Covalent Modifications of Histone H3K9 Promote Binding of CHD3
Summary: Chromatin remodeling is required for genome function and is facilitated by ATP-dependent complexes, such as nucleosome remodeling and deacetylase (NuRD). Among its core components is the chromodomain helicase DNA binding protein 3 (CHD3) whose functional significance is not well established...
| Main Authors: | , , , , , , , , , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2017-10-01
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| Series: | Cell Reports |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S221112471731344X |
| _version_ | 1818256463175352320 |
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| author | Adam H. Tencer Khan L. Cox Luo Di Joseph B. Bridgers Jie Lyu Xiaodong Wang Jennifer K. Sims Tyler M. Weaver Hillary F. Allen Yi Zhang Jovylyn Gatchalian Michael A. Darcy Matthew D. Gibson Jinzen Ikebe Wei Li Paul A. Wade Jeffrey J. Hayes Brian D. Strahl Hidetoshi Kono Michael G. Poirier Catherine A. Musselman Tatiana G. Kutateladze |
| author_facet | Adam H. Tencer Khan L. Cox Luo Di Joseph B. Bridgers Jie Lyu Xiaodong Wang Jennifer K. Sims Tyler M. Weaver Hillary F. Allen Yi Zhang Jovylyn Gatchalian Michael A. Darcy Matthew D. Gibson Jinzen Ikebe Wei Li Paul A. Wade Jeffrey J. Hayes Brian D. Strahl Hidetoshi Kono Michael G. Poirier Catherine A. Musselman Tatiana G. Kutateladze |
| author_sort | Adam H. Tencer |
| collection | DOAJ |
| description | Summary: Chromatin remodeling is required for genome function and is facilitated by ATP-dependent complexes, such as nucleosome remodeling and deacetylase (NuRD). Among its core components is the chromodomain helicase DNA binding protein 3 (CHD3) whose functional significance is not well established. Here, we show that CHD3 co-localizes with the other NuRD subunits, including HDAC1, near the H3K9ac-enriched promoters of the NuRD target genes. The tandem PHD fingers of CHD3 bind histone H3 tails and posttranslational modifications that increase hydrophobicity of H3K9—methylation or acetylation (H3K9me3 or H3K9ac)—enhance this interaction. Binding of CHD3 PHDs promotes H3K9Cme3-nucleosome unwrapping in vitro and perturbs the pericentric heterochromatin structure in vivo. Methylation or acetylation of H3K9 uniquely alleviates the intra-nucleosomal interaction of histone H3 tails, increasing H3K9 accessibility. Collectively, our data suggest that the targeting of covalently modified H3K9 by CHD3 might be essential in diverse functions of NuRD. : Tencer et al. find that CHD3 co-localizes with the other subunits of the NuRD complex and H3K9ac at NuRD target genes. The authors further demonstrate that the PHD fingers of CHD3 associate with histone H3 tails, and this association is augmented through methylation or acetylation of H3K9. Keywords: CHD3, NuRD, PHD finger, H3K9me3, H3K9ac, histone, chromatin |
| first_indexed | 2024-12-12T17:28:09Z |
| format | Article |
| id | doaj.art-7ca566c3011e443687e83fac93b1d9f8 |
| institution | Directory Open Access Journal |
| issn | 2211-1247 |
| language | English |
| last_indexed | 2024-12-12T17:28:09Z |
| publishDate | 2017-10-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj.art-7ca566c3011e443687e83fac93b1d9f82022-12-22T00:17:27ZengElsevierCell Reports2211-12472017-10-01212455466Covalent Modifications of Histone H3K9 Promote Binding of CHD3Adam H. Tencer0Khan L. Cox1Luo Di2Joseph B. Bridgers3Jie Lyu4Xiaodong Wang5Jennifer K. Sims6Tyler M. Weaver7Hillary F. Allen8Yi Zhang9Jovylyn Gatchalian10Michael A. Darcy11Matthew D. Gibson12Jinzen Ikebe13Wei Li14Paul A. Wade15Jeffrey J. Hayes16Brian D. Strahl17Hidetoshi Kono18Michael G. Poirier19Catherine A. Musselman20Tatiana G. Kutateladze21Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USADepartment of Physics, Ohio State University, Columbus, OH 43210, USAMolecular Modeling and Simulation Group, National Institutes for Quantum and Radiological Science and Technology, Kizugawa, Kyoto 619 0215, JapanDepartment of Biochemistry and Biophysics and the Lineberger Comprehensive Cancer Center, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USADan L. Duncan Cancer