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Antibiotic streptolydigin requires noncatalytic Mg2+ for binding to RNA polymerase.

Authors
  • Zorov, Savva
  • Yuzenkova, Yulia
  • Nikiforov, Vadim
  • Severinov, Konstantin
  • Zenkin, Nikolay
Type
Published Article
Journal
Antimicrobial Agents and Chemotherapy
Publisher
American Society for Microbiology
Publication Date
Jan 01, 2014
Volume
58
Issue
3
Pages
1420–1424
Identifiers
DOI: 10.1128/AAC.02248-13
PMID: 24342645
Source
Medline
License
Unknown

Abstract

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.

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