6E86

Solution structure of ZZZ3 ZZ domain in complex with histone H3K4ac peptide

Summary for 6E86

• Entry DOI: 10.2210/pdb6e86/pdb
• Related: 6E83
• NMR Information: BMRB: 30502
• Descriptor: ZZ-type zinc finger-containing protein 3, H3K4ac, ZINC ION (3 entities in total)
• Functional Keywords: zzz3, zz domain, histone, chromatin, gene regulation
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 8385.05

Authors

Zhang, Y.,Kutateladze, T.G. (deposition date: 2018-07-27, release date: 2018-09-19, Last modification date: 2024-10-16)

Primary citation

Mi, W.,Zhang, Y.,Lyu, J.,Wang, X.,Tong, Q.,Peng, D.,Xue, Y.,Tencer, A.H.,Wen, H.,Li, W.,Kutateladze, T.G.,Shi, X.
The ZZ-type zinc finger of ZZZ3 modulates the ATAC complex-mediated histone acetylation and gene activation.
Nat Commun, 9:3759-3759, 2018

PubMed 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.

PubMed: 30217978
DOI: 10.1038/s41467-018-06247-5

Experimental method

SOLUTION NMR