Center, Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USADepartment of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, NY 14642, USALaboratory of Molecular Carcinogenesis, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709, USADepartment of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242, USADepartment of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USADepartment of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USADepartment of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USADepartment of Physics, Ohio State University, Columbus, OH 43210, USADepartment of Physics, Ohio State University, Columbus, OH 43210, USAMolecular Modeling and Simulation Group, National Institutes for Quantum and Radiological Science and Technology, Kizugawa, Kyoto 619 0215, JapanDan L. Duncan Cancer Center, Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USALaboratory of Molecular Carcinogenesis, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709, USADepartment of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, NY 14642, USADepartment of Biochemistry and Biophysics and the Lineberger Comprehensive Cancer Center, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USAMolecular Modeling and Simulation Group, National Institutes for Quantum and Radiological Science and Technology, Kizugawa, Kyoto 619 0215, JapanDepartment of Physics, Ohio State University, Columbus, OH 43210, USA; Corresponding authorDepartment of Biochemistry, University of Iowa College of Medicine, Iowa City, IA 52242, USA; Corresponding authorDepartment of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA; Corresponding authorSummary: Chromatin remodeling is required for genome function and is facilitated by ATP-dependent complexes, such as nucleosome remodeling and deacetylase (NuRD). Among its core components is the chromodomain helicase DNA binding protein 3 (CHD3) whose functional significance is not well established. Here, we show that CHD3 co-localizes with the other NuRD subunits, including HDAC1, near the H3K9ac-enriched promoters of the NuRD target genes. The tandem PHD fingers of CHD3 bind histone H3 tails and posttranslational modifications that increase hydrophobicity of H3K9—methylation or acetylation (H3K9me3 or H3K9ac)—enhance this interaction. Binding of CHD3 PHDs promotes H3K9Cme3-nucleosome unwrapping in vitro and perturbs the pericentric heterochromatin structure in vivo. Methylation or acetylation of H3K9 uniquely alleviates the intra-nucleosomal interaction of histone H3 tails, increasing H3K9 accessibility. Collectively, our data suggest that the targeting of covalently modified H3K9 by CHD3 might be essential in diverse functions of NuRD. : Tencer et al. find that CHD3 co-localizes with the other subunits of the NuRD complex and H3K9ac at NuRD target genes. The authors further demonstrate that the PHD fingers of CHD3 associate with histone H3 tails, and this association is augmented through methylation or acetylation of H3K9. Keywords: CHD3, NuRD, PHD finger, H3K9me3, H3K9ac, histone, chromatinhttp://www.sciencedirect.com/science/article/pii/S221112471731344X |
| spellingShingle | Adam H. Tencer Khan L. Cox Luo Di Joseph B. Bridgers Jie Lyu Xiaodong Wang Jennifer K. Sims Tyler M. Weaver Hillary F. Allen Yi Zhang Jovylyn Gatchalian Michael A. Darcy Matthew D. Gibson Jinzen Ikebe Wei Li Paul A. Wade Jeffrey J. Hayes Brian D. Strahl Hidetoshi Kono Michael G. Poirier Catherine A. Musselman Tatiana G. Kutateladze Covalent Modifications of Histone H3K9 Promote Binding of CHD3 Cell Reports |
| title | Covalent Modifications of Histone H3K9 Promote Binding of CHD3 |
| title_full | Covalent Modifications of Histone H3K9 Promote Binding of CHD3 |
| title_fullStr | Covalent Modifications of Histone H3K9 Promote Binding of CHD3 |
| title_full_unstemmed | Covalent Modifications of Histone H3K9 Promote Binding of CHD3 |
| title_short | Covalent Modifications of Histone H3K9 Promote Binding of CHD3 |
| title_sort | covalent modifications of histone h3k9 promote binding of chd3 |
| url | http://www.sciencedirect.com/science/article/pii/S221112471731344X |
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