ArticleProceedings of the National Academy of Sciences of the United States of America2002
Omnipotent decoding potential resides in eukaryotic translation termination factor eRF1 of variant-code organisms and is modulated by the interactions of amino acid sequences within domain 1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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36 citing papers in PubMed, 83 citations in OpenAlex.
- Misdecoding of rare CGA codon by translation termination factors, eRF1/eRF3, suggests novel class of ribosome rescue pathway in S. cerevisiae.The FEBS journal · 2019Article
- Eukaryotic translational termination efficiency is influenced by the 3' nucleotides within the ribosomal mRNA channel.Nucleic acids research · 2018Article
- Atomic mutagenesis of stop codon nucleotides reveals the chemical prerequisites for release factor-mediated peptide release.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- 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
- Therapeutic suppression of premature termination codons: mechanisms and clinical considerations (review).International journal of molecular medicine · 2014Review
- A genetic approach for analyzing the co-operative function of the tRNA mimicry complex, eRF1/eRF3, in translation termination on the ribosome.Nucleic acids research · 2014Article
- Structure of the mammalian ribosomal pre-termination complex associated with eRF1.eRF3.GDPNP.Nucleic acids research · 2014Article
- Overcoming stalled translation in human mitochondria.Frontiers in microbiology · 2014Article
- Protein biosynthesis in mitochondria.Biochemistry. Biokhimiia · 2013Review
- 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
- Termination of protein synthesis in mammalian mitochondria.The Journal of biological chemistry · 2011Review
- A single amino acid change of translation termination factor eRF1 switches between bipotent and omnipotent stop-codon specificity.Nucleic acids research · 2011Article
- Three distinct peptides from the N domain of translation termination factor eRF1 surround stop codon in the ribosome.RNA (New York, N.Y.) · 2010Article
- Fidelity in archaeal information processing.Archaea (Vancouver, B.C.) · 2010Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In eukaryotes, a single translational release factor, eRF1, deciphers three stop codons, although its decoding mechanism remains puzzling. In the ciliate Tetrahymena thermophila, UAA and UAG codons are reassigned to Gln codons. A yeast eRF1-domain swap containing Tetrahymena domain 1 responded only to UGA in vitro and failed to complement a defect in yeast eRF1 in vivo at 37 degrees C. This finding demonstrates that decoding specificity of eRF1 from variant code organisms resides at domain 1. However, the wild-type eRF1 hybrid fully restored the growth of eRF1-deficient yeast at 30 degrees C. Tetrahymena eRF1 contains a variant sequence, KATNIKD, at the tip of domain 1. The TASNIKD variant of hybrid eRF1 rendered the eRF1-nullified yeast viable, although in an in vitro assay, the same hybrid eRF1 responded only to UGA. Nevertheless, the yeast eRF1 bearing the KATNIKD motif instead of the TASNIKS heptapeptide present in higher eukaryotes remains omnipotent in vivo. Collectively, these data suggest that variant genetic code organisms like Tetrahymena have an intrinsic potential to decode three stop codons in vivo, and that interaction within domain 1 between the KAT tripeptide and other sequences modulates the decoding specificity of Tetrahymena eRF1.
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