2026-04-13T05:51:42Zhttps://recercat.cat/oai/request

oai:recercat.cat:2445/1260232025-12-04T21:12:09Zcom_2072_1057col_2072_478781col_2072_478908col_2072_478917

00925njm 22002777a 4500 dc Pluta, Radoslaw author Boer, Roeland author Lorenzo Díaz, Fabián author Russi, Silvia author Gómez, Hansel author Fernández López, Cris author Pérez Luque, Rosa author Orozco López, Modesto author Espinosa, Manuel author Coll, Miquel author 2018-11-12T17:02:53Z 2018-11-12T17:02:53Z 2017-07-24 2018-11-07T09:11:41Z Relaxases are metal-dependent nucleases that break and join DNA for the initiation and completion of conjugative bacterial gene transfer. Conjugation is the main process through which antibiotic resistance spreads among bacteria, with multidrug-resistant staphylococci and streptococci infections posing major threats to human health. The MOBV family of relaxases accounts for approximately 85% of all relaxases found in Staphylococcus aureus isolates. Here, we present six structures of the MOBV relaxase MobM from the promiscuous plasmid pMV158 in complex with several origin of transfer DNA fragments. A combined structural, biochemical, and computational approach reveals that MobM follows a previously uncharacterized histidine/metal-dependent DNA processing mechanism, which involves the formation of a covalent phosphoramidate histidine-DNA adduct for cell-to-cell transfer. We discuss how the chemical features of the high-energy phosphorus-nitrogen bond shape the dominant position of MOBV histidine relaxases among small promiscuous plasmids and their preference toward Gram-positive bacteria. Resistència als medicaments ADN Drug resistance DNA Structural basis of a histidine-DNA nicking/joining mechanism for gene transfer and promiscuous spread of antibiotic resistance