Structure and function of human histone H3.Y nucleosome

Tomoya Kujirai, Naoki Horikoshi, Koichi Sato, Kazumitsu Maehara, Shinichi Machida, Akihisa Osakabe, Hiroshi Kimura, Yasuyuki Ohkawa, Hitoshi Kurumizaka

    Research output: Contribution to journalArticlepeer-review

    39 Citations (Scopus)

    Abstract

    Histone H3.Y is a primate-specific, distant H3 variant. It is evolutionarily derived from H3.3, and may function in transcription regulation. However, the mechanism by which H3.Y regulates transcription has not been elucidated. In the present study, we determined the crystal structure of the H3.Y nucleosome, and found that many H3.Y-specific residues are located on the entry/exit sites of the nucleosome. Biochemical analyses revealed that the DNA ends of the H3.Y nucleosome were more flexible than those of the H3.3 nucleosome, although the H3.Y nucleosome was stable in vitro and in vivo. Interestingly, the linker histone H1, which compacts nucleosomal DNA, appears to bind to the H3.Y nucleosome less efficiently, as compared to the H3.3 nucleosome. These characteristics of the H3.Y nucleosome are also conserved in the H3.Y/H3.3 heterotypic nucleosome, which may be the predominant form in cells. In human cells, H3.Y preferentially accumulated around transcription start sites (TSSs). Taken together, H3.Y-containing nucleosomes around transcription start sites may form relaxed chromatin that allows transcription factor access, to regulate the transcription status of specific genes.

    Original languageEnglish
    Pages (from-to)6127-6141
    Number of pages15
    JournalNucleic acids research
    Volume44
    Issue number13
    DOIs
    Publication statusPublished - Jul 27 2016

    All Science Journal Classification (ASJC) codes

    • Genetics

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