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Updated: Aug 2, 2025
Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses
Published on: February 25, 2011
Translation factor accelerating peptide bond formation on the ribosome: EF-P and eIF5A as entropic catalysts and a
Vitalii Mudryi1, Frank Peske1, Marina Rodnina1
1Department of Physical Biochemistry, Max Planck Institute for Multidisciplinary Sciences, 37077 Goettingen, Germany.
Insights
Elongation factor P (EF-P) and eIF5A are crucial translation factors. Their unique modifications offer promising targets for developing novel antibiotics against pathogenic bacteria.
Area of Science:
- Molecular Biology
- Biochemistry
- Microbiology
Background:
- Elongation factor P (EF-P) and eukaryotic eIF5A are essential translation factors.
- They facilitate peptide bond formation, particularly during proline-rich sequence synthesis.
- These factors bind the ribosomal exit site, stabilizing tRNA in the peptidyl transferase center.
Purpose of the Study:
- To review the structure and function of EF-P and eIF5A.
- To describe the enzymes responsible for their crucial posttranslational modifications.
- To present a drug screening strategy targeting EF-P modification enzymes.
Main Methods:
- Literature review on EF-P and eIF5A structure-function.
- Analysis of EF-P/eIF5A modification pathways across organisms.
- Proposal of a drug screening approach for bacterial EF-P modification enzymes.
Main Results:
- EF-P and eIF5A require specific posttranslational modifications for activity.
- Modification strategies differ between bacteria and eukaryotes.
- EF-P modification enzymes are potential antibiotic targets.
Conclusions:
- The diverse modifications of EF-P/eIF5A present unique opportunities for antimicrobial drug development.
- Targeting enzymes like EarP, essential for EF-P modification in pathogens, is a viable strategy.
- Understanding these factors and their modifications is key to novel therapeutic interventions.
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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