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The antibiotic streptolydigin inhibits RNA polymerase by sequestering the active center in a catalytically inactive conformation. Here, we show that binding of streptolydigin to RNA polymerase strictly depends on a noncatalytic magnesium ion which is likely chelated by the aspartate of the bridge helix of the active center. Substitutions of this aspartate may explain different sensitivities of bacterial RNA polymerases to streptolydigin. These results provide the first evidence for the role of noncatalytic magnesium ions in the functioning of RNA polymerase and suggest new routes for the modification of existing and the design of new inhibitors of transcription.<\/jats:p>","DOI":"10.1128\/aac.02248-13","type":"journal-article","created":{"date-parts":[[2013,12,17]],"date-time":"2013-12-17T02:23:13Z","timestamp":1387246993000},"page":"1420-1424","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":12,"title":["Antibiotic Streptolydigin Requires Noncatalytic Mg\n            <sup>2+<\/sup>\n            for Binding to RNA Polymerase"],"prefix":"10.1128","volume":"58","author":[{"given":"Savva","family":"Zorov","sequence":"first","affiliation":[{"name":"Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, United Kingdom"},{"name":"Waksman Institute, Rutgers, the State University of New 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