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. Author manuscript; available in PMC: 2016 Jan 21.
Published in final edited form as: Nat Struct Mol Biol. 2014 Nov 10;21(12):1047–1057. doi: 10.1038/nsmb.2912

Figure 8. A model depicting the interdependence between the passage of Pol II elongation complexes through nucleosomes and acetyl-histone binding of BRD4 at enhancers and within protein-coding genes.

Figure 8

BRD4 contributes to the progression of the elongation complexes via its histone chaperone activity depending on its interaction with hyper-acetylated nucleosomes. The BET bromodomain inhibitor JQ1 occludes the acetyl-histone binding pockets of the BRD4 bromodomains, disabling the elongation-facilitating activity of BRD4.