ArticleNucleic acids research2005
Invariant amino acids essential for decoding function of polypeptide release factor eRF1.
Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 69 citations in OpenAlex.
- RNAViruses · 2026Review
- 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
- Functional Activity of Isoform 2 of Human eRF1.International journal of molecular sciences · 2024Article
- The eRF1 degrader SRI-41315 acts as a molecular glue at the ribosomal decoding center.Nature chemical biology · 2024Article
- 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
- Genetically Encoded Protein Phosphorylation in Mammalian Cells.Cell chemical biology · 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
- Origin of the omnipotence of eukaryotic release factor 1.Nature communications · 2017Article
- Structural characterization of eRF1 mutants indicate a complex mechanism of stop codon recognition.Scientific reports · 2016Article
- Article
- 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
- Translational readthrough potential of natural termination codons in eucaryotes--The impact of RNA sequence.RNA biology · 2015Review
- 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
- The elongation, termination, and recycling phases of translation in eukaryotes.Cold Spring Harbor perspectives in biology · 2012Review
- 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
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In eukaryotic ribosome, the N domain of polypeptide release factor eRF1 is involved in decoding stop signals in mRNAs. However, structure of the decoding site remains obscure. Here, we specifically altered the stop codon recognition pattern of human eRF1 by point mutagenesis of the invariant Glu55 and Tyr125 residues in the N domain. The 3D structure of generated eRF1 mutants was not destabilized as demonstrated by calorimetric measurements and calculated free energy perturbations. In mutants, the UAG response was most profoundly and selectively affected. Surprisingly, Glu55Arg mutant completely retained its release activity. Substitution of the aromatic ring in position 125 reduced response toward all stop codons. This result demonstrates the critical importance of Tyr125 for maintenance of the intact structure of the eRF1 decoding site. The results also suggest that Tyr125 is implicated in recognition of the 3d stop codon position and probably forms an H-bond with Glu55. The data point to a pivotal role played by the YxCxxxF motif (positions 125-131) in purine discrimination of the stop codons. We speculate that eRF1 decoding site is formed by a 3D network of amino acids side chains.
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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.