English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/3523
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Exportar a otros formatos:


The Relaxase of the Rhizobium etli Symbiotic Plasmid Shows nic Site cis-Acting Preference

AuthorsPérez-Mendoza, Daniel; Lucas, María; Muñoz, Socorro; Olivares Pascual, José; Cruz, Fernando de la ; Sanjuán, Juan
Issue DateNov-2006
PublisherAmerican Society for Microbiology
CitationJournal of Bacteriology 188(21): 7488–7499 (2006)
AbstractGenetic and biochemical characterization of TraA, the relaxase of symbiotic plasmid pRetCFN42d from Rhizobium etli, is described. 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 in the family Rhizobiaceae. We studied the range of N265TraA relaxase specificity in vitro by testing different oligonucleotides in binding and nicking assays. In addition, the ability of pRetCFN42d to mobilize different Rhizobiaceae plasmid origins of transfer (oriT) was examined. Data obtained with these approaches allowed us to establish functional and phylogenetic relationships between different plasmids of this family. Our results suggest novel characteristics of the R. etli pSym relaxase for previously described conjugative systems, with emphasis on the oriT cis-acting preference of this enzyme and its possible biological relevance.
Publisher version (URL)http://dx.doi.org/10.1128/JB.00701-06
Appears in Collections:(EEZ) Artículos
(CIB) Artículos
Files in This Item:
There are no files associated with this item.
Show full item record
Review this work

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.