ArticleThe EMBO journal2012
Structural insights into initial and intermediate steps of the ribosome-recycling process.
Article in The EMBO journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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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
33 citing papers in PubMed, 54 citations in OpenAlex.
- Structural characterization of ribosome recycling and fusidic acid inhibition in Staphylococcus aureus.Nucleic acids research · 2026Article
- Mechanisms of fusidic acid resistance.Biochemical Society transactions · 2025Review
- Multifaceted roles of mycobacterial HflX: ribosome splitting, rRNA disordering, and drug resistance.Biochemical Society transactions · 2025Article
- HflX-mediated drug resistance through ribosome splitting and rRNA disordering in mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Drug resistance through ribosome splitting and rRNA disordering in mycobacteria.bioRxiv : the preprint server for biology · 2024Article
- Starvation sensing by mycobacterial RelA/SpoT homologue through constitutive surveillance of translation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Role of ribosome recycling factor in natural termination and translational coupling as a ribosome releasing factor.PloS one · 2023Article
- Recollection of How We Came Across the Protein Modification with Amino Acids by Aminoacyl tRNA-Protein Transferase.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Mechanisms of ribosome recycling in bacteria and mitochondria: a structural perspective.RNA biology · 2022Review
- Distinct mechanisms of the human mitoribosome recycling and antibiotic resistance.Nature communications · 2021Article
- In silico analysis of bacterial translation factors reveal distinct translation event specific pI values.BMC genomics · 2021Article
- Alternative conformations and motions adopted by 30S ribosomal subunits visualized by cryo-electron microscopy.RNA (New York, N.Y.) · 2020Article
- Structural basis for ribosome recycling by RRF and tRNA.Nature structural & molecular biology · 2020Article
- The Origin and Evolution of Release Factors: Implications for Translation Termination, Ribosome Rescue, and Quality Control Pathways.International journal of molecular sciences · 2019Review
- Structural insights into unique features of the human mitochondrial ribosome recycling.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The kinetic mechanism of bacterial ribosome recycling.Nucleic acids research · 2017Article
- In-Culture Cross-Linking of Bacterial Cells Reveals Large-Scale Dynamic Protein-Protein Interactions at the Peptide Level.Journal of proteome research · 2017Article
- Article
- Key Intermediates in Ribosome Recycling Visualized by Time-Resolved Cryoelectron Microscopy.Structure (London, England : 1993) · 2016Article
- Ribosome recycling defects modify the balance between the synthesis and assembly of specific subunits of the oxidative phosphorylation complexes in yeast mitochondria.Nucleic acids research · 2016Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
The ribosome-recycling factor (RRF) and elongation factor-G (EF-G) disassemble the 70S post-termination complex (PoTC) into mRNA, tRNA, and two ribosomal subunits. We have determined cryo-electron microscopic structures of the PoTC·RRF complex, with and without EF-G. We find that domain II of RRF initially interacts with universally conserved residues of the 23S rRNA helices 43 and 95, and protein L11 within the 50S ribosomal subunit. Upon EF-G binding, both RRF and tRNA are driven towards the tRNA-exit (E) site, with a large rotational movement of domain II of RRF towards the 30S ribosomal subunit. During this intermediate step of the recycling process, domain II of RRF and domain IV of EF-G adopt hitherto unknown conformations. Furthermore, binding of EF-G to the PoTC·RRF complex reverts the ribosome from ratcheted to unratcheted state. These results suggest that (i) the ribosomal intersubunit reorganizations upon RRF binding and subsequent EF-G binding could be instrumental in destabilizing the PoTC and (ii) the modes of action of EF-G during tRNA translocation and ribosome-recycling steps are markedly different.
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Registered trials
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.