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In order for migration to occur, RuvA must be associated with RuvB and [[Adenosine triphosphate|ATP]]. RuvB has the ability to [[ATP hydrolysis|hydrolyze]] ATP, driving the movement of the branch point. RuvB is a hexamer with [[helicase]] activity, and also binds the DNA. As ATP is hydrolyzed, RuvB rotates the recombined strands while pulling them out of the junction, but does not separate the strands as helicase would.<ref name=":2" />
The final step in branch migration is called resolution and requires the protein [[RuvABC|RuvC]]. The protein is a dimer, and will bind to the Holliday junction when it takes on the stacked X form. The protein has [[endonuclease]] activity, and cleaves the strands at exactly the same time. The cleavage is symmetrical, and gives two recombined DNA molecules with single stranded breaks.<ref>
The eukaryotic mechanism is much more complex involving different and additional proteins, but follows the same general path.<ref name=":1" /> [[RAD54B|Rad54]], a highly conserved eukaryotic protein, is reported to oligomerize on [[Holliday junction]]s to promote branch migration.<ref name="pmid29295984">{{cite journal |vauthors=Goyal N, Rossi MJ, Mazina OM, Chi Y, Moritz RL, Clurman BE, Mazin AV |title=RAD54 N-terminal domain is a DNA sensor that couples ATP hydrolysis with branch migration of Holliday junctions |journal=Nat Commun |volume=9 |issue=1 |pages=34 |year=2018 |pmid=29295984 |pmc=5750232 |doi=10.1038/s41467-017-02497-x }}</ref>
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