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

Jaigeeth Deveryshetty, Rahul Chadda, Jenna R. Mattice, Simrithaa Karunakaran, Michael J. Rau, Katherine Basore, Nilisha Pokhrel, Noah Englander, James A. J. Fitzpatrick, Brian Bothner and Edwin Antony ()
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Jaigeeth Deveryshetty: Saint Louis University School of Medicine
Rahul Chadda: Saint Louis University School of Medicine
Jenna R. Mattice: Montana State University
Simrithaa Karunakaran: Saint Louis University School of Medicine
Michael J. Rau: Washington University in St. Louis School of Medicine
Katherine Basore: Washington University in St. Louis School of Medicine
Nilisha Pokhrel: Marquette University
Noah Englander: Saint Louis University School of Medicine
James A. J. Fitzpatrick: Washington University in St. Louis School of Medicine
Brian Bothner: Montana State University
Edwin Antony: Saint Louis University School of Medicine

Nature Communications, 2023, vol. 14, issue 1, 1-16

Abstract: 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 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 Rad51 filaments in HR.

Date: 2023
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DOI: 10.1038/s41467-023-41993-1

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