Distinct features of the histone core structure in nucleosomes containing the histone h2a.b variant

Masaaki Sugiyama, Yasuhiro Arimura, Kazuyoshi Shirayama, Risa Fujita, Yojiro Oba, Nobuhiro Sato, Rintaro Inoue, