ArticleNucleic acids research2006
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.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 69 citations in OpenAlex.
- Cancer Biology of GSPT1: Mechanisms and Targeted Therapy Opportunities of Molecular Glue Degraders.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- The orally bioavailable GSPT1/2 degrader SJ6986 exhibits in vivo efficacy in acute lymphoblastic leukemia.Blood · 2023Article
- Features and factors that dictate if terminating ribosomes cause or counteract nonsense-mediated mRNA decay.The Journal of biological chemistry · 2022Review
- Degradation of GSPT1 causes TP53-independent cell death in leukemia while sparing normal hematopoietic stem cells.The Journal of clinical investigation · 2022Article
- Mechanisms that ensure speed and fidelity in eukaryotic translation termination.Science (New York, N.Y.) · 2021Article
- Translation Termination and Ribosome Recycling in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018Review
- Structural Basis for Translation Termination on a Pseudouridylated Stop Codon.Journal of molecular biology · 2016Article
- 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
- Translational readthrough potential of natural termination codons in eucaryotes--The impact of RNA sequence.RNA biology · 2015Review
- Therapeutic suppression of premature termination codons: mechanisms and clinical considerations (review).International journal of molecular medicine · 2014Review
- 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
- Critical role of γ-phosphate in structural transition of Na,K-ATPase upon ATP binding.Scientific reports · 2014Article
- eIF5B employs a novel domain release mechanism to catalyze ribosomal subunit joining.The EMBO journal · 2014Article
- Structure of the mammalian ribosomal pre-termination complex associated with eRF1.eRF3.GDPNP.Nucleic acids research · 2014Article
- 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
- S-glutathionylation of the Na,K-ATPase catalytic α subunit is a determinant of the enzyme redox sensitivity.The Journal of biological chemistry · 2012Article
- GTPases IF2 and EF-G bind GDP and the SRL RNA in a mutually exclusive manner.Scientific reports · 2012Article
- Adenine and guanine recognition of stop codon is mediated by different N domain conformations of translation termination factor eRF1.Nucleic acids research · 2011Article
- Structural aspects of translation termination on the ribosome.RNA (New York, N.Y.) · 2011Review
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6 authors at 1 institution in 1 country.
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Abstract
GTP hydrolysis catalyzed in the ribosome by a complex of two polypeptide release factors, eRF1 and eRF3, is required for fast and efficient termination of translation in eukaryotes. Here, isothermal titration calorimetry is used for the quantitative thermodynamic characterization of eRF3 interactions with guanine nucleotides, eRF1 and Mg2+. We show that (i) eRF3 binds GDP (K(d) = 1.9 microM) and this interaction depends only minimally on the Mg(2+) concentration; (ii) GTP binds to eRF3 (K(d) = 0.5 microM) only in the presence of eRF1 and this interaction depends on the Mg2+ concentration; (iii) GTP displaces GDP from the eRF1*eRF3*GDP complex, and vice versa; (iv) eRF3 in the GDP-bound form improves its ability to bind eRF1; (v) the eRF1*eRF3 complex binds GDP as efficiently as free eRF3; (vi) the eRF1*eRF3 complex is efficiently formed in the absence of GDP/GTP but requires the presence of the C-terminus of eRF1 for complex formation. Our results show that eRF1 mediates GDP/GTP displacement on eRF3. We suggest that after formation of eRF1*eRF3*GTP*Mg2+, this quaternary complex binds to the ribosomal pretermination complex containing P-site-bound peptidyl-tRNA and the A-site-bound stop codon. The guanine nucleotide binding properties of eRF3 and of the eRF3*eRF1 complex profoundly differ from those of prokaryotic RF3.
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