Quality control mechanisms during translation

被引:180
作者
Ibba, M
Söll, D
机构
[1] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA
[2] Yale Univ, Dept Chem, New Haven, CT 06520 USA
[3] Yale Univ, Dept Mol Cellular & Dev Biol, New Haven, CT 06520 USA
[4] Univ Copenhagen, Panum Inst, Ctr Biomol Recognit, Dept Med Biochem & Genet,Lab B, DK-2200 Copenhagen, Denmark
关键词
D O I
10.1126/science.286.5446.1893
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Translation uses the genetic information in messenger RNA (mRNA) to synthesize proteins. Transfer RNAs (tRNAs) are charged with an amino acid and brought to the ribosome, where they are paired with the corresponding trinucleotide codon in mRNA. The amino acid is attached to the nascent polypeptide and the ribosome moves on to the next codon. The cycle is then repeated to produce a full-length protein. Proofreading and editing processes are used throughout protein synthesis to ensure the faithful translation of genetic information. The maturation of tRNAs and mRNAs is monitored, as is the identity of amino acids attached to tRNAs. Accuracy is further enhanced during the selection of aminoacyl-tRNAs on the ribosome and their base pairing with mRNA. Recent studies have begun to reveal the molecular mechanisms underpinning quality control and go some way to explaining the phenomenal accuracy of translation first observed over three decades ago.
引用
收藏
页码:1893 / 1897
页数:5
相关论文
共 89 条
[31]   An adenosine deaminase that generates inosine at the wobble position of tRNAs [J].
Gerber, AP ;
Keller, W .
SCIENCE, 1999, 286 (5442) :1146-1149
[32]   Universal rules and idiosyncratic features in tRNA identity [J].
Giegé, R ;
Sissler, M ;
Florentz, C .
NUCLEIC ACIDS RESEARCH, 1998, 26 (22) :5017-5035
[33]   The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system [J].
Gottesman, S ;
Roche, E ;
Zhou, YN ;
Sauer, RT .
GENES & DEVELOPMENT, 1998, 12 (09) :1338-1347
[34]   Discrete determinants in transfer RNA for editing and aminoacylation [J].
Hale, SP ;
Auld, DS ;
Schmidt, E ;
Schimmel, P .
SCIENCE, 1997, 276 (5316) :1250-1252
[35]   A perfect message: RNA surveillance and nonsense-mediated decay [J].
Hentze, MW ;
Kulozik, AE .
CELL, 1999, 96 (03) :307-310
[36]   Ribosome release factor RF4 and termination factor RF3 are involved in dissociation of peptidyl-tRNA from the ribosome [J].
Heurgué-Hamard, V ;
Karimi, R ;
Mora, L ;
MacDougall, J ;
Leboeuf, C ;
Grentzmann, G ;
Ehrenberg, M ;
Buckingham, RH .
EMBO JOURNAL, 1998, 17 (03) :808-816
[37]   mRNA surveillance in eukaryotes: Kinetic proofreading of proper translation termination as assessed by mRNP domain organization? [J].
Hilleren, P ;
Parker, R .
RNA, 1999, 5 (06) :711-719
[38]   ADAPTABILITY OF NONNATURAL AROMATIC-AMINO-ACIDS TO THE ACTIVE-CENTER OF THE ESCHERICHIA-COLI RIBOSOMAL A-SITE [J].
HOHSAKA, T ;
SATO, K ;
SISIDO, M ;
TAKAI, K ;
YOKOYAMA, S .
FEBS LETTERS, 1993, 335 (01) :47-50
[39]   Aminoacyl-tRNA synthesis: Divergent routes to a common goal [J].
Ibba, M ;
Curnow, AW ;
Soll, D .
TRENDS IN BIOCHEMICAL SCIENCES, 1997, 22 (02) :39-42
[40]   Misacylation of tRNALys with noncognate amino acids by Lysyl-tRNA synthetase [J].
Jakubowski, H .
BIOCHEMISTRY, 1999, 38 (25) :8088-8093