Figure 3

Domain mapping of Mus musculus RAD51D. (A-B) Yeast two-hybrid analysis of RAD51DΔ3 and RAD51D+int3 are directly compared with the original deletion constructs of RAD51D. (C) Diagram of the RAD51DΔ3 and RAD5D+int3 alternative splice constructs compared with the amino (4–77) and carboxy-terminal (77–329) regions of RAD51D. The black box represents the predicted linker region of RAD51D. (D) The region of the protein that allows interaction with XRCC2 is illustrated in bold type, while sequence required for its interaction with RAD51C is presented in italics (note a small area of overlap between residues 223–233). The underlined 24 amino acid region (residues 54–77) appears to be critical for determining the specificity of the interaction between RAD51D isoforms and XRCC2. (E) Homology model of RAD51D from the Pyrococcus furiosus RAD51 crystal structure. The yellow highlighted region (left) represents the linker region and the yellow area (right) represents the 24 amino acid region proposed to determine XRCC2 specificity. Abbreviations: 51D; RAD51D-FL, 51C; RAD51C, X2; XRCC2, 4–77; residues 4–77 of the amino-terminal domain of RAD51D, 77–329; residues 77–329 of the carboxy-terminal domain of RAD51D, pGAD; pGADT7 vector, pGBK; pGBKT7 vector.