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Deubiquitylation of histone H2A activates transcriptional initiation via trans-histone cross-talk with H3K4 di- and trimethylation.

Deubiquitylation of histone H2A activates transcriptional initiation via trans-histone cross-talk with H3K4 di- and trimethylation. Research Abstract Details 

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  • Deubiquitylation of histone H2A activates transcriptional initiation via trans-histone cross-talk with H3K4 di- and trimethylation. Abstract Text:

    takeya nakagawaTakeya Nakagawa,takuya kajitaniTakuya Kajitani,shinji togoShinji Togo,norio masukoNorio Masuko,hideki ohdanHideki Ohdan,yoshitaka hishikawaYoshitaka Hishikawa,takehiko kojiTakehiko Koji,toshifumi matsuyamaToshifumi Matsuyama,tsuyoshi ikuraTsuyoshi Ikura,masami muramatsuMasami Muramatsu,takashi itoTakashi Ito,takeya nakagawaTakeya Nakagawa,takuya kajitaniTakuya Kajitani,shinji togoShinji Togo,norio masukoNorio Masuko,hideki ohdanHideki Ohdan,yoshitaka hishikawaYoshitaka Hishikawa,takehiko kojiTakehiko Koji,toshifumi matsuyamaToshifumi Matsuyama,tsuyoshi ikuraTsuyoshi Ikura,masami muramatsuMasami Muramatsu,takashi itoTakashi Ito,

    Transcriptional initiation is a key step in the control of mRNA synthesis and is intimately related to chromatin structure and histone modification. Here, we show that the ubiquitylation of H2A (ubH2A) correlates with silent chromatin and regulates transcriptional initiation. The levels of ubH2A vary during hepatocyte regeneration, and based on microarray expression data from regenerating liver, we identified USP21, a ubiquitin-specific protease that catalyzes the hydrolysis of ubH2A. When chromatin is assembled in vitro, ubH2A, but not H2A, specifically represses the di- and trimethylation of H3K4. USP21 relieves this ubH2A-specific repression. In addition, in vitro transcription analysis revealed that ubH2A represses transcriptional initiation, but not transcriptional elongation, by inhibiting H3K4 methylation. Notably, ubH2A-mediated repression was not observed when H3 Lys 4 was changed to arginine. Furthermore, overexpression of USP21 in the liver up-regulates a gene that is normally down-regulated during hepatocyte regeneration. Our studies revealed a novel mode of trans-histone cross-talk, in which H2A ubiquitylation controls the di- and trimethylation of H3K4, resulting in regulation of transcriptional initiation.

    Deubiquitylation of histone H2A activates transcriptional initiation via trans-histone cross-talk with H3K4 di- and trimethylation. Publishing Authors By Initials

    t nakagawaT Nakagawa,t kajitaniT Kajitani,s togoS Togo,n masukoN Masuko,h ohdanH Ohdan,y hishikawaY Hishikawa,t kojiT Koji,t matsuyamaT Matsuyama,t ikuraT Ikura,m muramatsuM Muramatsu,t itoT Ito,t nakagawaT Nakagawa,t kajitaniT Kajitani,s togoS Togo,n masukoN Masuko,h ohdanH Ohdan,y hishikawaY Hishikawa,t kojiT Koji,t matsuyamaT Matsuyama,t ikuraT Ikura,m muramatsuM Muramatsu,t itoT Ito,

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    Deubiquitylation of histone H2A activates transcriptional initiation via trans-histone cross-talk with H3K4 di- and trimethylation. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Genes & development

    VOLUME: 22

    Page Numbers: 37-49

    Journal Abbreviation: Genes Dev.

    ISSN: 0890-9369

    DAY: 1

    MONTH: Jan

    YEAR: 2008

    Deubiquitylation of histone H2A activates transcriptional initiation via trans-histone cross-talk with H3K4 di- and trimethylation. Information

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    LANGUAGE: eng

    NlmUniqueID: 8711660

    Deubiquitylation of histone H2A activates transcriptional initiation via trans-histone cross-talk with H3K4 di- and trimethylation. Keywords Mesh Terms:

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    Grant and Affiliation Information for Deubiquitylation of histone H2A activates transcriptional initiation via trans-histone cross-talk with H3K4 di- and trimethylation.

    AFFILIATION: Nagasaki University School of Medicine, Nagasaki 852-8523, Japan;

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: Genes Dev

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