Antibiotic streptolydigin requires noncatalytic Mg2+for binding to RNA polymerase

Savva Zorov, Yulia Yuzenkova, Vadim Nikiforov, Konstantin Severinov, Nikolay Zenkin

    Research output: Contribution to journalArticlepeer-review

    6 Citations (Scopus)


    Multisubunit RNA polymerase, an enzyme that accomplishes transcription in all living organisms, is a potent target for antibiotics. 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.

    Original languageEnglish
    Pages (from-to)1420-1424
    Number of pages5
    JournalAntimicrobial Agents and Chemotherapy
    Issue number3
    Publication statusPublished - Mar 2014


    Dive into the research topics of 'Antibiotic streptolydigin requires noncatalytic Mg2+for binding to RNA polymerase'. Together they form a unique fingerprint.

    Cite this