The ZZ-type zinc finger of ZZZ3 modulates the ATAC complex-mediated histone acetylation and gene activation

Wenyi Mi, Yi Zhang, Jie Lyu, Xiaolu Wang, Qiong Tong, Danni Peng, Yongming Xue, Adam H. Tencer, Hong Wen, Wei Li, Tatiana G. Kutateladze () and Xiaobing Shi ()
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Wenyi Mi: The University of Texas MD Anderson Cancer Center
Yi Zhang: University of Colorado School of Medicine
Jie Lyu: Baylor College of Medicine
Xiaolu Wang: The University of Texas MD Anderson Cancer Center
Qiong Tong: University of Colorado School of Medicine
Danni Peng: The University of Texas MD Anderson Cancer Center
Yongming Xue: The University of Texas MD Anderson Cancer Center
Adam H. Tencer: University of Colorado School of Medicine
Hong Wen: The University of Texas MD Anderson Cancer Center
Wei Li: Baylor College of Medicine
Tatiana G. Kutateladze: University of Colorado School of Medicine
Xiaobing Shi: The University of Texas MD Anderson Cancer Center

Nature Communications, 2018, vol. 9, issue 1, 1-9

Abstract: Abstract Recognition of histones by epigenetic readers is a fundamental mechanism for the regulation of chromatin and transcription. Most reader modules target specific post-translational modifications on histones. Here, we report the identification of a reader of histone H3, the ZZ-type zinc finger (ZZ) domain of ZZZ3, a subunit of the Ada-two-A-containing (ATAC) histone acetyltransferase complex. The solution NMR structure of the ZZ in complex with the H3 peptide reveals a unique binding mechanism involving caging of the N-terminal Alanine 1 of histone H3 in an acidic cavity of the ZZ domain, indicating a specific recognition of H3 versus other histones. Depletion of ZZZ3 or disruption of the ZZ-H3 interaction dampens ATAC-dependent promoter histone H3K9 acetylation and target gene expression. Overall, our study identifies the ZZ domain of ZZZ3 as a histone H3 reader that is required for the ATAC complex-mediated maintenance of histone acetylation and gene activation.

Date: 2018
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DOI: 10.1038/s41467-018-06247-5

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