Fig. 5 | Signal Transduction and Targeted Therapy

Fig. 5

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

Fig. 5

The major histone contact surface in PcVps75. a, b Superposition of PcVps75 with NAP1 in S. cerevisiae (ScNAP1) in the NAP1-H2A–H2B complex. PcVps75 is orange, ScNAP1 is silver, H2A is pink, and H2B is purple. The major interface between ScNAP1 and H2A is circled in red, and the homologous residues in PcVps75F within the interface are shown as sticks and colored orange. c The acidic region in α7 of PcVps75 is aligned with ScNAP1 and marked K5, shown as surface and sticks and colored blue. d GST-tagged PcVps75F, PcVps75F-K5, PcVps75ΔC, and PcVps75ΔC-K5 were incubated with excess (H3–H4)2 and stained with Coomassie Blue. e GST-tagged PcVps75F, PcVps75F-K5, PcVps75ΔC, and PcVps75ΔC-K5 were incubated with excess H2A–H2B and stained with Coomassie Blue

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