Human tNASP promotes in vitro nucleosome assembly with histone H3.3

Daiki Kato, Akihisa Osakabe, Hiroaki Tachiwana, Hiroki Tanaka, Hitoshi Kurumizaka*

*この研究の対応する著者

    研究成果: Article査読

    11 被引用数 (Scopus)

    抄録

    Nuclear autoantigenic sperm proteins (NASPs) are members of the acidic histone chaperones, which promote nucleosome assembly. In humans, two splicing variants proposed for the somatic and testicular isoforms, sNASP and tNASP, respectively, have been found, and the shorter form, sNASP, reportedly promotes nucleosome assembly with the histone H3 isoforms, H3.1, H3.2, and H3.3. However, the biochemical properties of the longer form, tNASP, have not been reported. tNASP is considered to exist specifically in the testis. Our present results revealed that the tNASP protein is ubiquitously produced in various human tissues, in addition to testis. Unexpectedly, we found that the nucleosome assembly activity of purified tNASP was extremely low with the canonical histone H3.1 or H3.2, but was substantially detected with the replacement histone H3.3 variant. A mutational analysis revealed that the H3.3 Ile89 residue, corresponding to the H3.1 Val89 residue, is responsible for the tNASP-mediated nucleosome assembly with H3.3. A histone deposition assay showed that the H3.3-H4 complex is more efficiently deposited onto DNA by tNASP than the H3.1-H4 complex. These results provide evidence that tNASP is ubiquitously produced in various types of human tissues and promotes in vitro nucleosome assembly with H3 variant specificity.

    本文言語English
    ページ(範囲)1171-1179
    ページ数9
    ジャーナルBiochemistry
    54
    5
    DOI
    出版ステータスPublished - 2015 2月 10

    ASJC Scopus subject areas

    • 生化学

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