ArticleNature structural & molecular biology2016
EF4 disengages the peptidyl-tRNA CCA end and facilitates back-translocation on the 70S ribosome.
Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 24 citations in OpenAlex.
- Emerging mechanisms of human mitochondrial translation regulation.Trends in biochemical sciences · 2025Review
- Interplay between Inter-Subunit Rotation of the Ribosome and Binding of Translational GTPases.International journal of molecular sciences · 2023Article
- Hyper-swivel head domain motions are required for complete mRNA-tRNA translocation and ribosome resetting.Nucleic acids research · 2022Article
- Translational Control of COVID-19 and Its Therapeutic Implication.Frontiers in immunology · 2022Review
- Mitochondrial Protein Translation: Emerging Roles and Clinical Significance in Disease.Frontiers in cell and developmental biology · 2021Review
- The conserved translation factor LepA is required for optimal synthesis of a porin family inJournal of bacteriology · 2020Article
- Co-temporal Force and Fluorescence Measurements Reveal a Ribosomal Gear Shift Mechanism of Translation Regulation by Structured mRNAs.Molecular cell · 2019Article
- Translation Elongation Factor 4 (LepA) Contributes to Tetracycline Susceptibility by Stalling Elongating Ribosomes.Antimicrobial agents and chemotherapy · 2018Article
- Eukaryotic translation elongation factor 2 (eEF2) catalyzes reverse translocation of the eukaryotic ribosome.The Journal of biological chemistry · 2018Article
- Taking a Step Back from Back-Translocation: an Integrative View of LepA/EF4's Cellular Function.Molecular and cellular biology · 2017Review
- Conserved GTPase LepA (Elongation Factor 4) functions in biogenesis of the 30S subunit of the 70S ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Similarity and diversity of translational GTPase factors EF-G, EF4, and BipA: From structure to function.RNA biology · 2016Review
- EF4 reveals the energy barrier for tRNA back-translocation in the peptidyl transferase center.RNA biology · 2016Article
- Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome.The Journal of biological chemistry · 2016Article
- Step back for seminal translation.Nature structural & molecular biology · 2016Article
- Elongation factor 4 remodels the A-site tRNA on the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Mammalian elongation factor 4 regulates mitochondrial translation essential for spermatogenesis.Nature structural & molecular biology · 2016Article
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
EF4 catalyzes tRNA back-translocation through an unknown mechanism. We report cryo-EM structures of Escherichia coli EF4 in post- and pretranslocational ribosomes (Post- and Pre-EF4) at 3.7- and 3.2-Å resolution, respectively. In Post-EF4, peptidyl-tRNA occupies the peptidyl (P) site, but the interaction between its CCA end and the P loop is disrupted. In Pre-EF4, the peptidyl-tRNA assumes a unique position near the aminoacyl (A) site, denoted the A site/EF4 bound (A/4) site, with a large displacement at its acceptor arm. Mutagenesis analyses suggest that a specific region in the EF4 C-terminal domain (CTD) interferes with base-pairing between the peptidyl-tRNA 3'-CCA and the P loop, whereas the EF4 CTD enhances peptidyl-tRNA interaction at the A/4 site. Therefore, EF4 induces back-translocation by disengaging the tRNA's CCA end from the peptidyl transferase center of the translating ribosome.
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