Antimicrobial activity of fusidic acid in Escherichia coli is dependent on the relative levels of ribosome recycling factor and elongation factor G
Autor: | Shreya Ahana Ayyub, Kuldeep Lahry, Divya Dobriyal, Umesh Varshney, Sanjay Mondal |
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Rok vydání: | 2018 |
Předmět: |
Ribosomal Proteins
0301 basic medicine Fusidic acid Ribosome Recycling Factor Chromosomal translocation medicine.disease_cause Microbiology Ribosome 03 medical and health sciences chemistry.chemical_compound Escherichia coli Genetics medicine Protein biosynthesis Molecular Biology Microbiology & Cell Biology biology Escherichia coli Proteins Peptide Elongation Factor G Anti-Bacterial Agents Complementation 030104 developmental biology chemistry Biochemistry biology.protein Growth inhibition Fusidic Acid Ribosomes medicine.drug |
Zdroj: | IndraStra Global. |
ISSN: | 2381-3652 |
Popis: | During protein synthesis, elongation factor G (EFG) participates at the steps of translocation and ribosome recycling. Fusidic acid (FA) is a bacteriostatic antibiotic, which traps EFG on ribosomes, stalling them on mRNAs. How the bacterial susceptibility to FA is determined, and which of the two functions of EFG (translocation or ribosome recycling) is more vulnerable, has remained debatable. The in vivo studies addressing these aspects of FA mediated inhibition of protein synthesis are lacking. Here, we used a system of Escherichia coli strains and their complementation/supplementation with the plasmid borne copies of the inducible versions of EFG and ribosome recycling factor (RRF) genes. Additionally, we investigated FA sensitivity in a strain with increased proportion of stalled ribosomes. We show that the cells with high EFG/RRF (or low RRF/EFG) ratios are more susceptible to FA than those with low EFG/RRF (or high RRF/EFG) ratios. Our in vivo observations are consistent with the recent in vitro reports of dependence of FA susceptibility on EFG/RRF ratios, and the notion that an overriding target of FA is the translocation function of EFG. An applied outcome of our in vivo study is that FA mediated growth inhibition could be facilitated by depletion or inactivation of cellular RRF. |
Databáze: | OpenAIRE |
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