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. Author manuscript; available in PMC: 2026 Sep 23.
Published in final edited form as: Mol Cell. 2026 Aug 6;86(16):3185–3197.e7. doi: 10.1016/j.molcel.2026.07.012

Figure 4: Role of BRD4 BD1 bromodomain and basic patch 1 residues in nucleosome binding and structural compactness.

Figure 4:

(a) BRD4 BD1 interactions with the nucleosome with key regions highlighted, (b) TR-FRET dissociation constants for BRD4-S bromodomain mutants binding to H4 K12acK16ac nucleosomes, (c) model for how BRD4 basic region 1 could interact with nucleosome DNA minor groove with Cα positions of the 5 basic residues shown in blue spheres, (d) effect of BRD4-S BD1 mutations on BRD4-S/nucleosome complex mobility in gel mobility shift assay, (e) NMR structure of HMG-I(Y) AT-hook Arg-Gly-Arg region binding to DNA (PDB ID 2EZD), protein residues outside of the Arg-Gly-Arg region not shown, (f) TR-FRET dissociation constants for BRD4-S basic patch 1 mutants binding to H4 K12acK16ac nucleosomes, (g) the BRD4-S WT/H4 K12acK16 ac nucleosome complex elutes slightly later than the BRD4-S WT/WT nucleosome complex (peak elution of 9.8 vs 9.6 ml) in Superdex 200 increase size-exclusion chromatography, (h) the BRD4-S m12/H4 K12acK16ac nucleosome complex (blue) elutes earlier than the BRD4-S WT/H4 K12acK16ac nucleosome complex in Superdex 200 increase size-exclusion chromatography, (i) the BRD4-S m12 protein elutes at similar time as the BRD4 WT protein in Superdex 200 increase size-exclusion chromatography