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Histidine-Triad Hydrolases Provide Resistance to Peptide-Nucleotide Antibioticsстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 2 сентября 2020 г.
- Авторы: Yagmurov Eldar, Tsibulskaya Darya, Livenskyi Alexey, Serebryakova Marina, Wolf Yury I., Borukhov Sergei, Severinov Konstantin, Dubiley Svetlana
- Журнал: mBio
- Том: 11
- Номер: 2
- Год издания: 2020
- Издательство: American Society for Microbiology
- Местоположение издательства: United States
- Первая страница: e00497-20
- DOI: 10.1128/mbio.00497-20
- Аннотация: The Escherichia coli microcin C (McC) and related compounds are potent Trojan horse peptide-nucleotide antibiotics. The peptide part facilitates transport into sensitive cells. Inside the cell, the peptide part is degraded by nonspecific peptidases releasing an aspartamide-adenylate containing a phosphoramide bond. This nonhydrolyzable compound inhibits aspartyl-tRNA synthetase. In addition to the efficient export of McC outside the producing cells, special mechanisms have evolved to avoid self-toxicity caused by the degradation of the peptide part inside the producers. Here, we report that histidine-triad (HIT) hydrolases encoded in biosynthetic clusters of some McC homologs or by standalone genes confer resistance to McC-like compounds by hydrolyzing the phosphoramide bond in toxic aspartamide-adenosine, rendering them inactive.IMPORTANCE Uncovering the mechanisms of resistance is a required step for countering the looming antibiotic resistance crisis. In this communication, we show how universally conserved histidine-triad hydrolases provide resistance to microcin C, a potent inhibitor of bacterial protein synthesis.
- Добавил в систему: Серебрякова Марина Васильевна