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The ZZ domain of p300 mediates specificity of the adjacent HAT domain for histone H3

Yi Zhang,Yongming Xue,Jiejun Shi,Jaewoo Ahn,W. Mi,Muzaffar Ali,Xiaolu Wang,B. J. Klein,H. Wen,Xiaobing Shi,T. Kutateladze

Published 2018 in Nature Structural & Molecular Biology

ABSTRACT

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 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 of p300 play critical roles in modulating p300 enzymatic activity and its association with chromatin. The acetyllysine binding function of bromodomain is essential for acetylation of histones H3 and H4, whereas interaction of the ZZ domain with H3 promotes selective acetylation of the histone H3K27 and H3K18 sites. Structural and biochemical analyses identify the ZZ domain of p300 as a novel histone H3–binding module that promotes p300 chromatin association and is required for selective acetylation of H3K18 and H3K27 in human cells.

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