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首页> 外文期刊>Nature >ANP32E is a histone chaperone that removes H2A.Z from chromatin
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ANP32E is a histone chaperone that removes H2A.Z from chromatin

机译：ANP32E是一种组蛋白伴侣，可从染色质中去除H2A.Z

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摘要

组蛋白H2A．Z是组蛋白H2A（真核细胞的染色rn质中所存在的标准组蛋白之一）的一个变体。rnH2A．Z在转录和其他细胞核过程中有重要功rn能。在这篇论文中，Ali Hamiche及同事发现rn人蛋白ANP32E是一个H2A.Z伴侣，能够促使rnH2A．Z从染色质中被清除。生化和结构数据rn指出了ANP32E识别和驱赶H2A．Z的分子基rn础，而全基因组图谱分析则揭示了ANP32Ern是怎样调控H2A．Z在基因组重要调控区域中rn之存在的。%H2A.Z is an essential histone variant implicated in the regulation of key nuclear events. However, the metazoan chaperones responsible for H2A.Z deposition and its removal from chromatin remain unknown. Here we report the identification and characterization of the human protein ANP32E as a specific H2A.Z chaperone. We show that ANP32E is a member of the presumed H2A.Z histone-exchange complex p400/TIP60. ANP32E interacts with a short region of the docking domain of H2A.Z through a new motif termed H2A.Z interacting domain (ZID). The 1.48 A resolution crystal structure of the complex formed between the ANP32E-ZID and the H2A.Z/H2B dimer and biochemical data support an underlying molecular mechanism for H2A.Z/H2B eviction from the nucleosome and its stabilization by ANP32E through a specific extension of the H2A.Z carboxy-terminal α-helix. Finally, analysis of H2A.Z localization in ANP32E~(-/-) cells by chromatin immunoprecipitation followed by sequencing shows genome-wide enrichment, redistribution and accumulation of H2A.Z at specific chromatin control regions, in particular at enhancers and insulators.
机译：组蛋白H2A．Z是组蛋白H2A（真核细胞的染色rn质中所存在的标准组蛋白之一）的一个变体。rnH2A．Z在转录和其他细胞核过程中有重要功rn能。在这篇论文中，Ali Hamiche及同事发现rn人蛋白ANP32E是一个H2A.Z伴侣，能够促使rnH2A．Z从染色质中被清除。生化和结构数据rn指出了ANP32E识别和驱赶H2A．Z的分子基rn础，而全基因组图谱分析则揭示了ANP32Ern是怎样调控H2A．Z在基因组重要调控区域中rn之存在的。%H2A.Z is an essential histone variant implicated in the regulation of key nuclear events. However, the metazoan chaperones responsible for H2A.Z deposition and its removal from chromatin remain unknown. Here we report the identification and characterization of the human protein ANP32E as a specific H2A.Z chaperone. We show that ANP32E is a member of the presumed H2A.Z histone-exchange complex p400/TIP60. ANP32E interacts with a short region of the docking domain of H2A.Z through a new motif termed H2A.Z interacting domain (ZID). The 1.48 A resolution crystal structure of the complex formed between the ANP32E-ZID and the H2A.Z/H2B dimer and biochemical data support an underlying molecular mechanism for H2A.Z/H2B eviction from the nucleosome and its stabilization by ANP32E through a specific extension of the H2A.Z carboxy-terminal α-helix. Finally, analysis of H2A.Z localization in ANP32E~(-/-) cells by chromatin immunoprecipitation followed by sequencing shows genome-wide enrichment, redistribution and accumulation of H2A.Z at specific chromatin control regions, in particular at enhancers and insulators.

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  • 来源
    《Nature》 |2014年第7485期|648-653a11|共7页
  • 作者

    Arnaud Obri; Khalid Ouararhni; Christophe Papin; Marie-Laure Diebold; Kiran Padmanabhan; Martin Marek; Isabelle Stoll; Ludovic Roy; Patrick T. Reilly; Tak W. Mak; Stefan Dimitrov; Christophe Romier; Ali Hamiche;

  • 作者单位

    Departement de Genomique Fonctionnelle et Cancer, Institut de Genetique et Biologie Moleculaire et Cellulaire (IGBMC), Universite de Strasbourg, CNRS, INSERM, 1 rue Laurent Fries, BP. 10142, 67404 Illkirch Cedex, France;

    Departement de Genomique Fonctionnelle et Cancer, Institut de Genetique et Biologie Moleculaire et Cellulaire (IGBMC), Universite de Strasbourg, CNRS, INSERM, 1 rue Laurent Fries, BP. 10142, 67404 Illkirch Cedex, France;

    Departement de Genomique Fonctionnelle et Cancer, Institut de Genetique et Biologie Moleculaire et Cellulaire (IGBMC), Universite de Strasbourg, CNRS, INSERM, 1 rue Laurent Fries, BP. 10142, 67404 Illkirch Cedex, France;

    Departement de Biologie Structurale Integrative, Institut de Genetique et Biologie Moleculaire et Cellulaire (IGBMC), Universite de Strasbourg, CNRS, INSERM, 1 rue Laurent Fries, BP. 10142,67404 Illkirch Cedex, France;

    Equipe labelisee Ligue contre le Cancer, INSERM/Universite Joseph Fourier, Institut Albert Bonniot, U823, Site Sante-BP 170,38042 Grenoble Cedex 9, France;

    Departement de Biologie Structurale Integrative, Institut de Genetique et Biologie Moleculaire et Cellulaire (IGBMC), Universite de Strasbourg, CNRS, INSERM, 1 rue Laurent Fries, BP. 10142,67404 Illkirch Cedex, France;

    Departement de Genomique Fonctionnelle et Cancer, Institut de Genetique et Biologie Moleculaire et Cellulaire (IGBMC), Universite de Strasbourg, CNRS, INSERM, 1 rue Laurent Fries, BP. 10142, 67404 Illkirch Cedex, France;

    Departement de Genomique Fonctionnelle et Cancer, Institut de Genetique et Biologie Moleculaire et Cellulaire (IGBMC), Universite de Strasbourg, CNRS, INSERM, 1 rue Laurent Fries, BP. 10142, 67404 Illkirch Cedex, France;

    Laboratory of Inflammation Biology, Division of Cellular and Molecular Research, National Cancer Centre, Singapore, Singapore;

    Laboratory of Inflammation Biology, Division of Cellular and Molecular Research, National Cancer Centre, Singapore, Singapore,The Campbell Family Institute for Breast Cancer Research, University Health Network, Toronto, Ontario, Canada;

    Equipe labelisee Ligue contre le Cancer, INSERM/Universite Joseph Fourier, Institut Albert Bonniot, U823, Site Sante-BP 170,38042 Grenoble Cedex 9, France;

    Departement de Biologie Structurale Integrative, Institut de Genetique et Biologie Moleculaire et Cellulaire (IGBMC), Universite de Strasbourg, CNRS, INSERM, 1 rue Laurent Fries, BP. 10142,67404 Illkirch Cedex, France;

    Departement de Genomique Fonctionnelle et Cancer, Institut de Genetique et Biologie Moleculaire et Cellulaire (IGBMC), Universite de Strasbourg, CNRS, INSERM, 1 rue Laurent Fries, BP. 10142, 67404 Illkirch Cedex, France;

  • 收录信息 美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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