ArticleNature communications2019
The structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
What it found
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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
40 citing papers in PubMed, 42 citations in OpenAlex.
- Article
- Article
- 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
- Defective Ribosome Recycling: A Bridge Between Translation Fidelity, Organelle Dysfunction, and Diseases: Exploring How Flawed Ribosome Recycling Factors Impact Ribosome Metabolism and Organelle Homeostasis, Leading to Human Diseases.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Evolution of ribosome X-ray crystallography: from first crystals to atomic resolution.Biophysical reviews · 2025Review
- Distant ribose 2'-O-methylation of 23S rRNA helix 69 pre-orders the capreomycin drug binding pocket at the ribosome subunit interface.Nucleic acids research · 2025Article
- The origins and evolution of translation factors.Trends in genetics : TIG · 2025Review
- Structure-function comparison of Arbekacin with other aminoglycosides elucidates its higher potency as bacterial translation inhibitor.Scientific reports · 2025Article
- Xenon plasma focused ion beam lamella fabrication on high-pressure frozen specimens for structural cell biology.Nature communications · 2025Article
- Efficient Incorporation of DOPA into Proteins Free from Competition with Endogenous Translation Termination Machinery.Biomolecules · 2025Article
- Transient disome complex formation in native polysomes during ongoing protein synthesis captured by cryo-EM.Nature communications · 2024Article
- Article
- Embracing Heterogeneity: Challenging the Paradigm of Replisomes as Deterministic Machines.Chemical reviews · 2023Review
- Dynamics of release factor recycling during translation termination in bacteria.Nucleic acids research · 2023Article
- Salt-Specific Suppression of the Cold Denaturation of Thermophilic Multidomain Initiation Factor 2.International journal of molecular sciences · 2023Article
- Antibiotic thermorubin tethers ribosomal subunits and impedes A-site interactions to perturb protein synthesis in bacteria.Nature communications · 2023Article
- Frozen in time: analyzing molecular dynamics with time-resolved cryo-EM.Structure (London, England : 1993) · 2023Review
- A simple flash and freeze system for cryogenic time-resolved electron microscopy.Frontiers in molecular biosciences · 2023Article
- Exploring the Structural Variability of Dynamic Biological Complexes by Single-Particle Cryo-Electron Microscopy.Micromachines · 2022Review
- Structural dynamics: review of time-resolved cryo-EM.Acta crystallographica. Section D, Structural biology · 2022Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
When the ribosome encounters a stop codon, it recruits a release factor (RF) to hydrolyze the ester bond between the peptide chain and tRNA. RFs have structural motifs that recognize stop codons in the decoding center and a GGQ motif for induction of hydrolysis in the peptidyl transfer center 70 Å away. Surprisingly, free RF2 is compact, with only 20 Å between its codon-reading and GGQ motifs. Cryo-EM showed that ribosome-bound RFs have extended structures, suggesting that RFs are compact when entering the ribosome and then extend their structures upon stop codon recognition. Here we use time-resolved cryo-EM to visualize transient compact forms of RF1 and RF2 at 3.5 and 4 Å resolution, respectively, in the codon-recognizing ribosome complex on the native pathway. About 25% of complexes have RFs in the compact state at 24 ms reaction time, and within 60 ms virtually all ribosome-bound RFs are transformed to their extended forms.
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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.