RT Journal Article
T1 Replicative resolution of integron cassette insertion
A1 Loot, Céline
A1 Ducos Galand, Magaly
A1 Escudero García-Calderón, José Antonio
A1 Bouvier, Marie
A1 Mazel, Didier
AB Site-specific recombination catalyzed by tyrosine recombinases follows a common pathway consisting of two consecutive strand exchanges. The first strand exchange generates a Holliday junction (HJ), which is resolved by a second strand exchange. In integrons, attC sites recombine as folded single-stranded substrates. Only one of the two attC site strands, the bottom one, is efficiently bound and cleaved by the integrase during the insertion of gene cassettes at the double-stranded attI site. Due to the asymmetry of this complex, a second strand exchange on the attC bottom strand (bs) would form linearized abortive recombination products. We had proposed that HJ resolution would rely on an uncharacterized mechanism, probably replication. Using an attC site carried on a plasmid with each strand specifically tagged, we followed the destiny of each strand after recombination. We demonstrated that only one strand, the one carrying the attC bs, is exchanged. Furthermore, we show that the recombination products contain the attC site bs and its entire de novo synthesized complementary strand. Therefore, we demonstrate the replicative resolution of single-strand recombination in integrons and rule out the involvement of a second strand exchange of any kind in the attC×attI reaction
PB Oxford Univeristy Press
SN 0305-1048
YR 2012
FD 2012-06-26
LK https://hdl.handle.net/20.500.14352/116970
UL https://hdl.handle.net/20.500.14352/116970
LA eng
NO Loot, C., Ducos-Galand, M., Escudero, J. A., Bouvier, M., & Mazel, D. (2012). Replicative resolution of integron cassette insertion. Nucleic Acids Research, 40(17), 8361-8370. https://doi.org/10.1093/NAR/GKS620
NO The authors acknowledge Alfonso Soler Bistue´, Zeynep Baharoglu and Michael Jason Bland for critical reading of this article
NO Centre National de la Recherche Scientifique (Francia)
NO European Commission
DS Docta Complutense
RD 9 abr 2025