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The ZZ-type zinc finger of ZZZ3 modulates the ATAC complex-mediated histone acetylation and gene activation
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) dom...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6138639/ https://www.ncbi.nlm.nih.gov/pubmed/30217978 http://dx.doi.org/10.1038/s41467-018-06247-5 |
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author | Mi, Wenyi Zhang, Yi Lyu, Jie Wang, Xiaolu Tong, Qiong Peng, Danni Xue, Yongming Tencer, Adam H. Wen, Hong Li, Wei Kutateladze, Tatiana G. Shi, Xiaobing |
author_facet | Mi, Wenyi Zhang, Yi Lyu, Jie Wang, Xiaolu Tong, Qiong Peng, Danni Xue, Yongming Tencer, Adam H. Wen, Hong Li, Wei Kutateladze, Tatiana G. Shi, Xiaobing |
author_sort | Mi, Wenyi |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6138639 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-61386392018-09-17 The ZZ-type zinc finger of ZZZ3 modulates the ATAC complex-mediated histone acetylation and gene activation Mi, Wenyi Zhang, Yi Lyu, Jie Wang, Xiaolu Tong, Qiong Peng, Danni Xue, Yongming Tencer, Adam H. Wen, Hong Li, Wei Kutateladze, Tatiana G. Shi, Xiaobing Nat Commun Article 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. Nature Publishing Group UK 2018-09-14 /pmc/articles/PMC6138639/ /pubmed/30217978 http://dx.doi.org/10.1038/s41467-018-06247-5 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Mi, Wenyi Zhang, Yi Lyu, Jie Wang, Xiaolu Tong, Qiong Peng, Danni Xue, Yongming Tencer, Adam H. Wen, Hong Li, Wei Kutateladze, Tatiana G. Shi, Xiaobing The ZZ-type zinc finger of ZZZ3 modulates the ATAC complex-mediated histone acetylation and gene activation |
title | The ZZ-type zinc finger of ZZZ3 modulates the ATAC complex-mediated histone acetylation and gene activation |
title_full | The ZZ-type zinc finger of ZZZ3 modulates the ATAC complex-mediated histone acetylation and gene activation |
title_fullStr | The ZZ-type zinc finger of ZZZ3 modulates the ATAC complex-mediated histone acetylation and gene activation |
title_full_unstemmed | The ZZ-type zinc finger of ZZZ3 modulates the ATAC complex-mediated histone acetylation and gene activation |
title_short | The ZZ-type zinc finger of ZZZ3 modulates the ATAC complex-mediated histone acetylation and gene activation |
title_sort | zz-type zinc finger of zzz3 modulates the atac complex-mediated histone acetylation and gene activation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6138639/ https://www.ncbi.nlm.nih.gov/pubmed/30217978 http://dx.doi.org/10.1038/s41467-018-06247-5 |
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