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Single-nucleotide-resolution mapping of DNA gyrase cleavage sites across the Escherichia coli genomeстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 17 апреля 2024 г.
- Авторы: Sutormin D., Rubanova N., Logacheva M., Ghilarov D., Severinov K.
- Журнал: Nucleic Acids Research
- Том: 47
- Номер: 3
- Год издания: 2019
- Издательство: Oxford University Press
- Местоположение издательства: United Kingdom
- Первая страница: 1373
- Последняя страница: 1388
- DOI: 10.1093/nar/gky1222
- Аннотация: An important antibiotic target, DNA gyrase is an essential bacterial enzyme that introduces negative supercoils into DNA and relaxes positive supercoils accumulating in front of moving DNA and RNA polymerases. By altering the superhelical density, gyrase may regulate expression of bacterial genes. The information about how gyrase is distributed along genomic DNA and whether its distribution is affected by drugs is scarce. During catalysis, gyrase cleaves both DNA strands forming a covalently bound intermediate. By exploiting the ability of several topoisomerase poisons to stabilize this intermediate we developed a ChIP-Seq-based approach to locate, with single nucleotide resolution, DNA gyrase cleavage sites (GCSs) throughout the Escherichia coli genome. We identified an extended gyrase binding motif with phased 10-bp G/C content variation, indicating that bending ability of DNA contributes to gyrase binding. We also found that GCSs are enriched in extended regions located downstream of highly transcribed operons. Transcription inhibition leads to redistribution of gyrase suggesting that the enrichment is functionally significant. Our method can be applied for precise mapping of prokaryotic and eukaryotic type II topoisomerases cleavage sites in a variety of organisms and paves the way for future studies of various topoisomerase inhibitors.
- Добавил в систему: Сутормин Дмитрий Александрович