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. 2011 May 25;81(2):434–456. doi: 10.1111/j.1365-2958.2011.07703.x

Fig. 8.

Fig. 8

A comparison of RAD51 paralogue complexes, and their interaction with RAD51, in mammals, S. cerevisiae and T. brucei. The two principle Rad51 paralogue complexes found in mammals, XRCC2-Rad51D-Rad51C-Rad51B (2-D-C-B) and XRCC3-Rad51C (3-C), are shown as well as two further complexes (2-D, C-B). In S. cerevisiae, Rad55 (55) and Rad57 (57) are the only Rad51 paralogues, and form a stable complex. Experimentally determined interactions between the mammalian and yeast Rad51 paralogue complexes and Rad51 (51) are shown. In T. brucei, three Rad51 paralogues, RAD51-3 (3), RAD51-4 (4) and RAD51-6 (6), interact and experiments indicate either a stable trimer or distinct dimeric complexes; interactions with RAD51 or with a fourth Rad51 paralogue, RAD51-5 (5), have not been detected. Proteins are coloured to indicate potential orthology in the three organisms: Rad51 is orthologous in all (pink); Rad57 is considered orthologous with XRCC3 (dark blue) (Lin et al., 2006); and we propose that T. brucei RAD51-3 is orthologous with Rad51C (red).