Figure 3: Cysteine residues located in the putative zf-PARP-like domain and mutated in breast cancer patients affect the dsDNA binding activity of BRCA2T2.
From: A second DNA binding site in human BRCA2 promotes homologous recombination
(a) amino-acid sequence comprised in the putative zf-PARP-like domain defined by SMART showing the mutated cysteine residues. The ones found in breast cancer patients are highlighted in red. (b) Quantification of EMSA displayed in Supplementary Fig. 5b, (c) showing the binding of BRCA2T2, the indicated single mutants (c), and the double mutants to ssDNA. (d) EMSA showing the binding of BRCA2T2 and the indicated single mutants (e), and the double mutants to dsDNA. (f) Quantification of d. (g) Quantification of e. (h) EMSA showing the binding of BRCA2T2 and BRCA2 C315S to 3’ overhang ssDNA. (i) Quantification of h. Error bars, s.d. (n=3).
