Mechanism of recycling of post-termination ribosomal complexes in eubacteria: a new role of initiation factor 3

被引:13
作者
Seshadri, Anuradha [1 ]
Varshney, Umesh [1 ]
机构
[1] Indian Inst Sci, Dept Microbiol & Cell Biol, Bangalore 560012, Karnataka, India
关键词
EFG; IF3; post-TC; protein synthesis; RF; specific interactions;
D O I
10.1007/BF02703921
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
Ribosome recycling is a process which dissociates the post-termination complexes (post-TC) consisting of mRNA-bound ribosomes harbouring deacylated tRNA(s). Ribosome recycling factor (RRF), and elongation factor G (EFG) participate in this crucial process to free the ribosomal subunits for a new round of translation. We discuss the overall pathway of ribosome recycling in eubacteria with especial reference to the important role of the initiation factor 3 (IF3) in this process. Depending on the step(s) at which IF3 function is implicated, three models have been proposed. In model 1, RRF and EFG dissociate the post-TCs into the 50S and 30S subunits, mRNA and tRNA(s). In this model, IF3, which binds to the 30S subunit, merely keeps the dissociated subunits apart by its anti-association activity. In model 2, RRF and EFG separate the 50S subunit from the post-TC. IF3 then dissociates the remaining complex of mRNA, tRNA and the 30S subunit, and keeps the ribosomal subunits apart from each other. However, in model 3, both the genetic and biochemical evidence support a more active role for IF3 even at the step of dissociation of the post-TC by RRF and EFG into the 50S and 30S subunits.
引用
收藏
页码:281 / 289
页数:9
相关论文
共 55 条
[1]   Visualization of ribosome-recycling factor on the Escherichia coli 70S ribosome:: Functional implications [J].
Agrawal, RK ;
Sharma, MR ;
Kiel, MC ;
Hirokawa, G ;
Booth, TM ;
Spahn, CMT ;
Grassucci, RA ;
Kaji, A ;
Frank, J .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (24) :8900-8905
[2]   Polypeptide chain release factors [J].
Buckingham, RH ;
Grentzmann, G ;
Kisselev, L .
MOLECULAR MICROBIOLOGY, 1997, 24 (03) :449-456
[3]   X-ray crystal structures of 70S ribosome functional complexes [J].
Cate, JH ;
Yusupov, MM ;
Yusupova, GZ ;
Earnest, TN ;
Noller, HF .
SCIENCE, 1999, 285 (5436) :2095-2104
[4]   Interaction of translation initiation factor 3 with the 30S ribosomal subunit [J].
Dallas, A ;
Noller, HF .
MOLECULAR CELL, 2001, 8 (04) :855-864
[5]   THE MINIMAL GENE COMPLEMENT OF MYCOPLASMA-GENITALIUM [J].
FRASER, CM ;
GOCAYNE, JD ;
WHITE, O ;
ADAMS, MD ;
CLAYTON, RA ;
FLEISCHMANN, RD ;
BULT, CJ ;
KERLAVAGE, AR ;
SUTTON, G ;
KELLEY, JM ;
FRITCHMAN, JL ;
WEIDMAN, JF ;
SMALL, KV ;
SANDUSKY, M ;
FUHRMANN, J ;
NGUYEN, D ;
UTTERBACK, TR ;
SAUDEK, DM ;
PHILLIPS, CA ;
MERRICK, JM ;
TOMB, JF ;
DOUGHERTY, BA ;
BOTT, KF ;
HU, PC ;
LUCIER, TS ;
PETERSON, SN ;
SMITH, HO ;
HUTCHISON, CA ;
VENTER, JC .
SCIENCE, 1995, 270 (5235) :397-403
[6]   Release factor RF3 in E-coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner [J].
Freistroffer, DV ;
Pavlov, MY ;
MacDougall, J ;
Buckingham, RH ;
Ehrenberg, M .
EMBO JOURNAL, 1997, 16 (13) :4126-4133
[7]   Ribosome recycling factor disassembles the post-termination ribosomal complex independent of the ribosomal translocase activity of elongation factor G [J].
Fujiwara, T ;
Ito, K ;
Yamami, T ;
Nakamura, Y .
MOLECULAR MICROBIOLOGY, 2004, 53 (02) :517-528
[8]   Solution structure of the E. coli 70S ribosome at 11.5 Å resolution [J].
Gabashvili, IS ;
Agrawal, RK ;
Spahn, CMT ;
Grassucci, RA ;
Svergun, DI ;
Frank, J ;
Penczek, P .
CELL, 2000, 100 (05) :537-549
[9]   Study of the structural dynamics of the E-coli 70S ribosome using real-space refinement [J].
Gao, HX ;
Sengupta, J ;
Valle, M ;
Korostelev, A ;
Eswar, N ;
Stagg, SM ;
Van Roey, P ;
Agrawal, RK ;
Harvey, SC ;
Sali, A ;
Chapman, MS ;
Frank, J .
CELL, 2003, 113 (06) :789-801
[10]   Mechanism for the disassembly of the posttermination complex inferred from cryo-EM studies [J].
Gao, N ;
Zavialov, AV ;
Li, W ;
Sengupta, J ;
Valle, M ;
Gursky, RP ;
Ehrenberg, M ;
Frank, J .
MOLECULAR CELL, 2005, 18 (06) :663-674