Structural studies of elongation and release factors

被引:38
作者
Noble, C. G. [1 ]
Song, H. [1 ]
机构
[1] ASTAR, Inst Mol & Cell Biol, Lab Macromol Struct, Singapore 138673, Singapore
关键词
elongation factor; release factor; termination factor; ribosome structure; GTPase; protein synthesis;
D O I
10.1007/s00018-008-7495-6
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 elongation and termination steps of protein synthesis are controlled by elongation and release factors, respectively. Elongation factors deliver the aminoacyl tRNA to the ribosomal A site, ensuring the elongation of the nascent polypeptide chain by one amino acid at a time, while release factors recognize the stop codons and trigger the release of the polypeptide from the ribosome. Recently, high-resolution crystal structures of ribosomes as well as translation factors on and off the ribosome have contributed a great deal to our understanding of the molecular basis of protein synthesis. This review concentrates on recent developments in our understanding of the elongation and termination steps of protein synthesis, particularly the roles of translation factors and their similarities and differences in the eukaryotic cytosol and prokaryotic systems, through a combination of structural and biochemical studies.
引用
收藏
页码:1335 / 1346
页数:12
相关论文
共 102 条
[1]   An alpha to beta conformational switch in EF-Tu [J].
Abel, K ;
Yoder, MD ;
Hilgenfeld, R ;
Jurnak, F .
STRUCTURE, 1996, 4 (10) :1153-1159
[2]   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
[3]   Visualization of elongation factor G on the Escherichia coli 70S ribosome:: The mechanism of translocation [J].
Agrawal, RK ;
Penczek, P ;
Grassucci, RA ;
Frank, J .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (11) :6134-6138
[4]   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
[5]   The structure of elongation factor G in complex with GDP: Conformational flexibility and nucleotide exchange [J].
Al-Karadaghi, S ;
AEvarsson, A ;
Garber, M ;
Zheltonosova, J ;
Liljas, A .
STRUCTURE, 1996, 4 (05) :555-565
[6]   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
[7]   Structure of eEF3 and the mechanism of transfer RNA release from the E-site [J].
Andersen, Christian B. F. ;
Becker, Thomas ;
Blau, Michael ;
Anand, Monika ;
Halic, Mario ;
Balar, Bharvi ;
Mielke, Thorsten ;
Boesen, Thomas ;
Pedersen, Jan Skov ;
Spahn, Christian M. T. ;
Kinzy, Terri Goss ;
Andersen, Gregers R. ;
Beckmann, Roland .
NATURE, 2006, 443 (7112) :663-668
[8]   Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Bα [J].
Andersen, GR ;
Pedersen, L ;
Valente, L ;
Chatterjee, I ;
Kinzy, TG ;
Kjeldgaard, M ;
Nyborg, J .
MOLECULAR CELL, 2000, 6 (05) :1261-1266
[9]   Elongation factors in protein biosynthesis [J].
Andersen, GR ;
Nissen, P ;
Nyborg, J .
TRENDS IN BIOCHEMICAL SCIENCES, 2003, 28 (08) :434-441
[10]   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