ArticleNature communications2021
Time-resolved cryo-EM visualizes ribosomal translocation with EF-G and GTP.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 92 citations in OpenAlex.
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- Structural characterization of ribosome recycling and fusidic acid inhibition in Staphylococcus aureus.Nucleic acids research · 2026Article
- Molecular mechanism of IF1- and IF2-driven translation initiation in bacteria.bioRxiv : the preprint server for biology · 2026Article
- RiboScreenBiomedicines · 2026Review
- Structural studies of nedicistrovirus IRES-driven, initiation factor-independent translation shed light on key steps of eukaryotic translation elongation.Nucleic acids research · 2026Article
- Capturing ribosomal structures in cellular extracts with cryoPRISM: A purification-free cryoEM approach reveals novel structural states.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Ribosome heterogeneity and specialization in musculoskeletal physiology and pathology.JBMR plus · 2026Article
- Advances in Crystallography and Cryo-Electron Microscopy for the Study of Membrane Proteins.Advances in experimental medicine and biology · 2026Review
- The ribosome derives the energy to translocate and unwind mRNA from EF-G binding.Nature communications · 2025Article
- Structural mechanism of mRNA decoding by mammalian GTPase GTPBP1.Nature communications · 2025Article
- EF-G Mutations Reveal Correlation between Power Stroke and Translocation Fidelity in Protein Synthesis.bioRxiv : the preprint server for biology · 2025Article
- Saskemycin, a potent and selective antimycobacterial agent targeting a unique site on the ribosome.Research square · 2025Article
- Structural Studies of Nedicistrovirus IRES-Driven, Initiation Factor-independent Translation Shed Light on Key Steps of Eukaryotic Translation Elongation.bioRxiv : the preprint server for biology · 2025Article
- Structural mechanism of mRNA decoding by mammalian GTPase GTPBP1.bioRxiv : the preprint server for biology · 2025Article
- Mechanisms of fusidic acid resistance.Biochemical Society transactions · 2025Review
- An RNA modification prevents extended codon-anticodon interactions from facilitating +1 frameshifting.Nature communications · 2025Article
- Multi-channel smFRET study reveals a compact conformation of EF-G on the ribosome.The international journal of biochemistry & cell biology · 2025Article
- Advancing time-resolved structural biology: latest strategies in cryo-EM and X-ray crystallography.Nature methods · 2025Review
10 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
During translation, a conserved GTPase elongation factor-EF-G in bacteria or eEF2 in eukaryotes-translocates tRNA and mRNA through the ribosome. EF-G has been proposed to act as a flexible motor that propels tRNA and mRNA movement, as a rigid pawl that biases unidirectional translocation resulting from ribosome rearrangements, or by various combinations of motor- and pawl-like mechanisms. Using time-resolved cryo-EM, we visualized GTP-catalyzed translocation without inhibitors, capturing elusive structures of ribosome•EF-G intermediates at near-atomic resolution. Prior to translocation, EF-G binds near peptidyl-tRNA, while the rotated 30S subunit stabilizes the EF-G GTPase center. Reverse 30S rotation releases Pi and translocates peptidyl-tRNA and EF-G by ~20 Å. An additional 4-Å translocation initiates EF-G dissociation from a transient ribosome state with highly swiveled 30S head. The structures visualize how nearly rigid EF-G rectifies inherent and spontaneous ribosomal dynamics into tRNA-mRNA translocation, whereas GTP hydrolysis and Pi release drive EF-G dissociation.
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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.