eEF1B: At the dawn of the 21st century

被引:82
作者
Le Sourd, Frederic [1 ]
Boulben, Sandrine [1 ]
Le Bouffant, Ronan [1 ]
Cormier, Patrick [1 ]
Morales, Julia [1 ]
Belle, Robert [1 ]
Mulner-Lorillon, Odile [1 ]
机构
[1] UPMC, CNRS, Stn Biol Roscoff, Equipe Cycle & Dev,Unite Mer & Sante,UMR 7150, F-29682 Roscoff, France
来源
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION | 2006年 / 1759卷 / 1-2期
关键词
elongation factor; gene expression; regulation; protein translation; cancer; virus;
D O I
10.1016/j.bbaexp.2006.02.003
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
Translational regulation of gene expression in eukaryotes can rapidly and accurately control cell activity in response to stimuli or when rapidly dividing. There is increasing evidence for a key role of the elongation step in this process. Elongation factor-1 (eEF1), which is responsible for aminoacyl-tRNA transfer on the ribosome, is comprised of two entities: a G-protein named eEF1A and a nucleotide exchange factor, eEF1B. The multifunctional nature of eEF1A, as well as its oncogenic potential, is currently the subject of a number of studies. Until recently, less work has been done on eEF1B. This review describes the macromolecular complexity of eEF1B, its multiple phosphorylation sites and numerous cellular partners, which lead us to suggest an essential role for the factor in the control of gene expression, particularly during the cell cycle. (c) 2006 Elsevier B.V. All rights reserved.
引用
收藏
页码:13 / 31
页数:19
相关论文
共 161 条
[1]   GENE-REGULATION - ACTION OF LEUCINE ZIPPERS [J].
ABEL, T ;
MANIATIS, T .
NATURE, 1989, 341 (6237) :24-25
[2]   The 3′untranslated region of human vimentin mRNA interacts with protein complexes containing eEF-1γ and HAX-1 [J].
Al-Maghrebi, M ;
Brulé, H ;
Padkina, M ;
Allen, C ;
Holmes, WM ;
Zehner, ZE .
NUCLEIC ACIDS RESEARCH, 2002, 30 (23) :5017-5028
[3]   Structure of the leucine zipper [J].
Alber, Tom .
CURRENT OPINION IN GENETICS & DEVELOPMENT, 1992, 2 (02) :205-210
[4]   Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].
Altschul, SF ;
Madden, TL ;
Schaffer, AA ;
Zhang, JH ;
Zhang, Z ;
Miller, W ;
Lipman, DJ .
NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402
[5]   THE LEUCINE-ZIPPER IN ELONGATION-FACTOR EF-1-DELTA, A GUANINE-NUCLEOTIDE EXCHANGE PROTEIN, IS CONSERVED IN ARTEMIA AND XENOPUS [J].
AMONS, R ;
GUERRUCCI, MA ;
KARSSIES, RH ;
MORALES, J ;
CORMIER, P ;
MOLLER, W ;
BELLE, R .
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION, 1994, 1218 (03) :346-350
[6]   SEQUENCE HOMOLOGY BETWEEN EF-1-ALPHA, THE ALPHA-CHAIN OF ELONGATION FACTOR-I FROM ARTEMIA-SALINA AND ELONGATION-FACTOR EF-TU FROM ESCHERICHIA-COLI [J].
AMONS, R ;
PLUIJMS, W ;
ROOBOL, K ;
MOLLER, W .
FEBS LETTERS, 1983, 153 (01) :37-42
[7]   Elongation factors in protein biosynthesis [J].
Andersen, GR ;
Nissen, P ;
Nyborg, J .
TRENDS IN BIOCHEMICAL SCIENCES, 2003, 28 (08) :434-441
[8]  
BEC G, 1994, J BIOL CHEM, V269, P2086
[9]  
Belle R, 1995, Prog Cell Cycle Res, V1, P265
[10]   A PURIFIED COMPLEX FROM XENOPUS OOCYTES CONTAINS A P47-PROTEIN, AN INVIVO SUBSTRATE OF MPF, AND A P30-PROTEIN RESPECTIVELY HOMOLOGOUS TO ELONGATION-FACTORS EF-1-GAMMA AND EF-1-BETA [J].
BELLE, R ;
DERANCOURT, J ;
POULHE, R ;
CAPONY, JP ;
OZON, R ;
MULNERLORILLON, O .
FEBS LETTERS, 1989, 255 (01) :101-104