ArticleRNA (New York, N.Y.)2010
Three distinct peptides from the N domain of translation termination factor eRF1 surround stop codon in the ribosome.
Article in RNA (New York, N.Y.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 43 citations in OpenAlex.
- Synergistic Methods to Investigate Eukaryotic Translation and Its Quality Control.Journal of molecular biology · 2025Review
- The eRF1 degrader SRI-41315 acts as a molecular glue at the ribosomal decoding center.Nature chemical biology · 2024Article
- Two alternative conformations of mRNA in the human ribosome during elongation and termination of translation as revealed by EPR spectroscopy.Computational and structural biotechnology journal · 2021Article
- Pharmacological approaches for targeting cystic fibrosis nonsense mutations.European journal of medicinal chemistry · 2020Review
- Translation Termination and Ribosome Recycling in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018Review
- 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
- Hydroxylation and translational adaptation to stress: some answers lie beyond the STOP codon.Cellular and molecular life sciences : CMLS · 2016Review
- Chemical footprinting reveals conformational changes of 18S and 28S rRNAs at different steps of translation termination on the human ribosome.RNA (New York, N.Y.) · 2016Article
- 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
- 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
- In Aspergillus nidulans the suppressors suaA and suaC code for release factors eRF1 and eRF3 and suaD codes for a glutamine tRNA.G3 (Bethesda, Md.) · 2014Article
- Two-step model of stop codon recognition by eukaryotic release factor eRF1.Nucleic acids research · 2013Article
- The mechanism of eukaryotic translation initiation: new insights and challenges.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
- The elongation, termination, and recycling phases of translation in eukaryotes.Cold Spring Harbor perspectives in biology · 2012Review
- 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
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To study positioning of the polypeptide release factor eRF1 toward a stop signal in the ribosomal decoding site, we applied photoactivatable mRNA analogs, derivatives of oligoribonucleotides. The human eRF1 peptides cross-linked to these short mRNAs were identified. Cross-linkers on the guanines at the second, third, and fourth stop signal positions modified fragment 31-33, and to lesser extent amino acids within region 121-131 (the "YxCxxxF loop") in the N domain. Hence, both regions are involved in the recognition of the purines. A cross-linker at the first uridine of the stop codon modifies Val66 near the NIKS loop (positions 61-64), and this region is important for recognition of the first uridine of stop codons. Since the N domain distinct regions of eRF1 are involved in a stop-codon decoding, the eRF1 decoding site is discontinuous and is not of "protein anticodon" type. By molecular modeling, the eRF1 molecule can be fitted to the A site proximal to the P-site-bound tRNA and to a stop codon in mRNA via a large conformational change to one of its three domains. In the simulated eRF1 conformation, the YxCxxxF motif and positions 31-33 are very close to a stop codon, which becomes also proximal to several parts of the C domain. Thus, in the A-site-bound state, the eRF1 conformation significantly differs from those in crystals and solution. The model suggested for eRF1 conformation in the ribosomal A site and cross-linking data are compatible.
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