Structures of human nucleosomes containing major histone H3 variants

Hiroaki Tachiwana, Akihisa Osakabe, Tatsuya Shiga, Yuta Miya, Hiroshi Kimura, Wataru Kagawa, Hitoshi Kurumizaka

    研究成果: Article

    63 引用 (Scopus)

    抜粋

    The nucleosome is the fundamental repeating unit of chromatin, via which genomic DNA is packaged into the nucleus in eukaryotes. In the nucleosome, two copies of each core histone, H2A, H2B, H3 and H4, form a histone octamer which wraps 146 base pairs of DNA around itself. All of the core histones except for histone H4 have nonallelic isoforms called histone variants. In humans, eight histone H3 variants, H3.1, H3.2, H3.3, H3T, H3.5, H3.X, H3.Y and CENP-A, have been reported to date. Previous studies have suggested that histone H3 variants possess distinct functions in the formation of specific chromosome regions and/or in the regulation of transcription and replication. H3.1, H3.2 and H3.3 are the most abundant H3 variants. Here, crystal structures of human nucleosomes containing either H3.2 or H3.3 have been solved. The structures were essentially the same as that of the H3.1 nucleosome. Since the amino-acid residues specific for H3.2 and H3.3 are located on the accessible surface of the H3/H4 tetramer, they may be potential interaction sites for H3.2- and H3.3-specific chaperones.

    元の言語English
    ページ(範囲)578-583
    ページ数6
    ジャーナルActa Crystallographica Section D: Biological Crystallography
    67
    発行部数6
    DOI
    出版物ステータスPublished - 2011 6

    ASJC Scopus subject areas

    • Structural Biology

    フィンガープリント Structures of human nucleosomes containing major histone H3 variants' の研究トピックを掘り下げます。これらはともに一意のフィンガープリントを構成します。

  • これを引用

    Tachiwana, H., Osakabe, A., Shiga, T., Miya, Y., Kimura, H., Kagawa, W., & Kurumizaka, H. (2011). Structures of human nucleosomes containing major histone H3 variants. Acta Crystallographica Section D: Biological Crystallography, 67(6), 578-583. https://doi.org/10.1107/S0907444911014818