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. Author manuscript; available in PMC: 2017 Jan 3.
Published in final edited form as: Biochemistry. 2016 Dec 1;55(49):6766–6775. doi: 10.1021/acs.biochem.6b00841

Figure 4.

Figure 4

Isolated p300 KAT domain, lacking a CH3 domain, is not stimulated by TDG. The rate of full length p300 (A and C) or p300 KAT domain (B and D) acetylation of H3K18 (A and B) or H3K23 (C and D) is shown, in the presence of varying concentrations of wild-type TDG. The p53 peptide abrogates stimulation of p300 by TDG. The rate of acetylation at H3K18 (E) and H3K23 (F) decreases when p300 is bound by the p53 (amino acids 38–61) peptide. This interaction interferes with the stimulation caused by TDG. *p < 0.05; **p < 0.01; ***p < 0.001.