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

    Research output: Contribution to journalArticle

    8 Citations (Scopus)

    Abstract

    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.

    Original languageEnglish
    Pages (from-to)252-263
    Number of pages12
    JournalGenes to Cells
    Volume21
    Issue number3
    DOIs
    Publication statusPublished - 2016 Mar 1

    Fingerprint

    Nucleosome Assembly Protein 1
    Histone Chaperones
    Histones
    Calorimetry
    Mass Spectrometry
    Yeasts
    DNA

    ASJC Scopus subject areas

    • Genetics
    • Cell Biology

    Cite this

    Ohtomo, H., Akashi, S., Moriwaki, Y., Okuwaki, M., Osakabe, A., Nagata, K., ... Nishimura, Y. (2016). C-terminal acidic domain of histone chaperone human NAP1 is an efficient binding assistant for histone H2A-H2B, but not H3-H4. Genes to Cells, 21(3), 252-263. https://doi.org/10.1111/gtc.12339

    C-terminal acidic domain of histone chaperone human NAP1 is an efficient binding assistant for histone H2A-H2B, but not H3-H4. / Ohtomo, Hideaki; Akashi, Satoko; Moriwaki, Yoshihito; Okuwaki, Mitsuru; Osakabe, Akihisa; Nagata, Kyosuke; Kurumizaka, Hitoshi; Nishimura, Yoshifumi.

    In: Genes to Cells, Vol. 21, No. 3, 01.03.2016, p. 252-263.

    Research output: Contribution to journalArticle

    Ohtomo, H, Akashi, S, Moriwaki, Y, Okuwaki, M, Osakabe, A, Nagata, K, Kurumizaka, H & Nishimura, Y 2016, 'C-terminal acidic domain of histone chaperone human NAP1 is an efficient binding assistant for histone H2A-H2B, but not H3-H4', Genes to Cells, vol. 21, no. 3, pp. 252-263. https://doi.org/10.1111/gtc.12339
    Ohtomo, Hideaki ; Akashi, Satoko ; Moriwaki, Yoshihito ; Okuwaki, Mitsuru ; Osakabe, Akihisa ; Nagata, Kyosuke ; Kurumizaka, Hitoshi ; Nishimura, Yoshifumi. / C-terminal acidic domain of histone chaperone human NAP1 is an efficient binding assistant for histone H2A-H2B, but not H3-H4. In: Genes to Cells. 2016 ; Vol. 21, No. 3. pp. 252-263.
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    AU - Okuwaki, Mitsuru

    AU - Osakabe, Akihisa

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