Structural basis of DNA crossover capture by Escherichia coli DNA gyrase

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 derive...

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Bibliographic Details
Published in:	Science (American Association for the Advancement of Science) Vol. 384; no. 6692; pp. 227 - 232
Main Authors:	Vayssières, Marlène, Marechal, Nils, Yun, Long, Lopez Duran, Brian, Murugasamy, Naveen Kumar, Fogg, Jonathan M, Zechiedrich, Lynn, Nadal, Marc, Lamour, Valérie
Format:	Journal Article
Language:	English
Published:	United States The American Association for the Advancement of Science 12-04-2024 American Association for the Advancement of Science (AAAS)
Subjects:	Biochemistry, Molecular Biology Cryoelectron Microscopy Deoxyribonucleic acid DNA DNA Gyrase - chemistry DNA Gyrase - metabolism DNA topoisomerase DNA Topoisomerases, Type II - metabolism DNA, Superhelical E coli Electron microscopy Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Grooves Life Sciences Structural Biology Substrates Supercoiling Torsional stress structural biology DNA topology DNA DNA topoisomerase
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Summary:	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 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.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 PMCID: PMC11108255 Author contributions: Conceptualization: J.M. F., L.Z., M.N., and V.L. Methodology: N.M., J.M.F., L.Z., M.N., and V.L. Investigation: M.V., N.M., L.Y., B.L.D., N.K.M., M.N., and V.L. Visualization: M.V., N.M., M.N., and V.L. Funding acquisition: L.Z., M.N., and V.L. Project administration: V.L. Supervision: M.N. and V.L. Writing – original draft: M.V., N.M., M.N., and V.L. Writing – review and editing: M.V., N.M., N.K.M., B.L.D., J.M.F., L.Z., M.N., and V.L.
ISSN:	0036-8075 1095-9203
DOI:	10.1126/science.adl5899