ESCUDERO, Jose Antonio; LOOT, Celine; PARISSI, Vincent; NIVINA, Aleksandra; BOUCHIER, Christiane; MAZEL, Didier

doi:10.1038/ncomms10937

Microbiologie Fondamentale et Pathogénicité [MFP]

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Article de revue

Ce document a été publié dans

2016-03-10, vol. 7, p. Article number 10937

Nature Publishing Group

Résumé en anglais

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.< Réduire

Mots clés en anglais

Biological sciences

Molecular biology

URI

https://oskar-bordeaux.fr/handle/20.500.12278/183269

DOI

http://dx.doi.org/10.1038/ncomms10937

Projet Européen

Evolution and Transfer of Antibiotic Resistance
The Integron Cassette Dynamics and the Integrase Gene Expression

Project ANR

Integrative Biology of Emerging Infectious Diseases - ANR-10-LABX-0062
Recombination des cassettes d'intégron: dynamique in vivo et in vitro - ANR-12-BSV3-0015

Unités de recherche

MFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234

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Unmasking the ancestral activity of integron integrases reveals a smooth evolutionary transition during functional innovation