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. 2012 Nov 8;8(11):e1003047. doi: 10.1371/journal.pgen.1003047

Figure 3. Acetylated H4 lysines are the primary binding sites for Brd2 and are enriched on H2A.Z nucleosomes.

Figure 3

A. A schematic depicting the experimental design of the peptide competition assay. B. Western blots of eluted material from H2A.Z mononucleosome IPs performed in the presence of various competing peptides—sites of acetylation of the various peptides are indicated (UN, unacetylated peptide). H4 peptides acetylated at K12 alone or at K5, K8, K12 and K16 (Tetra) were able to efficiently compete away Brd2 binding to H2A.Z nucleosomes. C. H2A and H2A.Z nucleosomes were immunoprecipitated following treatment with DMSO or TSA—eluted material was analyzed by Western blot for various acetylation marks on H4 and H3. H2A.Z nucleosomes contain higher levels of acetylated H3 and H4 under both basal and hyperacetylated conditions. AcLys, an anti-pan-acetyl lysine antibody, which detects both acetyl H4 and H3 bands in our Western blot, was used as indicated.