Corentin Claeys Bouuaert @ccb-lab.bsky.social · Jan 18 Spo11 cleaves DNA via a topoisomerase-like mechanism involving hybrid active sites located at the dimer interface. Spo11 forms a complex with Ski8, Rec102 and Rec104, but unlike its topoisomerase relative, the complex has a monomeric (1:1:1:1) stoichiometry. How does it dimerize?
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We previously showed that the Spo11 core complex binds DNA and hypothesized that it may dimerize on DNA. Based on AFM imaging, we also proposed that the Spo11 complex bends DNA and perhaps traps a second DNA duplex prior to DNA cleavage, like type II topoisomerases do.