Structures of human nucleosomes containing major histone H3 variants

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

*この研究の対応する著者

    研究成果: Article査読

    80 被引用数 (Scopus)

    抄録

    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.

    本文言語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
    6
    DOI
    出版ステータスPublished - 2011 6月

    ASJC Scopus subject areas

    • 構造生物学

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