C-terminal acidic domain of histone chaperone human NAP1 is an efficient binding assistant for histone H2A-H2B, but not H3-H4

Hideaki Ohtomo, Satoko Akashi, Yoshihito Moriwaki, Mitsuru Okuwaki, Akihisa Osakabe, Kyosuke Nagata, Hitoshi Kurumizaka, Yoshifumi Nishimura*

*この研究の対応する著者

    研究成果: Article査読

    15 被引用数 (Scopus)

    抄録

    Nucleosome assembly protein 1 (NAP1) binds both the (H3-H4)2 tetramer and two H2A-H2B dimers, mediating their sequential deposition on DNA. NAP1 contains a C-terminal acidic domain (CTAD) and a core domain that promotes dimer formation. Here, we have investigated the roles of the core domain and CTAD of human NAP1 in binding to H2A-H2B and H3-H4 by isothermal calorimetry and native mass spectrometry and compared them with the roles of yeast NAP1. We show that the hNAP1 and yNAP1 dimers bind H2A-H2B by two different modes: a strong endothermic interaction and a weak exothermic interaction. A mutant hNAP1, but not yNAP1, dimer lacking CTAD loses the exothermic interaction and shows greatly reduced H2A-H2B binding activity. The isolated CTAD of hNAP1 binds H2A-H2B only exothermically with relatively stronger binding as compared with the exothermic interaction observed for the full-length hNAP1 dimer. Thus, the two CTADs in the hNAP1 dimer seem to provide binding assistance for the strong endothermic interaction of the core domain with H2A-H2B. By contrast, in the relatively weaker binding of hNAP1 to H3-H4 as compared with yNAP1, CTAD of hNAP1 has no significant role. To our knowledge, this is the first distinct role identified for the hNAP1 CTAD.

    本文言語English
    ページ(範囲)252-263
    ページ数12
    ジャーナルGenes to Cells
    21
    3
    DOI
    出版ステータスPublished - 2016 3 1

    ASJC Scopus subject areas

    • 遺伝学
    • 細胞生物学

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