ArticleThe EMBO journal1995
Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3.
Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 259 papers, 1 of them a synthesis that pooled it.
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Who cites it
259 citing papers in PubMed, 1 synthesis or guideline pooled it, 598 citations in OpenAlex.
- PABPC1--mRNA stability, protein translation and tumorigenesis.Frontiers in oncology · 2022Pooled it
- Glutamine codon-driven translational readthrough reveals context-dependent stop codon decoding fidelity.bioRxiv : the preprint server for biology · 2026Article
- GSPT1-specific protein degradation is effective in preclinical models of chemoresistant MYCN-amplified neuroblastoma.Journal of experimental & clinical cancer research : CR · 2026Article
- Eukaryotic initiation factor eIF3 facilitates loading of eukaryotic release factor eRF1 or suppressor tRNA to the ribosome.Nucleic acids research · 2026Article
- Induction of Apoptosis and Activation of Endoplasmic Reticulum Stress by SJ6986 in Diffuse Large B-cell Lymphoma.Anti-cancer agents in medicinal chemistry · 2026Article
- Identity, functional consequences, and context effects of amino acids inserted during suppression of CFTR nonsense mutations.Journal of cystic fibrosis : official journal of the European Cystic Fibrosis Society · 2026Article
- Cancer Biology of GSPT1: Mechanisms and Targeted Therapy Opportunities of Molecular Glue Degraders.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Design and Application of Cereblon-Recruiting Prodegraders.Journal of the American Chemical Society · 2025Article
- Prion-Dependent Lethality ofInternational journal of molecular sciences · 2025Article
- Eukaryotic initiation factors eIF4F and eIF4B promote translation termination upon closed-loop formation.Nucleic acids research · 2025Article
- Innovative payloads for ADCs in cancer treatment: moving beyond the selective delivery of chemotherapy.Therapeutic advances in medical oncology · 2025Review
- Noncanonical Amino Acid Tools and Their Application to Membrane Protein Studies.Chemical reviews · 2024Review
- The ABCF ATPase New1 resolves translation termination defects associated with specific tRNAArg and tRNALys isoacceptors in the P site.Nucleic acids research · 2024Article
- Functional Activity of Isoform 2 of Human eRF1.International journal of molecular sciences · 2024Article
- The impact of mRNA poly(A) tail length on eukaryotic translation stages.Nucleic acids research · 2024Article
- Gene Expression Analysis of Yeast Strains with a Nonsense Mutation in the eRF3-Coding Gene Highlights Possible Mechanisms of Adaptation.International journal of molecular sciences · 2024Article
- The ABCF ATPase New1 resolves translation termination defects associated with specific tRNAbioRxiv : the preprint server for biology · 2024Article
- Amyloids and prions in the light of evolution.Current genetics · 2023Review
- The Properties and Domain Requirements for Phase Separation of the Sup35 Prion Protein In Vivo.Biomolecules · 2023Article
- How Big Is the Yeast Prion Universe?International journal of molecular sciences · 2023Review
199 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Termination of translation in higher organisms is a GTP-dependent process. However, in the structure of the single polypeptide chain release factor known so far (eRF1) there are no GTP binding motifs. Moreover, in prokaryotes, a GTP binding protein, RF3, stimulates translation termination. From these observations we proposed that a second eRF should exist, conferring GTP dependence for translation termination. Here, we have shown that the newly sequenced GTP binding Sup35-like protein from Xenopus laevis, termed eRF3, exhibits in vitro three important functional properties: (i) although being inactive as an eRF on its own, it greatly stimulates eRF1 activity in the presence of GTP and low concentrations of stop codons, resembling the properties of prokaryotic RF3; (ii) it binds and probably hydrolyses GTP; and (iii) it binds to eRF1. The structure of the C-domain of the X.laevis eRF3 protein is highly conserved with other Sup35-like proteins, as was also shown earlier for the eRF1 protein family. From these and our previous data, we propose that yeast Sup45 and Sup35 proteins belonging to eRF1 and eRF3 protein families respectively are also yeast termination factors. The absence of structural resemblance of eRF1 and eRF3 to prokaryotic RF1/2 and RF3 respectively, may point to the different evolutionary origin of the translation termination machinery in eukaryotes and prokaryotes. It is proposed that a quaternary complex composed of eRF1, eRF3, GTP and a stop codon of the mRNA is involved in termination of polypeptide synthesis in ribosomes.
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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.