Engaging the ribosome: universal IFs of translation

被引:61
作者
Roll-Mecak, A
Shin, BS
Dever, TE
Burley, SK
机构
[1] Rockefeller Univ, Howard Hughes Med Inst, Lab Mol Biophys, New York, NY 10021 USA
[2] NICHHD, Lab Gene Regulat & Dev, NIH, Bethesda, MD 20892 USA
关键词
D O I
10.1016/S0968-0004(01)02024-2
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
Eukaryotic initiation factor 1A (eIF1A) and the GTPase IF2/eIF5B are the only universally conserved translation initiation factors. Recent structural, biochemical and genetic data indicate that these two factors form an evolutionarily conserved structural and functional unit in translation initiation. Based on insights gathered from studies of the translation elongation factor GTPases, we propose that these factors occupy the aminoacyl-tRNA site (A site) on the ribosome, and promote initiator tRNA binding and ribosomal subunit joining. These processes yield a translationally competent ribosome with Met-tRNA in the ribosomal peptidyl-tRNA site (P site), base-paired to the AUG start codon of a mRNA.
引用
收藏
页码:705 / 709
页数:5
相关论文
共 32 条
[1]   3-DIMENSIONAL STRUCTURE OF THE RIBOSOMAL TRANSLOCASE - ELONGATION-FACTOR-G FROM THERMUS-THERMOPHILUS [J].
AEVARSSON, A ;
BRAZHNIKOV, E ;
GARBER, M ;
ZHELTONOSOVA, J ;
CHIRGADZE, Y ;
AL-KARADAGHI, S ;
SVENSSON, LA ;
LILJAS, A .
EMBO JOURNAL, 1994, 13 (16) :3669-3677
[2]   EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome [J].
Agrawal, RK ;
Heagle, AB ;
Penczek, P ;
Grassucci, RA ;
Frank, J .
NATURE STRUCTURAL BIOLOGY, 1999, 6 (07) :643-647
[3]   The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution [J].
Ban, N ;
Nissen, P ;
Hansen, J ;
Moore, PB ;
Steitz, TA .
SCIENCE, 2000, 289 (5481) :905-920
[4]   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
[5]   CRYSTAL-STRUCTURE OF ACTIVE ELONGATION-FACTOR TU REVEALS MAJOR DOMAIN REARRANGEMENTS [J].
BERCHTOLD, H ;
RESHETNIKOVA, L ;
REISER, COA ;
SCHIRMER, NK ;
SPRINZL, M ;
HILGENFELD, R .
NATURE, 1993, 365 (6442) :126-132
[6]   DIRECT CROSS-LINKS BETWEEN INITIATION FACTOR-I, FACTOR-II, AND FACTOR-III AND RIBOSOMAL-PROTEINS PROMOTED BY 2-IMINOTHIOLANE [J].
BOILEAU, G ;
BUTLER, P ;
HERSHEY, JWB ;
TRAUT, RR .
BIOCHEMISTRY, 1983, 22 (13) :3162-3170
[7]   Crystal structure of an initiation factor bound to the 30S ribosomal subunit [J].
Carter, AP ;
Clemons, WM ;
Brodersen, DE ;
Morgan-Warren, RJ ;
Hartsch, T ;
Wimberly, BT ;
Ramakrishnan, V .
SCIENCE, 2001, 291 (5503) :498-501
[8]   Promotion of Met-tRNAiMet binding to ribosomes by yIF2, a bacterial IF2 homolog in yeast [J].
Choi, SK ;
Lee, JH ;
Zoll, WL ;
Merrick, WC ;
Dever, TE .
SCIENCE, 1998, 280 (5370) :1757-1760
[9]   Physical and functional interaction between the eukaryotic orthologs of prokaryotic translation initiation factors IF1 and IF2 [J].
Choi, SK ;
Olsen, DS ;
Roll-Mecak, A ;
Martung, A ;
Remo, KL ;
Burley, SK ;
Hinnebusch, AG ;
Dever, TE .
MOLECULAR AND CELLULAR BIOLOGY, 2000, 20 (19) :7183-7191
[10]   THE CRYSTAL-STRUCTURE OF ELONGATION-FACTOR-G COMPLEXED WITH GDP, AT 2.7-ANGSTROM RESOLUTION [J].
CZWORKOWSKI, J ;
WANG, J ;
STEITZ, TA ;
MOORE, PB .
EMBO JOURNAL, 1994, 13 (16) :3661-3668