ArticleBBA advances2023
Translation factor accelerating peptide bond formation on the ribosome: EF-P and eIF5A as entropic catalysts and a potential drug targets.
Article in BBA advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 13 citations in OpenAlex.
- Translation factors that keep the ribosome Pro-active.Microbiology and molecular biology reviews : MMBR · 2026Review
- The Alteromonas macleodii ribosome enables consecutive incorporation of bulky D-amino acids into peptides.Nucleic acids research · 2026Article
- Harnessing Microalgae as Sustainable Cell Factories for Polyamine-Based Nanosilica for Biomedical Applications.Molecules (Basel, Switzerland) · 2025Review
- Girolline is a sequence context-selective modulator of eIF5A activity.Nature communications · 2025Article
- Development of a reliable, sensitive, and convenient assay for the discovery of new eIF5A hypusination inhibitors.PloS one · 2025Article
- EF-P and its paralog EfpL (YeiP) differentially control translation of proline-containing sequences.Nature communications · 2024Article
- Kinetic mechanism and determinants of EF-P recruitment to translating ribosomes.Nucleic acids research · 2024Article
- The crosstalk between metabolism and translation.Cell metabolism · 2024Review
- DHPS-Mediated Hypusination Regulates METTL3 Self-m6A-Methylation Modification to Promote Melanoma Proliferation and the Development of Novel Inhibitors.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Engineering tRNAs for the Ribosomal Translation of Non-proteinogenic Monomers.Chemical reviews · 2024Review
- The Structural and Molecular Mechanisms ofMolecules (Basel, Switzerland) · 2024Review
- Ukrainian science in the context of its anticolonial struggle.BBA advances · 2023Article
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Authors and funding
3 authors at 1 institution.
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No grant is acknowledged in the PubMed record.
Abstract
Elongation factor P (EF-P) and its eukaryotic homolog eIF5A are auxiliary translation factors that facilitate peptide bond formation when several sequential proline (Pro) residues are incorporated into the nascent chain. EF-P and eIF5A bind to the exit (E) site of the ribosome and contribute to favorable entropy of the reaction by stabilizing tRNA binding in the peptidyl transferase center of the ribosome. In most organisms, EF-P and eIF5A carry a posttranslational modification that is crucial for catalysis. The chemical nature of the modification varies between different groups of bacteria and between pro- and eukaryotes, making the EF-P-modification enzymes promising targets for antibiotic development. In this review, we summarize our knowledge of the structure and function of EF-P and eIF5A, describe their modification enzymes, and present an approach for potential drug screening aimed at EarP, an enzyme that is essential for EF-P modification in several pathogenic bacteria.
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