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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.
  • Mi W; Department of Epigenetics and Molecular Carcinogenesis, Center for Cancer Epigenetics, The University of Texas MD Anderson Cancer Center, Houston, Texas, 77030, USA.
  • Zhang Y; Center for Epigenetics, Van Andel Research Institute, Grand Rapids, Michigan, 49503, USA.
  • Lyu J; Department of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado, 80045, USA.
  • Wang X; Dan L. Duncan Cancer Center, Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas, 77030, USA.
  • Tong Q; Department of Epigenetics and Molecular Carcinogenesis, Center for Cancer Epigenetics, The University of Texas MD Anderson Cancer Center, Houston, Texas, 77030, USA.
  • Peng D; Center for Epigenetics, Van Andel Research Institute, Grand Rapids, Michigan, 49503, USA.
  • Xue Y; Department of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado, 80045, USA.
  • Tencer AH; Department of Epigenetics and Molecular Carcinogenesis, Center for Cancer Epigenetics, The University of Texas MD Anderson Cancer Center, Houston, Texas, 77030, USA.
  • Wen H; Department of Epigenetics and Molecular Carcinogenesis, Center for Cancer Epigenetics, The University of Texas MD Anderson Cancer Center, Houston, Texas, 77030, USA.
  • Li W; Department of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado, 80045, USA.
  • Kutateladze TG; Department of Epigenetics and Molecular Carcinogenesis, Center for Cancer Epigenetics, The University of Texas MD Anderson Cancer Center, Houston, Texas, 77030, USA.
  • Shi X; Center for Epigenetics, Van Andel Research Institute, Grand Rapids, Michigan, 49503, USA.
Nat Commun ; 9(1): 3759, 2018 09 14.
Article en En | MEDLINE | ID: mdl-30217978
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.
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Factores de Transcripción / Histonas / Activación Transcripcional / Código de Histonas / Proteínas de Unión al ADN / Histona Acetiltransferasas Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Año: 2018 Tipo del documento: Article
Texto completo
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Factores de Transcripción / Histonas / Activación Transcripcional / Código de Histonas / Proteínas de Unión al ADN / Histona Acetiltransferasas Tipo de estudio: Prognostic_studies Límite: Humans Idioma: En Año: 2018 Tipo del documento: Article