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

Nature Structural & Molecular Biology
Yi ZhangTatiana G Kutateladze

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.

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Citations

Jan 30, 2019·Critical Reviews in Biochemistry and Molecular Biology·Yi ZhangTatiana G Kutateladze
Jul 6, 2019·Nature Reviews. Drug Discovery·Andrea G CochranRobert J Sims
Nov 7, 2019·Scientific Reports·Deb Ranjan BanerjeeJonathan T Sczepanski
Oct 15, 2020·Open Biology·Amanuel Tafessu, Laura A Banaszynski
Nov 24, 2020·Journal of Molecular Biology·Yucong YuXiaobing Shi
Feb 20, 2021·Developmental Biology·Clara R StelmanRachel H Roberts-Galbraith
Jun 26, 2021·The EMBO Journal·Ying-Ying WangLi-Lin Du
Jul 30, 2020·Structure·Jiuyang LiuTatiana G Kutateladze

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Datasets Mentioned

BETA
GSE109591

Methods Mentioned

BETA
acetylation
pull-down
NMR
ChIP
immunoprecipitation
histone acetylation
acetylate
ChIP-seq
size exclusion chromatography
X-ray

Software Mentioned

bowtie
Kaleidagraph
MACS
deepTools
NIH
MOLProbity
Phoenix Refine
EpiCypher
R
Coot

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