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dc.rights.licenseopenen_US
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorROSA, Leonardo Talachia
dc.contributor.authorVERNHES, Émeline
dc.contributor.authorSOULET, Anne-Lise
dc.contributor.authorPOLARD, Patrice
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorFRONZES, Rémi
dc.date.accessioned2024-11-05T12:40:28Z
dc.date.available2024-11-05T12:40:28Z
dc.date.issued2024-10-18
dc.identifier.issn1460-2075en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/203122
dc.description.abstractEnSome DNA helicases play central and specific roles in genome maintenance and plasticity through their branch migration activity in different pathways of homologous recombination. RadA is a highly conserved bacterial helicase involved in DNA repair throughout all bacterial species. In Gram-positive Firmicutes, it also has a role in natural transformation, while in Gram-negative bacteria, ComM is the canonical transformation-specific helicase. Both RadA and ComM helicases form hexameric rings and use ATP hydrolysis as an energy source to propel themselves along DNA. In this study, we present the cryoEM structures of RadA and ComM interacting with DNA and ATP analogs. These structures reveal important molecular interactions that couple ATP hydrolysis and DNA binding in RadA, as well as the role of the Lon protease-like domain, shared by RadA and ComM, in this process. Taken together, these results provide new molecular insights into the mechanisms of DNA branch migration in different pathways of homologous recombination.
dc.language.isoENen_US
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.subject.enDNA Recombination; Helicase; DNA Translocation; Bacterial Transformation
dc.title.enStructural insights into the mechanism of DNA branch migration during homologous recombination in bacteria.
dc.title.alternativeEMBO Jen_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1038/s44318-024-00264-5en_US
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologieen_US
dc.identifier.pubmed39424952en_US
bordeaux.journalEMBO Journalen_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
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hal.popularnonen_US
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dc.rights.ccPas de Licence CCen_US
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