ArticleeLife2018
Dynamics of ribosomes and release factors during translation termination in
Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
31 citing papers in PubMed, 64 citations in OpenAlex.
- A cascade of structural rearrangements positions peptide release factor 2 for polypeptide hydrolysis on the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The role of ribosomal protein networks in ribosome dynamics.Nucleic acids research · 2025Article
- The ribosome termination complex remodels release factor RF3 and ejects GDP.Nature structural & molecular biology · 2024Article
- Kinetics of programmed and spontaneous ribosome sliding along the mRNA.Nucleic acids research · 2024Article
- Application of bio-layer interferometry for the analysis of ribosome-protein interactions.Frontiers in molecular biosciences · 2024Article
- Nonsense mutation suppression is enhanced by targeting different stages of the protein synthesis process.PLoS biology · 2023Article
- Dynamics of release factor recycling during translation termination in bacteria.Nucleic acids research · 2023Article
- Quality control of protein synthesis in the early elongation stage.Nature communications · 2023Article
- Interplay between Inter-Subunit Rotation of the Ribosome and Binding of Translational GTPases.International journal of molecular sciences · 2023Article
- Peptide chain release factor DIG8 regulates plant growth by affecting ROS-mediated sugar transportation inFrontiers in plant science · 2023Article
- The Structural Dynamics of Translation.Annual review of biochemistry · 2022Review
- Antimicrobial Activity and 70S Ribosome Binding of Apidaecin-Derived Api805 with Increased Bacterial Uptake Rate.Antibiotics (Basel, Switzerland) · 2022Article
- Structural basis of l-tryptophan-dependent inhibition of release factor 2 by the TnaC arrest peptide.Nucleic acids research · 2021Article
- Diversity and Similarity of Termination and Ribosome Rescue in Bacterial, Mitochondrial, and Cytoplasmic Translation.Biochemistry. Biokhimiia · 2021Review
- In silico analysis of bacterial translation factors reveal distinct translation event specific pI values.BMC genomics · 2021Article
- Charting the sequence-activity landscape of peptide inhibitors of translation termination.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Evolution of the Standard Genetic Code.Journal of molecular evolution · 2021Article
- ArfB can displace mRNA to rescue stalled ribosomes.Nature communications · 2020Article
- Genome-wide effects of the antimicrobial peptide apidaecin on translation termination in bacteria.eLife · 2020Article
- Molecular determinants of release factor 2 for ArfA-mediated ribosome rescue.The Journal of biological chemistry · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Release factors RF1 and RF2 promote hydrolysis of peptidyl-tRNA during translation termination. The GTPase RF3 promotes recycling of RF1 and RF2. Using single molecule FRET and biochemical assays, we show that ribosome termination complexes that carry two factors, RF1-RF3 or RF2-RF3, are dynamic and fluctuate between non-rotated and rotated states, whereas each factor alone has its distinct signature on ribosome dynamics and conformation. Dissociation of RF1 depends on peptide release and the presence of RF3, whereas RF2 can dissociate spontaneously. RF3 binds in the GTP-bound state and can rapidly dissociate without GTP hydrolysis from termination complex carrying RF1. In the absence of RF1, RF3 is stalled on ribosomes if GTP hydrolysis is blocked. Our data suggest how the assembly of the ribosome-RF1-RF3-GTP complex, peptide release, and ribosome fluctuations promote termination of protein synthesis and recycling of the release factors.
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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.