ArticleRNA (New York, N.Y.)1999
C-terminal interaction of translational release factors eRF1 and eRF3 of fission yeast: G-domain uncoupled binding and the role of conserved amino acids.
Article in RNA (New York, N.Y.), 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 75 citations in OpenAlex.
- Two classes of EF1-family translational GTPases encoded by giant viruses.Nucleic acids research · 2019Article
- Structural characterization of eRF1 mutants indicate a complex mechanism of stop codon recognition.Scientific reports · 2016Article
- Crystallization and preliminary X-ray analysis of the C-terminal fragment of Ski7 from Saccharomyces cerevisiae.Acta crystallographica. Section F, Structural biology communications · 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
- Three distinct peptides from the N domain of translation termination factor eRF1 surround stop codon in the ribosome.RNA (New York, N.Y.) · 2010Article
- NMR solution structure and function of the C-terminal domain of eukaryotic class 1 polypeptide chain release factor.The FEBS journal · 2010Article
- 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
- Evolution of nonstop, no-go and nonsense-mediated mRNA decay and their termination factor-derived components.BMC evolutionary biology · 2008Article
- Mutation at tyrosine in AMLRY (GILRY like) motif of yeast eRF1 on nonsense codons suppression and binding affinity to eRF3.International journal of biological sciences · 2008Article
- Proteasomal degradation of human release factor eRF3a regulates translation termination complex formation.RNA (New York, N.Y.) · 2008Article
- N-terminal region of Saccharomyces cerevisiae eRF3 is essential for the functioning of the eRF1/eRF3 complex beyond translation termination.BMC molecular biology · 2006Article
- Eukaryotic release factor 1 phosphorylation by CK2 protein kinase is dynamic but has little effect on the efficiency of translation termination in Saccharomyces cerevisiae.Eukaryotic cell · 2006Article
- Termination of translation in eukaryotes is mediated by the quaternary eRF1*eRF3*GTP*Mg2+ complex. The biological roles of eRF3 and prokaryotic RF3 are profoundly distinct.Nucleic acids research · 2006Article
- Distinct paths to stop codon reassignment by the variant-code organisms Tetrahymena and Euplotes.Molecular and cellular biology · 2006Article
- GTP hydrolysis by eRF3 facilitates stop codon decoding during eukaryotic translation termination.Molecular and cellular biology · 2004Article
- Antizyme frameshifting as a functional probe of eukaryotic translational termination.Nucleic acids research · 2003Article
- Assessing functional divergence in EF-1alpha and its paralogs in eukaryotes and archaebacteria.Nucleic acids research · 2003Article
- Viable nonsense mutants for the essential gene SUP45 of Saccharomyces cerevisiae.BMC molecular biology · 2003Article
- Inhibition of translation termination mediated by an interaction of eukaryotic release factor 1 with a nascent peptidyl-tRNA.Molecular and cellular biology · 2002Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Translation termination in eukaryotes requires a stop codon-responsive (class-I) release factor, eRF1, and a guanine nucleotide-responsive (class-II) release factor, eRF3. Schizosaccharomyces pombe eRF3 has an N-terminal polypeptide similar in size to the prion-like domain of Saccharomyces cerevisiae eRF3 in addition to the EF-1alpha-like catalytic domain. By in vivo two-hybrid assay as well as by an in vitro pull-down analysis using purified proteins of S. pombe as well as of S. cerevisiae, eRF1 bound to the C-terminal one-third domain of eRF3, named eRF3C, but not to the N-terminal two-thirds, which was inconsistent with the previous report by Paushkin et al. (1997, Mol Cell Biol 17:2798-2805). The activity of S. pombe eRF3 in eRF1 binding was affected by Ala substitutions for the C-terminal residues conserved not only in eRF3s but also in elongation factors EF-Tu and EF-1alpha. These single mutational defects in the eRF1-eRF3 interaction became evident when either truncated protein eRF3C or C-terminally altered eRF1 proteins were used for the authentic protein, providing further support for the presence of a C-terminal interaction. Given that eRF3 is an EF-Tu/EF-1alpha homolog required for translation termination, the apparent dispensability of the N-terminal domain of eRF3 for binding to eRF1 is in contrast to importance, direct or indirect, in EF-Tu/EF-1alpha for binding to aminoacyl-tRNA, although both eRF3 and EF-Tu/EF-1alpha share some common amino acids for binding to eRF1 and aminoacyl-tRNA, respectively. These differences probably reflect the independence of eRF1 binding in relation to the G-domain function of eRF3 (i.e., probably uncoupled with GTP hydrolysis), whereas aminoacyl-tRNA binding depends on that of EF-Tu/EF-1alpha(i.e., coupled with GTP hydrolysis), which sheds some light on the mechanism of eRF3 function.
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