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

dc.contributor.authorESCUDERO, Jose Antonio
dc.contributor.authorLOOT, Celine
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorPARISSI, Vincent
dc.contributor.authorNIVINA, Aleksandra
dc.contributor.authorBOUCHIER, Christiane
dc.contributor.authorMAZEL, Didier
dc.date.accessioned2023-07-04T12:22:47Z
dc.date.available2023-07-04T12:22:47Z
dc.date.issued2016-03-10
dc.identifier.issn2041-1723
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/183269
dc.description.abstractEnTyrosine (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.
dc.description.sponsorshipIntegrative Biology of Emerging Infectious Diseases - ANR-10-LABX-0062
dc.description.sponsorshipRecombination des cassettes d'intégron: dynamique in vivo et in vitro - ANR-12-BSV3-0015
dc.language.isoen
dc.publisherNature Publishing Group
dc.rights.urihttp://creativecommons.org/licenses/by/
dc.subject.enBiological sciences
dc.subject.enMolecular biology
dc.title.enUnmasking the ancestral activity of integron integrases reveals a smooth evolutionary transition during functional innovation
dc.typeArticle de revueen_US
dc.identifier.doi10.1038/ncomms10937
dc.subject.halSciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biologie moléculaire
dc.subject.halSciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologie/Bactériologie
dc.subject.halSciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biologie structurale [q-bio.BM]
dc.subject.halSciences du Vivant [q-bio]/Génétique
dc.subject.halSciences du Vivant [q-bio]/Microbiologie et Parasitologie
dc.description.sponsorshipEuropeEvolution and Transfer of Antibiotic Resistance
dc.description.sponsorshipEuropeThe Integron Cassette Dynamics and the Integrase Gene Expression
bordeaux.pageArticle number 10937
bordeaux.volume7
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.institutionCNRS
bordeaux.peerReviewedoui
bordeaux.import.sourcehal
hal.identifierpasteur-01292328
hal.version1
hal.popularnonen_US
hal.audienceInternationaleen_US
hal.exportfalse
workflow.import.sourcehal
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.date=2016-03-10&rft.volume=7&rft.spage=Article%20number%2010937&rft.epage=Article%20number%2010937&rft.eissn=2041-1723&rft.issn=2041-1723&rft.au=ESCUDERO,%20Jose%20Antonio&LOOT,%20Celine&PARISSI,%20Vincent&NIVINA,%20Aleksandra&BOUCHIER,%20Christiane&rft.genre=article


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