Fig. 3: TRRAP-TIP60 complex is responsible for histone acetylation at specific residues.

a Occupancy of pan-acetylated histone H3 and H4 in HSP72 promoter. ChIP assay was performed using HeLa cells treated as described in Fig. 2f. b Components of the TRRAP-TIP60 complex identified dominantly in heat-shocked cells. Nuclear extracts were prepared from cells overexpressing hTRRAP-3 × FLAG, and proteins co-immunoprecipitated with anti-FLAG were identified by MS. c Interaction between HSF1 and TIP60. Complexes co-immunoprecipitated using anti-HSF1 in nuclear extracts of heat-shocked cells were subjected to immunoblotting. d Occupancy of TIP60 in cells expressing HSF1-S419 mutants. ChIP assay was performed using cells treated as described in a. e Cells, in which components of HAT complexes were knocked down, were treated with heat shock. Levels of HSP72 mRNA were quantified, and relative levels are shown. f Occupancy of active chromatin marks in HSP72 promoter. ChIP assay was performed using untreated (Cont.) or heat-shocked (HS) cells, in which HSF1, TRRAP, TIP60, or p300 were knocked down. Norminal p-values were determined by one-way ANOVA, followed by Tukey-Kramer test in a and d–f. Error bars indicate SEM (n = 3) in a and d–f. Experiments were repeated two times for c.