ArticleNature communications2021
Structural mechanism of GTPase-powered ribosome-tRNA movement.
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 44 papers.
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Who cites it
44 citing papers in PubMed, 65 citations in OpenAlex.
- Recoding by NNature communications · 2026Article
- Structural characterization of ribosome recycling and fusidic acid inhibition in Staphylococcus aureus.Nucleic acids research · 2026Article
- How Medically Important Antimicrobials Bind to the 30S Ribosomal Subunit in a Bacterial Pathogen.Biochemistry · 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
- 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
- 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
- Selective silencing of antibiotic-tethered ribosomes as a resistance mechanism against aminoglycosides.Nature communications · 2025Article
- Mechanisms of fusidic acid resistance.Biochemical Society transactions · 2025Review
- Multi-channel smFRET study reveals a compact conformation of EF-G on the ribosome.The international journal of biochemistry & cell biology · 2025Article
- Evolutionary insights into elongation factor G using AlphaFold and ancestral analysis.Computers in biology and medicine · 2025Article
- The role of ribosomal protein networks in ribosome dynamics.Nucleic acids research · 2025Article
- Elongation factor 2 in cancer: a promising therapeutic target in protein translation.Cellular & molecular biology letters · 2024Review
- Paenilamicins are context-specific translocation inhibitors of protein synthesis.Nature chemical biology · 2024Article
- The ribosome termination complex remodels release factor RF3 and ejects GDP.Nature structural & molecular biology · 2024Article
- Allosteric Effects of EF-G Domain I Mutations Inducing Ribosome Frameshifting Revealed by Multiplexed Force Spectroscopy.Chembiochem : a European journal of chemical biology · 2024Article
- Developing Multichannel smFRET Approach to Dissecting Ribosomal Mechanisms.Chemical & biomedical imaging · 2024Article
- Structures of the Staphylococcus aureus ribosome inhibited by fusidic acid and fusidic acid cyclopentane.Scientific reports · 2024Article
- Paenilamicins from the honey bee pathogenbioRxiv : the preprint server for biology · 2024Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
GTPases are regulators of cell signaling acting as molecular switches. The translational GTPase EF-G stands out, as it uses GTP hydrolysis to generate force and promote the movement of the ribosome along the mRNA. The key unresolved question is how GTP hydrolysis drives molecular movement. Here, we visualize the GTPase-powered step of ongoing translocation by time-resolved cryo-EM. EF-G in the active GDP-Pi form stabilizes the rotated conformation of ribosomal subunits and induces twisting of the sarcin-ricin loop of the 23 S rRNA. Refolding of the GTPase switch regions upon Pi release initiates a large-scale rigid-body rotation of EF-G pivoting around the sarcin-ricin loop that facilitates back rotation of the ribosomal subunits and forward swiveling of the head domain of the small subunit, ultimately driving tRNA forward movement. The findings demonstrate how a GTPase orchestrates spontaneous thermal fluctuations of a large RNA-protein complex into force-generating molecular movement.
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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.