Structural basis of DNA crossover capture by Escherichia coli DNA gyrase

• 成果类型: Article
• 署名作者: Vayssieres, Marlene; Marechal, Nils; Yun, Long; Duran, Brian Lopez; Murugasamy, Naveen Kumar; Fogg, Jonathan M.; Zechiedrich, Lynn; Nadal, Marc; Lamour, Valerie
• 署名单位: Universites de Strasbourg Etablissements Associes; Universite de Strasbourg; Centre National de la Recherche Scientifique (CNRS); CNRS - National Institute for Biology (INSB); Institut National de la Sante et de la Recherche Medicale (Inserm); Institut National de la Sante et de la Recherche Medicale (Inserm); Institut National de la Sante et de la Recherche Medicale (Inserm); Universite PSL; Ecole Normale Superieure (ENS); Centre National de la Recherche Scientifique (CNRS); Baylor College of Medicine; Baylor College of Medicine; Universite Paris Cite; Universites de Strasbourg Etablissements Associes; Universite de Strasbourg; CHU Strasbourg
• 刊物名称: SCIENCE
• ISSN/ISSBN: 0036-8167
• DOI: 10.1126/science.adl5899
• 发表日期: 2024-04-12
• 页码: 227-232
• 关键词: positively supercoiled dna; c-terminal domain; cryo-em; single-molecule; preferential relaxation; topoisomerase-iv; electron; TOPOLOGY; mechanism; RECOGNITION

摘要

DNA supercoiling must be precisely regulated by topoisomerases to prevent DNA entanglement. The interaction of type IIA DNA topoisomerases with two DNA molecules, enabling the transport of one duplex through the transient double-stranded break of the other, remains elusive owing to structures derived solely from single linear duplex DNAs lacking topological constraints. Using cryo-electron microscopy, we solved the structure of Escherichia coli DNA gyrase bound to a negatively supercoiled minicircle DNA. We show how DNA gyrase captures a DNA crossover, revealing both conserved molecular grooves that accommodate the DNA helices. Together with molecular tweezer experiments, the structure shows that the DNA crossover is of positive chirality, reconciling the binding step of gyrase-mediated DNA relaxation and supercoiling in a single structure.