ArticleNucleic acids research2015
New insights into the enzymatic role of EF-G in ribosome recycling.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Unlocking Enhanced Efficacy of Aminoglycoside Antibiotics Against Pseudomonas aeruginosa.Microbial biotechnology · 2025Review
- Illuminating mitochondrial translation through mouse models.Human molecular genetics · 2024Review
- An Amino Acid Substitution in Elongation Factor EF-G1A Alters the Antibiotic Susceptibility of Pseudomonas aeruginosa LasR-Null Mutants.Journal of bacteriology · 2023Article
- Transcription regulates ribosome hibernation.Molecular microbiology · 2021Article
- Distinct mechanisms of the human mitoribosome recycling and antibiotic resistance.Nature communications · 2021Article
- Multifaceted Mechanism of Amicoumacin A Inhibition of Bacterial Translation.Frontiers in microbiology · 2021Article
- Mutations in GeneAntimicrobial agents and chemotherapy · 2018Article
- Novel GFM2 variants associated with early-onset neurological presentations of mitochondrial disease and impaired expression of OXPHOS subunits.Neurogenetics · 2017Article
- A Possible Role of the Full-Length Nascent Protein in Post-Translational Ribosome Recycling.PloS one · 2017Article
- A pseudouridylation switch in rRNA is implicated in ribosome function during the life cycle of Trypanosoma brucei.Scientific reports · 2016Article
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During translation, elongation factor G (EF-G) plays a catalytic role in tRNA translocation and a facilitative role in ribosome recycling. By stabilizing the rotated ribosome and interacting with ribosome recycling factor (RRF), EF-G was hypothesized to induce the domain rotations of RRF, which subsequently performs the function of splitting the major intersubunit bridges and thus separates the ribosome into subunits for recycling. Here, with systematic mutagenesis, FRET analysis and cryo-EM single particle approach, we analyzed the interplay between EF-G/RRF and post termination complex (PoTC). Our data reveal that the two conserved loops (loop I and II) at the tip region of EF-G domain IV possess distinct roles in tRNA translocation and ribosome recycling. Specifically, loop II might be directly involved in disrupting the main intersubunit bridge B2a between helix 44 (h44 from the 30S subunit) and helix 69 (H69 from the 50S subunit) in PoTC. Therefore, our data suggest a new ribosome recycling mechanism which requires an active involvement of EF-G. In addition to supporting RRF, EF-G plays an enzymatic role in destabilizing B2a via its loop II.
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