8G3G

CryoEM structure of yeast recombination mediator Rad52

Summary for 8G3G

• Entry DOI: 10.2210/pdb8g3g/pdb
• EMDB information: 29695
• Descriptor: DNA repair and recombination protein RAD52 (1 entity in total)
• Functional Keywords: recombination mediator protein, dna repair, apo structure, decamer, recombination
• Biological source: Saccharomyces cerevisiae S288C
• Total number of polymer chains: 10
• Total formula weight: 524764.96

Authors

Deveryshetty, J.,Basore, K.,Rau, M.,Fitzpatrick, J.A.J.,Antony, E. (deposition date: 2023-02-07, release date: 2023-11-15)

Primary citation

Deveryshetty, J.,Chadda, R.,Mattice, J.R.,Karunakaran, S.,Rau, M.J.,Basore, K.,Pokhrel, N.,Englander, N.,Fitzpatrick, J.A.J.,Bothner, B.,Antony, E.
Yeast Rad52 is a homodecamer and possesses BRCA2-like bipartite Rad51 binding modes.
Nat Commun, 14:6215-6215, 2023

PubMed 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.

PubMed: 37798272
DOI: 10.1038/s41467-023-41993-1

Experimental method

ELECTRON MICROSCOPY (3.5 Å)