Structural insights into the mechanism of DNA branch migration during homologous recombination in bacteria
Year: 2024
Type: article
Abstract: 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.
Source: The EMBO Journal
Institutions: Centre National de la Recherche Scientifique, Université de Bordeaux, Universidade Estadual de Campinas (UNICAMP), Institut Européen de Chimie et Biologie, Laboratoire de Microbiologie Fondamentale et Pathogénicité, Université Toulouse III - Paul Sabatier, Institut National des Sciences Appliquées de Toulouse, Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement, Laboratoire de Microbiologie et Génétique Moléculaires, Université de Toulouse, Centre de Biologie Intégrative de Toulouse
Language: English
Topic: DNA Repair Mechanisms
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $6,890
OpenAlex ID: W4403514935
