Close
  Indian J Med Microbiol
 

Figure 5: p53-p300 collaboration is established by sulphur, which rescues p300 from p65NFκB in NSCLC cells. (A) p53-associated p300 was immunopurified with anti-p53 antibody from nuclear lysates of un-/placebo-/sulphur-treated A549 cells and were western-blotted (WB) with p300 and p53 antibodies. (B) A portion of cells from the same experimental set were subjected to ChIP assay for the determination of p53 binding on Bax promoter. (C) p53-/p65NFκBassociated p300 was immunopurified with anti-p53/p65NFκB antibodies from nuclear lysates of control and p53-cDNA transfected A549 cells and were western-blotted (WB) with p300 antibody. (D) p53-/p65NFκB-associated p300 was immunopurified with anti-p53 and p65NFκB antibodies from nuclear lysates of control, p53-cDNA transfected or IκBα-SR-cDNA transfected A549 cells and were western-blotted (WB) with anti-p300, p53 and p65NFκB antibodies (E) p65NFκB-associated p300 was immunopurified with p65NFκB antibody from nuclear lysates of un-/placebo-/sulphur-treated A549 cells and were western-blotted (WB) with p300 and p65NFκB antibodies. (F) A portion of cells from the same experimental set were subjected to ChIP assay for the determination of p65NFκB binding on Bcl-2 promoter. To verify comparable protein input during immunoprecipitation, 20% of supernatant from the nuclear lysates was blotted with histone H1 antibody

Figure 5: p53-p300 collaboration is established by sulphur, which rescues p300 from p65NFκB in NSCLC cells. (A) p53-associated p300 was immunopurified with anti-p53 antibody from nuclear lysates of un-/placebo-/sulphur-treated A549 cells and were western-blotted (WB) with p300 and p53 antibodies. (B) A portion of cells from the same experimental set were subjected to ChIP assay for the determination of p53 binding on Bax promoter. (C) p53-/p65NFκBassociated p300 was immunopurified with anti-p53/p65NFκB antibodies from nuclear lysates of control and p53-cDNA transfected A549 cells and were western-blotted (WB) with p300 antibody. (D) p53-/p65NFκB-associated p300 was immunopurified with anti-p53 and p65NFκB antibodies from nuclear lysates of control, p53-cDNA transfected or IκBα-SR-cDNA transfected A549 cells and were western-blotted (WB) with anti-p300, p53 and p65NFκB antibodies (E) p65NFκB-associated p300 was immunopurified with p65NFκB antibody from nuclear lysates of un-/placebo-/sulphur-treated A549 cells and were western-blotted (WB) with p300 and p65NFκB antibodies. (F) A portion of cells from the same experimental set were subjected to ChIP assay for the determination of p65NFκB binding on Bcl-2 promoter. To verify comparable protein input during immunoprecipitation, 20% of supernatant from the nuclear lysates was blotted with histone H1 antibody