ROSA, Leonardo Talachia; VERNHES, Émeline; SOULET, Anne-Lise; POLARD, Patrice; FRONZES, Rémi

doi:10.1038/s44318-024-00264-5

ROSA, Leonardo Talachia
Microbiologie Fondamentale et Pathogénicité [MFP]

VERNHES, Émeline

SOULET, Anne-Lise

Langue

Article de revue

Ce document a été publié dans

EMBO Journal. 2024-10-18

Résumé en anglais

Some 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.< Réduire

Mots clés en anglais

DNA Recombination; Helicase; DNA Translocation; Bacterial Transformation

URI

https://oskar-bordeaux.fr/handle/20.500.12278/203122

DOI

http://dx.doi.org/10.1038/s44318-024-00264-5

Unités de recherche

MFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234

Voir/Ouvrir

Métadonnées

Partager cette publication !

Licence d’utilisation du document

Structural insights into the mechanism of DNA branch migration during homologous recombination in bacteria.

Langue

Ce document a été publié dans

Résumé en anglais

Mots clés en anglais

URI

DOI

Unités de recherche