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Here we employ fast kinetics to reveal the molecular mechanism of action of a clinically used, new-generation, semisynthetic aminoglycoside Arbekacin (ABK), which is designed to avoid enzyme-mediated deactivation common to other aminoglycosides. Our results portray complete picture of ABK inhibition of bacterial translation with precise quantitative characterizations. We find that ABK inhibits different steps of translation in nanomolar to micromolar concentrations by imparting pleotropic effects. ABK binding stalls elongating ribosomes to a state, which is unfavorable for EF-G binding. This prolongs individual translocation step from \u223c50 ms to at least 2 s; the mean time of translocation increases inversely with EF-G concentration. ABK also inhibits translation termination by obstructing RF1\/RF2 binding to the ribosome. Furthermore, ABK decreases accuracy of mRNA decoding (UUC vs. CUC)\u00a0by \u223c80 000 fold, causing aberrant protein production. Importantly, translocation and termination events cannot be completely stopped even with high ABK concentration. Extrapolating our kinetic model of ABK action, we postulate that aminoglycosides impose bacteriostatic effect mainly by inhibiting translocation, while they become bactericidal in combination with decoding errors.<\/jats:p>","DOI":"10.1093\/nar\/gkab495","type":"journal-article","created":{"date-parts":[[2021,5,26]],"date-time":"2021-05-26T11:27:33Z","timestamp":1622028453000},"page":"6880-6892","source":"Crossref","is-referenced-by-count":21,"title":["Mechanistic insights into translation inhibition by aminoglycoside antibiotic arbekacin"],"prefix":"10.1093","volume":"49","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3228-9908","authenticated-orcid":false,"given":"Narayan\u00a0Prasad","family":"Parajuli","sequence":"first","affiliation":[{"name":"Department of Cell and Molecular Biology, Biomedical Center, Uppsala University, SE-75124\u00a0Uppsala, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3028-3270","authenticated-orcid":false,"given":"Chandra\u00a0Sekhar","family":"Mandava","sequence":"additional","affiliation":[{"name":"Department of Cell and Molecular Biology, Biomedical Center, Uppsala University, SE-75124\u00a0Uppsala, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3794-1870","authenticated-orcid":false,"given":"Michael\u00a0Y","family":"Pavlov","sequence":"additional","affiliation":[{"name":"Department of Cell and Molecular Biology, Biomedical Center, Uppsala University, SE-75124\u00a0Uppsala, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7124-792X","authenticated-orcid":false,"given":"Suparna","family":"Sanyal","sequence":"additional","affiliation":[{"name":"Department of Cell and Molecular Biology, Biomedical Center, Uppsala University, SE-75124\u00a0Uppsala, Sweden"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2021,6,14]]},"reference":[{"key":"2021070901254914500_B1","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1038\/nrmicro1265","article-title":"The bacterial ribosome as a target for antibiotics","volume":"3","author":"Poehlsgaard","year":"2005","journal-title":"Nat. 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Biol."},{"key":"2021070901254914500_B48","doi-asserted-by":"crossref","first-page":"13744","DOI":"10.1073\/pnas.1610917113","article-title":"Two proofreading steps amplify the accuracy of genetic code translation","volume":"113","author":"Ieong","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021070901254914500_B49","doi-asserted-by":"crossref","first-page":"3440","DOI":"10.1074\/jbc.M114.611608","article-title":"Fusidic acid targets elongation factor G in several stages of translocation on the bacterial ribosome","volume":"290","author":"Borg","year":"2015","journal-title":"J. Biol. 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Biol."},{"key":"2021070901254914500_B55","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1006\/abbi.1996.0136","article-title":"Rate of translation of natural mRNAs in an optimized in vitro system","volume":"328","author":"Pavlov","year":"1996","journal-title":"Arch. Biochem. Biophys."},{"key":"2021070901254914500_B56","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1042\/bj1600185","article-title":"Polypeptide-chain-elongation rate in Escherichia coli B\/r as a function of growth rate","volume":"160","author":"Young","year":"1976","journal-title":"Biochem. J."},{"key":"2021070901254914500_B57","doi-asserted-by":"crossref","first-page":"316","DOI":"10.1128\/mr.55.2.316-333.1991","article-title":"Growth rate of Escherichia coli","volume":"55","author":"Marr","year":"1991","journal-title":"Microbiol Rev"},{"key":"2021070901254914500_B58","doi-asserted-by":"crossref","first-page":"1830","DOI":"10.1038\/s41467-021-21942-6","article-title":"Translation error clusters induced by aminoglycoside antibiotics","volume":"12","author":"Wohlgemuth","year":"2021","journal-title":"Nat. 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