ArticleNucleic acids research2002
Convergence and constraint in eukaryotic release factor 1 (eRF1) domain 1: the evolution of stop codon specificity.
Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 73 citations in OpenAlex.
- High throughput screening of eukaryotic release factor 1 variants to enhance noncanonical amino acid incorporation.bioRxiv : the preprint server for biology · 2025Article
- Article
- Specificity of mRNA binding to proteins within the NMD machinery is influenced in cancer.Frontiers in molecular biosciences · 2025Article
- Eukaryotic translational termination efficiency is influenced by the 3' nucleotides within the ribosomal mRNA channel.Nucleic acids research · 2018Article
- Article
- Structural characterization of eRF1 mutants indicate a complex mechanism of stop codon recognition.Scientific reports · 2016Article
- Genetic analysis of L123 of the tRNA-mimicking eukaryote release factor eRF1, an amino acid residue critical for discrimination of stop codons.Nucleic acids research · 2015Article
- Two-step model of stop codon recognition by eukaryotic release factor eRF1.Nucleic acids research · 2013Article
- Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1.Nucleic acids research · 2012Article
- Structure and dynamics in solution of the stop codon decoding N-terminal domain of the human polypeptide chain release factor eRF1.Protein science : a publication of the Protein Society · 2012Article
- On the Diversification of the Translation Apparatus across Eukaryotes.Comparative and functional genomics · 2012Article
- A single amino acid change of translation termination factor eRF1 switches between bipotent and omnipotent stop-codon specificity.Nucleic acids research · 2011Article
- Complex phylogenetic distribution of a non-canonical genetic code in green algae.BMC evolutionary biology · 2010Article
- Three distinct peptides from the N domain of translation termination factor eRF1 surround stop codon in the ribosome.RNA (New York, N.Y.) · 2010Article
- Decoding accuracy in eRF1 mutants and its correlation with pleiotropic quantitative traits in yeast.Nucleic acids research · 2010Article
- Connection between stop codon reassignment and frequent use of shifty stop frameshifting.RNA (New York, N.Y.) · 2009Article
- Tandem stop codons in ciliates that reassign stop codons.Journal of molecular evolution · 2009Article
- Evolution of nonstop, no-go and nonsense-mediated mRNA decay and their termination factor-derived components.BMC evolutionary biology · 2008Article
- Distinct eRF3 requirements suggest alternate eRF1 conformations mediate peptide release during eukaryotic translation termination.Molecular cell · 2008Article
- Different modes of stop codon restriction by the Stylonychia and Paramecium eRF1 translation termination factors.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Class 1 release factor in eukaryotes (eRF1) recognizes stop codons and promotes peptide release from the ribosome. The 'molecular mimicry' hypothesis suggests that domain 1 of eRF1 is analogous to the tRNA anticodon stem-loop. Recent studies strongly support this hypothesis and several models for specific interactions between stop codons and residues in domain 1 have been proposed. In this study we have sequenced and identified novel eRF1 sequences across a wide diversity of eukaryotes and re-evaluated the codon-binding site by bioinformatic analyses of a large eRF1 dataset. Analyses of the eRF1 structure combined with estimates of evolutionary rates at amino acid sites allow us to define the residues that are under structural (i.e. those involved in intramolecular interactions) versus non-structural selective constraints. Furthermore, we have re-assessed convergent substitutions in the ciliate variant code eRF1s using maximum likelihood-based phylogenetic approaches. Our results favor the model proposed by Bertram et al. that stop codons bind to three 'cavities' on the protein surface, although we suggest that the stop codon may bind in the opposite orientation to the original model. We assess the feasibility of this alternative binding orientation with a triplet stop codon and the eRF1 domain 1 structures using molecular modeling techniques.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.