Literature DB >> 10978500

Release factors and their role as decoding proteins: specificity and fidelity for termination of protein synthesis.

E Poole1, W Tate.   

Abstract

The decoding of stop signals in mRNA requires protein release factors. Two classes of factor are found in both prokaryotes and eukaryotes, a decoding factor and a stimulatory recycling factor. These factors form complexes at the active centre of the ribosome and mimic in overall shape the complexes found at other stages of protein synthesis. The decoding release factor is shaped like a tRNA and has a domain for codon recognition at the decoding site of the ribosome, and a domain for peptidyl-tRNA hydrolysis that is inferred to be near the peptidyltransferase centre. Initial interaction of the decoding factor with the ribosome is a low fidelity event involving multiple contacts with the ribosomal components. A subsequent discrimination step, at present poorly defined, ensures high fidelity of codon recognition.

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Year:  2000        PMID: 10978500     DOI: 10.1016/s0167-4781(00)00162-7

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  17 in total

1.  Conversion of omnipotent translation termination factor eRF1 into ciliate-like UGA-only unipotent eRF1.

Authors:  Alim Seit-Nebi; Ludmila Frolova; Lev Kisselev
Journal:  EMBO Rep       Date:  2002-08-16       Impact factor: 8.807

2.  Mutational eidence for a functional connection between two domains of 23S rRNA in translation termination.

Authors:  Alexey L Arkov; Klas O F Hedenstierna; Emanuel J Murgola
Journal:  J Bacteriol       Date:  2002-09       Impact factor: 3.490

3.  Divergent tRNA-like element supports initiation, elongation, and termination of protein biosynthesis.

Authors:  Eric Jan; Terri Goss Kinzy; Peter Sarnow
Journal:  Proc Natl Acad Sci U S A       Date:  2003-12-12       Impact factor: 11.205

Review 4.  Termination of translation: interplay of mRNA, rRNAs and release factors?

Authors:  Lev Kisselev; Måns Ehrenberg; Ludmila Frolova
Journal:  EMBO J       Date:  2003-01-15       Impact factor: 11.598

5.  Three distinct peptides from the N domain of translation termination factor eRF1 surround stop codon in the ribosome.

Authors:  Konstantin N Bulygin; Yulia S Khairulina; Petr M Kolosov; Aliya G Ven'yaminova; Dmitri M Graifer; Yuri N Vorobjev; Ludmila Yu Frolova; Lev L Kisselev; Galina G Karpova
Journal:  RNA       Date:  2010-08-05       Impact factor: 4.942

6.  The mechanism of tryptophan induction of tryptophanase operon expression: tryptophan inhibits release factor-mediated cleavage of TnaC-peptidyl-tRNA(Pro).

Authors:  F Gong; K Ito; Y Nakamura; C Yanofsky
Journal:  Proc Natl Acad Sci U S A       Date:  2001-07-24       Impact factor: 11.205

7.  Highly conserved NIKS tetrapeptide is functionally essential in eukaryotic translation termination factor eRF1.

Authors:  Ludmila Frolova; Alim Seit-Nebi; Lev Kisselev
Journal:  RNA       Date:  2002-02       Impact factor: 4.942

8.  Convergence and constraint in eukaryotic release factor 1 (eRF1) domain 1: the evolution of stop codon specificity.

Authors:  Yuji Inagaki; Christian Blouin; W Ford Doolittle; Andrew J Roger
Journal:  Nucleic Acids Res       Date:  2002-01-15       Impact factor: 16.971

9.  Complex signals in the genomic 3' nontranslated region of bovine viral diarrhea virus coordinate translation and replication of the viral RNA.

Authors:  Olaf Isken; Claus W Grassmann; Haiying Yu; Sven-Erik Behrens
Journal:  RNA       Date:  2004-10       Impact factor: 4.942

10.  Assessing functional divergence in EF-1alpha and its paralogs in eukaryotes and archaebacteria.

Authors:  Yuji Inagaki; Christian Blouin; Edward Susko; Andrew J Roger
Journal:  Nucleic Acids Res       Date:  2003-07-15       Impact factor: 16.971

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