E. coli RuvB protein forms a complex with RuvA protein at the late stage of homologous recombination and recombination repair and binds specifically to the Holliday structure which is the intermediate of recombination, allowing the migration of Holliday junction using ATP hydrolysis energy and expands the heteroduplex region. RuvB forms a hexamer ring structure and surrounds the double chain DNA and covers RuvA tetramer bound to the Holliday junction from both sides. RuvB is a DNA motor protein which possesses the ATPase activity, activated by DNA and RuvA protein (1, 2). Its molecular weight is 37 kD and forms a dimer in solution in the physiological condition.
This product is a recombinant protein abundantly expressed by E. coli and purified by methods such as chromatography (Fig. 1).
1) Studies on homologous recombination mechanism.
2) To make use of the motor protein function that specifically migrates the Holliday junction by forming a complex with RuvA (branch-migration protein).
Fig.1 Polyacrylamide gel electrophoresis of RuvB 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 (1992) “Escherichia coli RuvA and RuvB proteins specifically interact with Holliday junctions and promote branch migration.” Genes Dev 6:2214-2220 PMID: 1427081
To be used for research only. DO NOT use for human gene therapy or clinical diagnosis.