E. coli RuvC protein is a structurally specific endonuclease which binds specifically to the Holliday structure, an intermediate of recombination, at the late stage of homologous recombination and recombination repair and introduces a nick in the symmetrical point of the Holliday junction cleaving and resolving the recombinant (1, 2). The product is a recombinant protein abundantly expressed by E. coli and purified by methods such as chromatography (Fig. 1). Its molecular weight is 19 kD and forms a dimer in liquid and in binding tate with the Holliday structure.
1) Studies on homologous recombination mechanism
2) To use as endonuclease which functions specifically to the Holliday structure
Fig.1 Polyacrylamide gel electrophoresis of RuvC protein.
1. Shinagawa H and Iwasaki H (1996) “Processing the holliday junction in homologous
recombination.” Trend Biochem Sci 21:107-111 PMID: 8882584
2. Iwasaki H et al (1991) “Escherichia coli RuvC protein is an endonuclease that resolves
the Holliday structure.” EMBO J 10:4381-4389 (1991) PMID: 1661673
3. Murayama Y et al (2008) “Formation and branch migration of Holliday junctions
mediated by eukaryotic recombinases.”Nature 451:1018-1021PMID:18256600
To be used for research only. DO NOT use for human gene therapy or clinical diagnosis.