2026-06-28T10:14:18Zhttps://docta.ucm.es/rest/oai/request

oai:docta.ucm.es:20.500.14352/1004442024-02-14T01:06:28Zcom_20.500.14352_14col_20.500.14352_15

00925njm 22002777a 4500 dc Loot, Celine author Parissi, Vincent author Nivina, Aleksandra author Bouchier, Christiane author Mazel, Didier author Escudero García-Calderón, José Antonio author 2016-03-10 Tyrosine (Y)-recombinases have evolved to deliver mechanistically different reactions on a variety of substrates, but these evolutionary transitions are poorly understood. Among them, integron integrases are hybrid systems recombining single- and double-stranded DNA partners. These reactions are asymmetric and need a replicative resolution pathway, an exception to the canonical second strand exchange model of Y-recombinases. Integron integrases possess a specific domain for this specialized pathway. Here we show that despite this, integrases are still capable of efficiently operating the ancestral second strand exchange in symmetrical reactions between double-stranded substrates. During these reactions, both strands are reactive and Holliday junction resolution can follow either pathway. A novel deep-sequencing approach allows mapping of the crossover point for the second strand exchange. The persistence of the ancestral activity in integrases illustrates their robustness and shows that innovation towards new recombination substrates and resolution pathways was a smooth evolutionary process. 10.1038/ncomms10937 https://hdl.handle.net/20.500.14352/100444 2041-1723 https://www.nature.com/articles/ncomms10937 26961432 Unmasking the ancestral activity of integron integrases reveals a smooth evolutionary transition during functional innovation