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. 2014 Oct 30;13(16):2554–2563. doi: 10.4161/15384101.2014.942204

Figure 1.

Figure 1.

The C-terminal region of HMG20b mediates complex formation with BRCA2. (A) Domain structure of HMG20b and design of N-terminal and C-terminal HMG20b fragments. The boundaries are shown as amino acid residue numbers. Binding affinity for BRC5 is shown next to each fragment. (B) Relative binding affinity of each HMG20b fragment for BRC5 repeat. Binding affinity was calculated by dividing band intensities of bound fractions by those of input. Relative binding affinity of each fragment compared to the full-length protein is shown as means ± s.e.m. from 3 independent experiments. Each HMG20b fragment is compared with the full-length HMG20b by Dunnett's multiple comparison test (**: 0.001 < P < 0.01, *: 0.01 < P < 0.05, ns: P > 0.05). (C) Coomassie brilliant blue staining of gel showing purified HMG20b fragments (marked with an asterisk). (D) C-terminal region of HMG20b mediates binding to BRC5 motif. Coomassie brilliant blue staining of gel from Streptavidin pull-down assay. HMG20b fragments bound to Biotin-BRC5 peptide are marked with an asterisk. BSA included in excess amount in the binding buffer appears after staining of the gel.