GSE109591
The ZZ domain of p300 mediates specificity of the adjacent HAT domain for histone H3
Human p300 is a transcriptional co-activator and a major acetyltransferase that acetylates histones and other proteins facilitating gene transcription. The activity of p300 relies on the fine-tuned interactome that involves a dozen p300 domains and hundreds of binding partners and links p300 to a wide range of vital signaling events. Here, we report on a novel function of the ZZ-type zinc finger (ZZ) of p300 as a reader of histone H3. We show that the ZZ domain and acetyllysine recognizing bromodomain (BD) of p300 play critical roles in modulating p300 enzymatic activity and its association with chromatin. Acetyllysine binding of BD is essential for acetylation of histones H3 and H4, whereas interaction of the ZZ domain with H3 promotes selective acetylation of histone H3K27 and H3K18. Overall design: ChIP-seq of Flag-p300, H3K27ac, H3K18ac were applied in human H1299 cells stably expressing WT or mutant (N1671A/D1690A) p300-BRPHZT fragment and control vector (V).