Beyond ribosome rescue: tmRNA and co-translational processes

被引:63
作者
Hayes, Christopher S. [2 ]
Keiler, Kenneth C. [1 ]
机构
[1] Penn State Univ, Dept Biochem & Mol Biol, University Pk, PA 16802 USA
[2] Univ Calif Santa Barbara, Dept Mol Cellular & Dev Biol, Santa Barbara, CA 93106 USA
基金
美国国家卫生研究院;
关键词
Ribosome pausing; SmpB; tmRNA; Translation; trans-Translation; MESSENGER-RNA CLEAVAGE; ELONGATION-FACTOR TU; PEPTIDE-TAGGING ACTIVITY; ESCHERICHIA-COLI; TRANS-TRANSLATION; BACILLUS-SUBTILIS; STOP CODONS; A-SITE; 10SA RNA; QUALITY-CONTROL;
D O I
10.1016/j.febslet.2009.11.023
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
tmRNA is a unique bi-functional RNA that acts as both a tRNA and an mRNA to enter stalled ribosomes and direct the addition of a peptide tag to the C terminus of nascent polypeptides. Despite a reasonably clear understanding of tmRNA activity, the reason for its absolute conservation throughout the eubacteria is unknown. Although tmRNA plays many physiological roles in different bacterial systems, recent studies suggest a general role for trans-translation in monitoring protein folding and perhaps other co-translational processes. This review will focus on these new hypotheses and the data that support them. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
引用
收藏
页码:413 / 419
页数:7
相关论文
共 65 条
[1]   SsrA-mediated tagging and proteolysis of Lacl and its role in the regulation of lac operon [J].
Abo, T ;
Inada, T ;
Ogawa, A ;
Aiba, H .
EMBO JOURNAL, 2000, 19 (14) :3762-3769
[2]   Kinetic parameters for tmRNA binding to alanyl-tRNA synthetase and elongation factor Tu from Escherichia coli [J].
Barends, S ;
Wower, J ;
Kraal, B .
BIOCHEMISTRY, 2000, 39 (10) :2652-2658
[3]   Planarian mitochondria sequence heterogeneity: Relationships between the type of cytochrome c oxidase subunit I gene sequence, karyotype and genital organ [J].
Bessho, Y ;
Tamura, S ;
Hori, H ;
Tanaka, H ;
Ohama, T ;
Osawa, S .
MOLECULAR ECOLOGY, 1997, 6 (02) :129-136
[4]   Subcellular sites for bacterial protein export [J].
Campo, N ;
Tjalsma, H ;
Buist, G ;
Stepniak, D ;
Meijer, M ;
Veenhuis, M ;
Westermann, M ;
Müller, JP ;
Bron, S ;
Kok, J ;
Kuipers, OP ;
Jongbloed, JDH .
MOLECULAR MICROBIOLOGY, 2004, 53 (06) :1583-1599
[5]   Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA [J].
Christensen, SK ;
Pedersen, K ;
Hansen, FG ;
Gerdes, K .
JOURNAL OF MOLECULAR BIOLOGY, 2003, 332 (04) :809-819
[6]   RelE toxins from Bacteria and Archaea cleave mRNAs on translating ribosomes, which are rescued by tmRNA [J].
Christensen, SK ;
Gerdes, K .
MOLECULAR MICROBIOLOGY, 2003, 48 (05) :1389-1400
[7]   Competition between SsrA tagging and translational termination at weak stop codons in Escherichia coli [J].
Collier, J ;
Binet, E ;
Bouloc, P .
MOLECULAR MICROBIOLOGY, 2002, 45 (03) :745-754
[8]   Features of ribosome-peptidyl-tRNA interactions essential for tryptophan induction of tna operon expression [J].
Cruz-Vera, LR ;
Rajagopal, S ;
Squires, C ;
Yanofsky, C .
MOLECULAR CELL, 2005, 19 (03) :333-343
[9]   Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli [J].
Danese, PN ;
Silhavy, TJ .
ANNUAL REVIEW OF GENETICS, 1998, 32 :59-94
[10]   The tmRNA website: reductive evolution of tmRNA in plastids and other endosymbionts [J].
de Novoa, PG ;
Williams, KP .
NUCLEIC ACIDS RESEARCH, 2004, 32 :D104-D108