Fig. 4: Rad52 (310–394) competes with Rad51 oligomers through the cooperative binding of several anchors.
From: A large C-terminal Rad52 segment acts as a chaperone to Form and Stabilize Rad51 Filaments
a Left panel, best AlphaFold2 model of the complex between Rad51 (77–400) (gray surface) and Rad52 (310–394) (colored in magenta). The three key residues mutated are highlighted with balls. Right panel, structure of three Rad51 monomers assembled in a multimer (PDB code 1SZP). The central protein is truncated (Rad51 (70–400) and shown as a gray surface), the two other Rad51 molecules (#-1 et #+1) are shown as cartoon in blue. Residue F144 side chain is highlighted. For both panels, the Rad51 surface buried upon formation of the Rad51 filament is colored in blue. b Zoomed-in of residues F316 and F337 (left panel) and Y376 (right panel). The Rad51 surface is shown with transparency to show the position of K214 and T161 from Rad51 contacting F337 and Y376, respectively. The Rad51 surface buried upon formation of the Rad51 filament is colored in blue. c In light gray, mapping of the interaction between Rad52-Cter domain mutants (295–394) and Rad51, using the intensities ratio (I/I0), where I and I0 are the intensity of the signals 1H-15N SOFAST-HMQC spectra before and after addition of Rad51, respectively. For comparison, values for the WT are indicated in dark gray. d SEC profile analysis of Rad51, Rad52 (295–394) and Rad51 + Rad52 (295–394) WT and mutants in a 1:1 ratio. Source data are provided in the Source Data file.
