ArticleProceedings of the National Academy of Sciences of the United States of America2014
Following movement of domain IV of elongation factor G during ribosomal translocation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 44 citations in OpenAlex.
- Life is chemistry plus information.BBA advances · 2025Article
- Interplay between Inter-Subunit Rotation of the Ribosome and Binding of Translational GTPases.International journal of molecular sciences · 2023Article
- The role of GTP hydrolysis by EF-G in ribosomal translocation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A Single Amino Acid Substitution in Elongation Factor G Can Confer Low-Level Gentamicin Resistance inAntimicrobial agents and chemotherapy · 2022Article
- Time-resolved cryo-EM visualizes ribosomal translocation with EF-G and GTP.Nature communications · 2021Article
- Optimization of a fluorescent-mRNA based real-time assay for precise kinetic measurements of ribosomal translocation.RNA biology · 2021Article
- The energetics of subunit rotation in the ribosome.Biophysical reviews · 2021Review
- Perturbation of ribosomal subunit dynamics by inhibitors of tRNA translocation.RNA (New York, N.Y.) · 2021Article
- Ribosome as a Translocase and Helicase.Biochemistry. Biokhimiia · 2021Review
- Mutations in domain IV of elongation factor EF-G confer -1 frameshifting.RNA (New York, N.Y.) · 2021Article
- Clinical and molecular findings in a family expressing a novel heterozygous variant of the G elongation factor mitochondrial 1 gene.Experimental and therapeutic medicine · 2020Article
- Observation of preQRNA biology · 2019Article
- 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
- mRNAs and lncRNAs intrinsically form secondary structures with short end-to-end distances.Nature communications · 2018Article
- The structure of an elongation factor G-ribosome complex captured in the absence of inhibitors.Nucleic acids research · 2018Article
- Ensemble and single-molecule FRET studies of protein synthesis.Methods (San Diego, Calif.) · 2018Article
- Similarity and diversity of translational GTPase factors EF-G, EF4, and BipA: From structure to function.RNA biology · 2016Review
- Structural insights into ribosome translocation.Wiley interdisciplinary reviews. RNA · 2016Review
- Elongation factor G initiates translocation through a power stroke.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- EF-G Activation by Phosphate Analogs.Journal of molecular biology · 2016Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Translocation of mRNA and tRNAs through the ribosome is catalyzed by a universally conserved elongation factor (EF-G in prokaryotes and EF-2 in eukaryotes). Previous studies have suggested that ribosome-bound EF-G undergoes significant structural rearrangements. Here, we follow the movement of domain IV of EF-G, which is critical for the catalysis of translocation, relative to protein S12 of the small ribosomal subunit using single-molecule FRET. We show that ribosome-bound EF-G adopts distinct conformations corresponding to the pre- and posttranslocation states of the ribosome. Our results suggest that, upon ribosomal translocation, domain IV of EF-G moves toward the A site of the small ribosomal subunit and facilitates the movement of peptidyl-tRNA from the A to the P site. We found no evidence of direct coupling between the observed movement of domain IV of EF-G and GTP hydrolysis. In addition, our results suggest that the pretranslocation conformation of the EF-G-ribosome complex is significantly less stable than the posttranslocation conformation. Hence, the structural rearrangement of EF-G makes a considerable energetic contribution to promoting tRNA translocation.
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