ABB  Vol.1 No.5 , December 2010
Cloning, expression, purification and characterization of replication protein from plasmid pGP2 from Acetobacter estunensis
Abstract: The Acetobacter estunensis Rep34 protein participates in the replication of bacterial plasmid pGP2. The Rep34 protein of the A. estunensis, was cloned to the expression vector, that ensure fusion with a His-tag sequence (Rep34 His-tagged), over-expressed in Escherichia coli and purified by metal-affinity chromatography to yield a highly purified and active protein. On this purified protein number different activities and motifs were detected. DNA band-shift assays showed that the Rep34 His-tagged protein bound to the regulation region for replication on the linear double-stranded DNA. In the protein was determined phosphatase activity, ATPase activity and protein is possible to unwind double strand DNA.
Cite this paper: nullGrones, P. and Grones, J. (2010) Cloning, expression, purification and characterization of replication protein from plasmid pGP2 from Acetobacter estunensis. Advances in Bioscience and Biotechnology, 1, 417-425. doi: 10.4236/abb.2010.15055.

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