Fig. 3: Rad52 (310–394) folds upon binding Rad51 burying a large conserved surface.
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 according to sequence conservation: from red for the highest conservation to white). Three boxes highlight zoomed-in regions shown in the right panels. Right panels: the side chains of Rad52 residues interacting with Rad51 are depicted as sticks, with mutated residues represented in ball-and-stick. Labels point to the C-alpha carbons of the mutated residues. Green dashed lines highlight hydrogen bonds. b AlphaFold2 model of the Rad51 (77–400) complex with its surface colored according to sequence conservation and Rad52 (310–394) shown as a gray cartoon. Two perpendicular orientations are provided in the upper and lower panels, respectively. c Interaction loss (%) plotted as a function of the surface area of each residue buried upon interaction. Interaction loss was determined by the intensity ratio between mutant and WT Rad52 co-immunoprecipitated with Rad51. d Serial 10-fold dilutions of haploid strains bearing different RAD52 mutations of residue involved in the interaction, spotted onto rich medium (YPD) containing different MMS concentrations. Upper panel: SRS2 background, lower panel: srs2∆ background. Source data are provided in the Source Data file.
