Fig. 6 | Signal Transduction and Targeted Therapy

Fig. 6

From: Structural basis for the acetylation of histone H3K9 and H3K27 mediated by the histone chaperone Vps75 in Pneumocystis carinii

Fig. 6

Vps75-dependent Rtt109 HAT activity on histone H3K9 and H3K27. a H3K9, H3K27, and H3K56 were acetylated by recombinant PcRtt109 and/or a mixture of PcRtt109 and PcVps75F, indicated as PcRtt109/PcVps75F. Acetyl-CoA was used in the HAT assay, and the presence of acetylated H3K9, H3K27, and H3K56 was determined by western blot analysis. The PcRtt109 proteins used in the assays were assessed by anti-His antibody (shown in the first panel). PcVps75F was assessed by Coomassie staining (second panel), while the substrate histone (H3–H4)2 was assessed by western blotting with anti-H3 antibody (last panel). b, c H3K9 and H3K27 were acetylated by recombinant PcRtt109 with b (H3–H4)2, PcVps75F:(H3–H4)2 (0.5:1), PcVps75F:(H3–H4)2 (1:1), or PcVps75F:(H3–H4)2 (1.5:1) and with c PcVps75F:(H3–H4)2 (1:1), PcVps75F-K5:(H3–H4)2 (1:1), PcVps75∆C:(H3–H4)2 (1:1), or PcVps75∆C-K5:(H3–H4)2 (1:1)

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