2024-03-28T13:33:31Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/35232021-12-28T15:52:03Zcom_10261_59com_10261_6com_10261_86com_10261_1col_10261_312col_10261_339
00925njm 22002777a 4500
dc
Pérez-Mendoza, Daniel
author
Lucas, María
author
Muñoz, Socorro
author
Olivares Pascual, José
author
Cruz, Fernando de la
author
Sanjuán, Juan
author
2006-11
Genetic 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.
Journal of Bacteriology 188(21): 7488–7499 (2006)
1098-5530
http://hdl.handle.net/10261/3523
10.1128/JB.00701-06
16916896
The Relaxase of the Rhizobium etli Symbiotic Plasmid Shows nic Site cis-Acting Preference