Fig. 1: PBRM1 and p53 display a physical association that is enhanced after DNA damage. | Nature Communications

Fig. 1: PBRM1 and p53 display a physical association that is enhanced after DNA damage.

From: PBRM1 acts as a p53 lysine-acetylation reader to suppress renal tumor growth

Fig. 1

a U2OS cells (left) and HEK293T cells (right) were transfected with vector or Flag-PBRM1 and harvested for immunoprecipitation with Flag-M2 beads and elution with 3X Flag peptide. Inputs and eluates were analyzed by immunoblots. b, c H1299 cells were transfected with Flag-PBRM1 and Myc-p53 and treated with etoposide (50 μM, b) or bleomycin (10 μg/ml, c) for the indicated times. Lysates were subjected to immunoprecipitation with Flag-M2 beads. Inputs and eluates were analyzed by immunoblots. d HEK293 cells were treated with vehicle (DMSO) or etoposide (50 μM) for 8 h and harvested for immunoprecipitation with control IgG and p53 antibodies. The bound PBRM1 and p53 were examined by immunoblots. e HCT116 and HCT116 p53−/− cells were treated with DMSO or 50 μM etoposide for 24 h. Lysates were immunoprecipitated with p53 antibody. The bound PBRM1 and p53 were examined by immunoblots. Source data are provided as a Source Data file.

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