ArticleJournal of molecular biology2015
Movement of elongation factor G between compact and extended conformations.
Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Article
- Multi-channel smFRET study reveals a compact conformation of EF-G on the ribosome.The international journal of biochemistry & cell biology · 2025Article
- Gene-Gene Interactions Reduce Aminoglycoside Susceptibility ofAntibiotics (Basel, Switzerland) · 2023Article
- Mechanisms of ribosome recycling in bacteria and mitochondria: a structural perspective.RNA biology · 2022Review
- Time-resolved cryo-EM visualizes ribosomal translocation with EF-G and GTP.Nature communications · 2021Article
- Crystal Structure ofFrontiers in molecular biosciences · 2021Article
- Mutations in domain IV of elongation factor EF-G confer -1 frameshifting.RNA (New York, N.Y.) · 2021Article
- Global reprogramming of virulence and antibiotic resistance inThe Journal of biological chemistry · 2020Article
- Structural basis for ribosome recycling by RRF and tRNA.Nature structural & molecular biology · 2020Article
- Spontaneous ribosomal translocation of mRNA and tRNAs into a chimeric hybrid state.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- New Insights into Ribosome Structure and Function.Cold Spring Harbor perspectives in biology · 2019Review
- Ribosome Structure, Function, and Early Evolution.International journal of molecular sciences · 2018Review
- Ensemble and single-molecule FRET studies of protein synthesis.Methods (San Diego, Calif.) · 2018Article
- The ribosome moves: RNA mechanics and translocation.Nature structural & molecular biology · 2017Article
- Structural insights into ribosome translocation.Wiley interdisciplinary reviews. RNA · 2016Review
- Review: Translational GTPases.Biopolymers · 2016Review
- Elongation factor G initiates translocation through a power stroke.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell.Chemical reviews · 2016Review
- Article
- Structural Insights into tRNA Dynamics on the Ribosome.International journal of molecular sciences · 2015Review
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Authors and funding
5 authors.
Funding
Abstract
Previous structural studies suggested that ribosomal translocation is accompanied by large interdomain rearrangements of elongation factor G (EF-G). Here, we follow the movement of domain IV of EF-G relative to domain II of EF-G using ensemble and single-molecule Förster resonance energy transfer. Our results indicate that ribosome-free EF-G predominantly adopts a compact conformation that can also, albeit infrequently, transition into a more extended conformation in which domain IV moves away from domain II. By contrast, ribosome-bound EF-G predominantly adopts an extended conformation regardless of whether it is interacting with pretranslocation ribosomes or with posttranslocation ribosomes. Our data suggest that ribosome-bound EF-G may also occasionally sample at least one more compact conformation. GTP hydrolysis catalyzed by EF-G does not affect the relative stability of the observed conformations in ribosome-free and ribosome-bound EF-G. Our data support a model suggesting that, upon binding to a pretranslocation ribosome, EF-G moves from a compact to a more extended conformation. This transition is not coupled to but likely precedes both GTP hydrolysis and mRNA/tRNA translocation.
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