Yeast Rad52 is a homodecamer and possesses BRCA2-like bipartite Rad51 binding modes

Yeast Rad52 is a homodecamer and possesses BRCA2-like bipartite Rad51 binding modes

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Abstract Homologous recombination (HR) is an essential double-stranded DNA break repair pathway.In HR, Rad52 facilitates the formation of Rad51 nucleoprotein filaments on RPA-coated ssDNA.Here, we decipher how Rad52 functions using single-particle cryo-electron microscopy and biophysical approaches.We report that Rad52 is a homodecameric ring and us polo assn mens sweaters each subunit possesses an ordered N-terminal and disordered C-terminal half.

An intrinsic structural asymmetry is observed where a few of the C-terminal halves interact with the ordered ring.We describe two conserved charged patches in the C-terminal half that harbor Rad51 and RPA interacting motifs.Interactions between these patches regulate ssDNA binding.Surprisingly, Rad51 interacts with Rad52 at two different bindings sites: one within the positive patch in the disordered C-terminus and the other in the ordered ring.

We propose that these features drive Rad51 nucleation onto a single position on the DNA to promote formation of uniform pre-synaptic chiggate.com Rad51 filaments in HR.