Antibiotic Streptolydigin Requires Noncatalytic Mg2+ for Binding to RNA Polymeraseстатья
Статья опубликована в высокорейтинговом журнале
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Дата последнего поиска статьи во внешних источниках: 2 мая 2014 г.
Аннотация: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.