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J. Bacteriol. doi:10.1128/JB.00701-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

The relaxase of the Rhizobium etli symbiotic plasmid shows nic site cis-acting preference

Departamento de Microbiología del Suelo y Sistemas Simbióticos. Estación Experimental del Zaidín, Consejo Superior de Investigaciones Científicas (CSIC), Granada, Spain; Departamento de Biología Molecular (Unidad asociada al CIB, CSIC), Universidad de Cantabria, C/Herrera Oria s/n, 39011 Santander, Spain

^* To whom correspondence should be addressed. Email: juan.sanjuan{at}eez.csic.es.

	Abstract

A genetic and biochemical characterization of TraA, the relaxase of symbiotic plasmid pRetCFN42d from Rhizobium etli is presented. After purifying the relaxase domain (N265TraA), we demonstrated nic binding and cleavage activity in vitro, and thus characterized for the first time the nick site (nic) of a plasmid within the Rhizobiaceae family. We studied the range of N265TraA relaxase specificity in vitro by testing different oligonucleotides in binding and nicking assays. Besides, the ability of pRetCFN42d to mobilize different Rhizobiaceae plasmid origins of transfer (oriT) was examined. Data obtained from those approaches allowed us to establish functional and phylogenetic relationships between different plasmids of this family. These studies suggest novel characteristics of the R. etli pSym relaxase among conjugative systems previously described, with emphasis in its oriT cis-acting preference and its possible biological relevance.

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