ArticleNature communications2018
Visualization of translation termination intermediates trapped by the Apidaecin 137 peptide during RF3-mediated recycling of RF1.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 69 citations in OpenAlex.
- Flipping antimicrobial peptides in the exit tunnel of the bacterial ribosome.Nature communications · 2026Article
- 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
- An RNA modification prevents extended codon-anticodon interactions from facilitating +1 frameshifting.Nature communications · 2025Article
- The origins and evolution of translation factors.Trends in genetics : TIG · 2025Review
- Substitution of Proline Residues by 4-Fluoro-l-Proline Affects the Mechanism of the Proline-Rich Antimicrobial Peptide Api137.Antibiotics (Basel, Switzerland) · 2025Article
- The structure of the Vibrio natriegens 70S ribosome in complex with the proline-rich antimicrobial peptide Bac5(1-17).Nucleic acids research · 2025Article
- The ribosome termination complex remodels release factor RF3 and ejects GDP.Nature structural & molecular biology · 2024Article
- Activity, structure, and diversity of Type II proline-rich antimicrobial peptides from insects.EMBO reports · 2024Article
- Sequence diversity of apidaecin-like peptides arresting the terminating ribosome.Nucleic acids research · 2024Article
- Integrating cryo-OrbiSIMS with computational modelling and metadynamics simulations enhances RNA structure prediction at atomic resolution.Nature communications · 2024Article
- Mechanistic insights into the alternative ribosome recycling by HflXr.Nucleic acids research · 2024Article
- Native architecture of a human GBP1 defense complex for cell-autonomous immunity to infection.Science (New York, N.Y.) · 2024Article
- Triphenylphosphonium Analogs of Short Peptide Related to Bactenecin 7 and Oncocin 112 as Antimicrobial Agents.Pharmaceutics · 2024Article
- Nonsense mutation suppression is enhanced by targeting different stages of the protein synthesis process.PLoS biology · 2023Article
- Structure-Activity Relationships of the Antimicrobial Peptide Natural Product Apidaecin.Journal of medicinal chemistry · 2023Article
- Structural basis for translation inhibition by the glycosylated drosocin peptide.Nature chemical biology · 2023Article
- Inhibition of translation termination by the antimicrobial peptide Drosocin.Nature chemical 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
- The Structural Dynamics of Translation.Annual review of biochemistry · 2022Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
During translation termination in bacteria, the release factors RF1 and RF2 are recycled from the ribosome by RF3. While high-resolution structures of the individual termination factors on the ribosome exist, direct structural insight into how RF3 mediates dissociation of the decoding RFs has been lacking. Here we have used the Apidaecin 137 peptide to trap RF1 together with RF3 on the ribosome and visualize an ensemble of termination intermediates using cryo-electron microscopy. Binding of RF3 to the ribosome induces small subunit (SSU) rotation and swivelling of the head, yielding intermediate states with shifted P-site tRNAs and RF1 conformations. RF3 does not directly eject RF1 from the ribosome, but rather induces full rotation of the SSU that indirectly dislodges RF1 from its binding site. SSU rotation is coupled to the accommodation of the GTPase domain of RF3 on the large subunit (LSU), thereby promoting GTP hydrolysis and dissociation of RF3 from the ribosome.
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