U. T. [2 ]
Pestova, Tatyana V. [2 ]
机构
[1] Univ Cambridge, Dept Biochem, Cambridge CB2 1GA, England
[2] Suny Downstate Med Ctr, Dept Cell Biol, Brooklyn, NY 11203 USA
基金
美国国家卫生研究院; 英国生物技术与生命科学研究理事会; 英国惠康基金;
关键词
MESSENGER-RNA TRANSLATION; 40S RIBOSOMAL-SUBUNIT; POLY(A)-BINDING PROTEIN; IN-VITRO; FUNCTIONAL INTERACTION; DEPENDENT TRANSLATION; BINDING-PROTEIN; 80S RIBOSOME; FACTORS; 1A; COMPLEX;
D O I
10.1038/nrm2838
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Protein synthesis is principally regulated at the initiation stage (rather than during elongation or termination), allowing rapid, reversible and spatial control of gene expression. Progress over recent years in determining the structures and activities of initiation factors, and in mapping their interactions in ribosomal initiation complexes, have advanced our understanding of the complex translation initiation process. These developments have provided a solid foundation for studying the regulation of translation initiation by mechanisms that include the modulation of initiation factor activity (which affects almost all scanning-dependent initiation) and through sequence-specific RNA-binding proteins and microRNAs (which affect individual mRNAs).
引用
收藏
页码:113 / 127
页数:15
相关论文
共 121 条
[1]   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
[2]   Kinetic Analysis of Late Steps of Eukaryotic Translation Initiation [J].
Acker, Michael G. ;
Shin, Byung-Sik ;
Nanda, Jagpreet S. ;
Saini, Adesh K. ;
Dever, Thomas E. ;
Lorsch, Jon R. .
JOURNAL OF MOLECULAR BIOLOGY, 2009, 385 (02) :491-506
[3]   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
[4]   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
[5]   Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA [J].
Andersen, Christian B. F. ;
Ballut, Lionel ;
Johansen, Jesper S. ;
Chamieh, Hala ;
Nielsen, Klaus H. ;
Oliveira, Cristiano L. P. ;
Pedersen, Jan Skov ;
Seraphin, Bertrand ;
Le Hir, Herve ;
Andersen, Gregers Rom .
SCIENCE, 2006, 313 (5795) :1968-1972
[6]   Splicing mediates the activity of four putative cellular internal ribosome entry sites [J].
Baranick, Brian T. ;
Lemp, Nathan A. ;
Nagashima, Jill ;
Hiraoka, Kei ;
Kasahara, Noriyuki ;
Logg, Christopher R. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2008, 105 (12) :4733-4738
[7]   MRNA degradation by miRNAs and GW182 requires both CCR4:NOT deadenylase and DCP1:DCP2 decapping complexes [J].
Behm-Ansmant, Isabelle ;
Rehwinkel, Jan ;
Doerks, Tobias ;
Stark, Alexander ;
Bork, Peer ;
Izaurralde, Elisa .
GENES & DEVELOPMENT, 2006, 20 (14) :1885-1898
[8]   Relief of microRNA-mediated translational repression in human cells subjected to stress [J].
Bhattacharyya, Suvendra N. ;
Habermacher, Regula ;
Martine, Ursula ;
Closs, Ellen I. ;
Filipowicz, Witold .
CELL, 2006, 125 (06) :1111-1124
[9]   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
[10]   PROTAMINE 3'-UNTRANSLATED SEQUENCES REGULATE TEMPORAL TRANSLATIONAL CONTROL AND SUBCELLULAR-LOCALIZATION OF GROWTH-HORMONE IN SPERMATIDS OF TRANSGENIC MICE [J].
BRAUN, RE ;
PESCHON, JJ ;
BEHRINGER, RR ;
BRINSTER, RL ;
PALMITER, RD .
GENES & DEVELOPMENT, 1989, 3 (06) :793-802