ArticleRNA (New York, N.Y.)1998
The stretch of C-terminal acidic amino acids of translational release factor eRF1 is a primary binding site for eRF3 of fission yeast.
Article in RNA (New York, N.Y.), 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 110 citations in OpenAlex.
- Synergistic Methods to Investigate Eukaryotic Translation and Its Quality Control.Journal of molecular biology · 2025Review
- Tissue-specific regulation of translational readthrough tunes functions of the traffic jam transcription factor.Nucleic acids research · 2022Article
- Upf proteins: highly conserved factors involved in nonsense mRNA mediated decay.Molecular biology reports · 2018Review
- A thiol probe for measuring unfolded protein load and proteostasis in cells.Nature communications · 2017Article
- 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
- 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
- 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
- Structural basis for translation termination by archaeal RF1 and GTP-bound EF1α complex.Nucleic acids research · 2012Article
- Prions in yeast.Genetics · 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
- A single amino acid change of translation termination factor eRF1 switches between bipotent and omnipotent stop-codon specificity.Nucleic acids research · 2011Article
- Omnipotent role of archaeal elongation factor 1 alpha (EF1α in translational elongation and termination, and quality control of protein synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- NMR solution structure and function of the C-terminal domain of eukaryotic class 1 polypeptide chain release factor.The FEBS journal · 2010Article
- The paradox of viable sup45 STOP mutations: a necessary equilibrium between translational readthrough, activity and stability of the protein.Molecular genetics and genomics : MGG · 2009Article
- Connection between stop codon reassignment and frequent use of shifty stop frameshifting.RNA (New York, N.Y.) · 2009Article
- Structural insights into eRF3 and stop codon recognition by eRF1.Genes & development · 2009Article
- Molecular dissection of translation termination mechanism identifies two new critical regions in eRF1.Nucleic acids research · 2009Article
- Evolution of nonstop, no-go and nonsense-mediated mRNA decay and their termination factor-derived components.BMC evolutionary biology · 2008Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Translation termination in eukaryotes requires a codon-specific (class-I) release factor, eRF1, and a GTP/GDP-dependent (class-II) release factor, eRF3. The model of "molecular mimicry between release factors and tRNA" predicts that eRF1 mimics tRNA to read the stop codon and that eRF3 mimics elongation factor EF-Tu to bring eRF1 to the A site of the ribosome for termination of protein synthesis. In this study, we set up three systems, in vitro affinity binding, a yeast two-hybrid system, and in vitro competition assay, to determine the eRF3-binding site of eRF1 using the fission yeast Schizosaccharomyces pombe proteins and creating systematic deletions in eRF1. The in vitro affinity binding experiments demonstrated that the predicted tRNA-mimicry truncation of eRF1 (Sup45) forms a stable complex with eRF3 (Sup35). All three test systems revealed that the most critical binding site is located at the C-terminal region of eRF1, which is conserved among eukaryotic eRF1s and rich in acidic amino acids. To our surprise, however, the C-terminal deletion eRF1 seems to be sufficient for cell viability in spite of the severe defect in eRF3 binding when expressed in a temperature-sensitive sup45 mutant of the budding yeast, Saccharomyces cerevisiae. These results cannot be accounted for by the simple "eRF3-EF-Tu mimicry" model, but may provide new insight into the eRF3 function for translation termination in eukaryotes.
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