ArticleNucleic acids research2012
Structural basis for translation termination by archaeal RF1 and GTP-bound EF1α complex.
Article in Nucleic acids research, 2012. 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, 35 citations in OpenAlex.
- RNAViruses · 2026Review
- The origins and evolution of translation factors.Trends in genetics : TIG · 2025Review
- Novel archaeal ribosome dimerization factor facilitating unique 30S-30S dimerization.Nucleic acids research · 2025Article
- Cryo-electron microscopy structure and translocation mechanism of the crenarchaeal ribosome.Nucleic acids research · 2023Article
- A Zpr1 co-chaperone mediates folding of eukaryotic translation elongation factor 1A via a GTPase cycle.Molecular cell · 2023Article
- Stop Codon Usage as a Window into Genome Evolution: Mutation, Selection, Biased Gene Conversion and the TAG Paradox.Genome biology and evolution · 2022Article
- Variation in Release Factor Abundance Is Not Needed to Explain Trends in Bacterial Stop Codon Usage.Molecular biology and evolution · 2022Article
- Effective Population Size Predicts Local Rates but Not Local Mitigation of Read-through Errors.Molecular biology and evolution · 2021Article
- Switch of the interactions between the ribosomal stalk and EF1A in the GTP- and GDP-bound conformations.Scientific reports · 2019Article
- The Origin and Evolution of Release Factors: Implications for Translation Termination, Ribosome Rescue, and Quality Control Pathways.International journal of molecular sciences · 2019Review
- Evolutionary insights into Trm112-methyltransferase holoenzymes involved in translation between archaea and eukaryotes.Nucleic acids research · 2018Article
- Conformational Control of Translation Termination on the 70S Ribosome.Structure (London, England : 1993) · 2018Article
- Protein glutaminylation is a yeast-specific posttranslational modification of elongation factor 1A.The Journal of biological chemistry · 2017Article
- Trm112, a Protein Activator of Methyltransferases Modifying Actors of the Eukaryotic Translational Apparatus.Biomolecules · 2017Review
- Evolution of the archaeal and mammalian information processing systems: towards an archaeal model for human disease.Cellular and molecular life sciences : CMLS · 2017Review
- Article
- 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
- Structural Insights into tRNA Dynamics on the Ribosome.International journal of molecular sciences · 2015Review
- A SelB/EF-Tu/aIF2γ-like protein from Methanosarcina mazei in the GTP-bound form binds cysteinyl-tRNA(Cys.).Journal of structural and functional genomics · 2015Article
- Cryo-EM of ribosomal 80S complexes with termination factors reveals the translocated cricket paralysis virus IRES.Molecular cell · 2015Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
When a stop codon appears at the ribosomal A site, the class I and II release factors (RFs) terminate translation. In eukaryotes and archaea, the class I and II RFs form a heterodimeric complex, and complete the overall translation termination process in a GTP-dependent manner. However, the structural mechanism of the translation termination by the class I and II RF complex remains unresolved. In archaea, archaeal elongation factor 1 alpha (aEF1α), a carrier GTPase for tRNA, acts as a class II RF by forming a heterodimeric complex with archaeal RF1 (aRF1). We report the crystal structure of the aRF1·aEF1α complex, the first active class I and II RF complex. This structure remarkably resembles the tRNA·EF-Tu complex, suggesting that aRF1 is efficiently delivered to the ribosomal A site, by mimicking tRNA. It provides insights into the mechanism that couples GTP hydrolysis by the class II RF to stop codon recognition and peptidyl-tRNA hydrolysis by the class I RF. We discuss the different mechanisms by which aEF1α recognizes aRF1 and aPelota, another aRF1-related protein and molecular evolution of the three functions of aEF1α.
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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.