ArticleThe Journal of biological chemistry2011
A central interdomain protein joint in elongation factor G regulates antibiotic sensitivity, GTP hydrolysis, and ribosome translocation.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- Structural insights into mammalian mitochondrial translation elongation catalyzed by mtEFG1.The EMBO journal · 2020Article
- A target-protection mechanism of antibiotic resistance at atomic resolution: insights into FusB-type fusidic acid resistance.Scientific reports · 2016Article
- A conserved histidine in switch-II of EF-G moderates release of inorganic phosphate.Scientific reports · 2015Article
- Control of ribosomal subunit rotation by elongation factor G.Science (New York, N.Y.) · 2013Article
- Mechanism of elongation factor-G-mediated fusidic acid resistance and fitness compensation in Staphylococcus aureus.The Journal of biological chemistry · 2012Article
- ppGpp inhibits peptide elongation cycle of chloroplast translation system in vitro.Plant molecular biology · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The antibiotic fusidic acid potently inhibits bacterial translation (and cellular growth) by lodging between domains I and III of elongation factor G (EF-G) and preventing release of EF-G from the ribosome. We examined the functions of key amino acid residues near the active site of EF-G that interact with fusidic acid and regulate hydrolysis of GTP. Alanine mutants of these residues spontaneously hydrolyzed GTP in solution, bypassing the normal activating role of the ribosome. A conserved phenylalanine in the switch II element of EF-G was important for suppressing GTP hydrolysis in solution and critical for catalyzing translocation of the ribosome along mRNA. These experimental results reveal the multipurpose roles of an interdomain joint in the heart of an essential translation factor that can both promote and inhibit bacterial translation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.