ArticleNucleic acids research2012
Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- RNAViruses · 2026Review
- Functional Activity of Isoform 2 of Human eRF1.International journal of molecular sciences · 2024Article
- Article
- Translation Termination and Ribosome Recycling in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018Review
- 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
- Structure of a human translation termination complex.Nucleic acids research · 2015Article
- 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
- Two-step model of stop codon recognition by eukaryotic release factor eRF1.Nucleic acids research · 2013Article
- GTPases IF2 and EF-G bind GDP and the SRL RNA in a mutually exclusive manner.Scientific reports · 2012Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Translation termination in eukaryotes is catalyzed by two release factors eRF1 and eRF3 in a cooperative manner. The precise mechanism of stop codon discrimination by eRF1 remains obscure, hindering drug development targeting aberrations at translation termination. By solving the solution structures of the wild-type N-domain of human eRF1 exhibited omnipotent specificity, i.e. recognition of all three stop codons, and its unipotent mutant with UGA-only specificity, we found the conserved GTS loop adopting alternate conformations. We propose that structural variability in the GTS loop may underline the switching between omnipotency and unipotency of eRF1, implying the direct access of the GTS loop to the stop codon. To explore such feasibility, we positioned N-domain in a pre-termination ribosomal complex using the binding interface between N-domain and model RNA oligonucleotides mimicking Helix 44 of 18S rRNA. NMR analysis revealed that those duplex RNA containing 2-nt internal loops interact specifically with helix α1 of N-domain, and displace C-domain from a non-covalent complex of N-domain and C-domain, suggesting domain rearrangement in eRF1 that accompanies N-domain accommodation into the ribosomal A site.
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