Translation termination in pyrrolysine-utilizing archaea

被引:21
作者
Alkalaeva, Elena [1 ]
Eliseev, Boris [1 ]
Ambrogelly, Alexandre [3 ]
Vlasov, Peter [1 ]
Kondrashov, Fyodor A. [2 ]
Gundllapalli, Sharath [3 ]
Frolova, Lyudmila [1 ]
Soll, Dieter [3 ,4 ]
Kisselev, Lev [1 ]
机构
[1] Russian Acad Sci, Engelhardt Inst Mol Biol, Moscow 119991, Russia
[2] Ctr Genom Regulat, Bioinformat & Genom Programme, Barcelona 08003, Spain
[3] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA
[4] Yale Univ, Dept Chem, New Haven, CT 06520 USA
基金
俄罗斯基础研究基金会; 美国国家科学基金会;
关键词
Translation termination; Archeon; Pyrrolysine-utilizing archea; aRF1; Polypeptide release factor; TRANSFER-RNA SYNTHETASE; RELEASE FACTOR ERF1; STOP CODON; IN-VITRO; AMINO-ACIDS; SELENOCYSTEINE; RECOGNITION; UAG; DOMAIN; MODES;
D O I
10.1016/j.febslet.2009.09.044
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
Although some data link archaeal and eukaryotic translation, the overall mechanism of protein synthesis in archaea remains largely obscure. Both archaeal (aRF1) and eukaryotic (eRF1) single release factors recognize all three stop codons. The archaeal genus Methanosarcinaceae contains two aRF1 homologs, and also uses the UAG stop to encode the 22nd amino acid, pyrrolysine. Here we provide an analysis of the last stage of archaeal translation in pyrrolysine-utilizing species. We demonstrated that only one of two Methanosarcina barkeri aRF1 homologs possesses activity and recognizes all three stop codons. The second aRF1 homolog may have another unknown function. The mechanism of pyrrolysine incorporation in the Methanosarcinaceae is discussed. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
引用
收藏
页码:3455 / 3460
页数:6
相关论文
共 40 条
[1]   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
[2]   Selenoprotein synthesis: UGA does not end the story [J].
Allmang, C. ;
Krol, A. .
BIOCHIMIE, 2006, 88 (11) :1561-1571
[3]   Functional annotation of class I lysyl-tRNA synthetase phylogeny indicates a limited role for gene transfer [J].
Ambrogelly, A ;
Korencic, D ;
Ibba, M .
JOURNAL OF BACTERIOLOGY, 2002, 184 (16) :4594-4600
[4]   Terminating eukaryote translation: Domain 1 of release factor eRF1 functions in stop codon recognition [J].
Bertram, G ;
Bell, HA ;
Ritchie, DW ;
Fullerton, G ;
Stansfield, I .
RNA, 2000, 6 (09) :1236-1247
[5]   Direct charging of tRNACUA with pyrrolysine in vitro and in vivo [J].
Blight, SK ;
Larue, RC ;
Mahapatra, A ;
Longstaff, DG ;
Chang, E ;
Zhao, G ;
Kang, PT ;
Church-Church, KB ;
Chan, MK ;
Krzycki, JA .
NATURE, 2004, 431 (7006) :333-335
[6]  
Bock M.T. August., 2005, The aminoacyl-tRNA synthetases, P320
[7]   Stop codon selection in eukaryotic translation termination: comparison of the discriminating potential between human and ciliate eRF1s [J].
Chavatte, L ;
Kervestin, S ;
Favre, A ;
Jean-Jean, O .
EMBO JOURNAL, 2003, 22 (07) :1644-1653
[8]  
Deppenmeier U, 2002, J MOL MICROB BIOTECH, V4, P453
[9]   Translation termination factor aRF1 from the archaeon Methanococcus jannaschii is active with eukaryotic ribosomes [J].
Dontsova, M ;
Frolova, L ;
Vassilieva, J ;
Piendl, W ;
Kisselev, L ;
Garber, M .
FEBS LETTERS, 2000, 472 (2-3) :213-216
[10]   MUSCLE: multiple sequence alignment with high accuracy and high throughput [J].
Edgar, RC .
NUCLEIC ACIDS RESEARCH, 2004, 32 (05) :1792-1797