ArticleThe FEBS journal2010
NMR solution structure and function of the C-terminal domain of eukaryotic class 1 polypeptide chain release factor.
Article in The FEBS journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- Exploring the conformational landscape of adenylate kinase and beyond with protein folding models.Scientific reports · 2026Article
- Synergistic Methods to Investigate Eukaryotic Translation and Its Quality Control.Journal of molecular biology · 2025Review
- Two classes of EF1-family translational GTPases encoded by giant viruses.Nucleic acids research · 2019Article
- Translation Termination and Ribosome Recycling in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018Review
- Cryo-EM of ribosomal 80S complexes with termination factors reveals the translocated cricket paralysis virus IRES.Molecular cell · 2015Article
- Therapeutic suppression of premature termination codons: mechanisms and clinical considerations (review).International journal of molecular medicine · 2014Review
- Cryoelectron microscopic structures of eukaryotic translation termination complexes containing eRF1-eRF3 or eRF1-ABCE1.Cell reports · 2014Article
- 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
- The actinobacterial transcription factor RbpA binds to the principal sigma subunit of RNA polymerase.Nucleic acids research · 2013Article
- Cryo-EM structure of the mammalian eukaryotic release factor eRF1-eRF3-associated termination complex.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- 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
- Adenine and guanine recognition of stop codon is mediated by different N domain conformations of translation termination factor eRF1.Nucleic acids research · 2011Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
Termination of translation in eukaryotes is triggered by two polypeptide chain release factors, eukaryotic class 1 polypeptide chain release factor (eRF1) and eukaryotic class 2 polypeptide chain release factor 3. eRF1 is a three-domain protein that interacts with eukaryotic class 2 polypeptide chain release factor 3 via its C-terminal domain (C-domain). The high-resolution NMR structure of the human C-domain (residues 277-437) has been determined in solution. The overall fold and the structure of the beta-strand core of the protein in solution are similar to those found in the crystal structure. The structure of the minidomain (residues 329-372), which was ill-defined in the crystal structure, has been determined in solution. The protein backbone dynamics, studied using (15)N-relaxation experiments, showed that the C-terminal tail 414-437 and the minidomain are the most flexible parts of the human C-domain. The minidomain exists in solution in two conformational states, slowly interconverting on the NMR timescale. Superposition of this NMR solution structure of the human C-domain onto the available crystal structure of full-length human eRF1 shows that the minidomain is close to the stop codon-recognizing N-terminal domain. Mutations in the tip of the minidomain were found to affect the stop codon specificity of the factor. The results provide new insights into the possible role of the C-domain in the process of translation termination.
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Registered trials
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.