ArticleProceedings of the National Academy of Sciences of the United States of America2007
Different modes of stop codon restriction by the Stylonychia and Paramecium eRF1 translation termination factors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 57 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
- Reaching New Heights in Genetic Code Manipulation with High Throughput Screening.Chemical reviews · 2024Review
- Eukaryotic release factor 1 from Euplotes promotes frameshifting at premature stop codons in human cells.iScience · 2024Article
- Identification of a non-canonical ciliate nuclear genetic code where UAA and UAG code for different amino acids.PLoS genetics · 2023Article
- Article
- Origin of the omnipotence of eukaryotic release factor 1.Nature communications · 2017Article
- Article
- Structural characterization of eRF1 mutants indicate a complex mechanism of stop codon recognition.Scientific reports · 2016Article
- Non-Standard Genetic Codes Define New Concepts for Protein Engineering.Life (Basel, Switzerland) · 2015Review
- 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
- New insights into stop codon recognition by eRF1.Nucleic acids research · 2015Article
- Efficient multisite unnatural amino acid incorporation in mammalian cells via optimized pyrrolysyl tRNA synthetase/tRNA expression and engineered eRF1.Journal of the American Chemical Society · 2014Article
- Two-step model of stop codon recognition by eukaryotic release factor eRF1.Nucleic acids research · 2013Article
- Structural basis for translation termination by archaeal RF1 and GTP-bound EF1α complex.Nucleic acids research · 2012Article
- Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1.Nucleic acids research · 2012Article
- Identification of eRF1 residues that play critical and complementary roles in stop codon recognition.RNA (New York, N.Y.) · 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
- Adenine and guanine recognition of stop codon is mediated by different N domain conformations of translation termination factor eRF1.Nucleic acids research · 2011Article
- A single amino acid change of translation termination factor eRF1 switches between bipotent and omnipotent stop-codon specificity.Nucleic acids research · 2011Article
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6 authors at 3 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
In universal-code eukaryotes, a single-translation termination factor, eukaryote class-1 polypeptide release factor (eRF1), decodes the three stop codons: UAA, UAG, and UGA. In some ciliates, like Stylonychia and Paramecium, eRF1s exhibit UGA-only decoding specificity, whereas UAG and UAA are reassigned as sense codons. Because variant-code ciliates may have evolved from universal-code ancestor(s), structural features should exist in ciliate eRF1s that restrict their stop codon recognition. In omnipotent eRF1s, stop codon recognition is associated with the N-terminal domain of the protein. Using both in vitro and in vivo assays, we show here that chimeric molecules composed of the N-terminal domain of Stylonychia eRF1 fused to the core domain (MC domain) of human eRF1 retained specificity toward UGA; this unambiguously associates eRF1 stop codon specificity to the nature of its N-terminal domain. Functional analysis of eRF1 chimeras constructed by swapping ciliate N-terminal domain sequences with the matching ones from the human protein highlighted the crucial role of the tripeptide QFM in restricting Stylonychia eRF1 specificity toward UGA. Using the site-directed mutagenesis, we show that Paramecium eRF1 specificity toward UGA resides within the NIKS (amino acids 61-64) and YxCxxxF (amino acids 124-131) motifs. Thus, we establish that eRF1 from two different ciliates relies on different molecular mechanisms to achieve specificity toward the UGA stop codon. This finding suggests that eRF1 restriction of specificity to only UGA might have been an early event occurring in independent instances in ciliate evolutionary history, possibly facilitating the reassignment of UAG and UAA to sense codons.
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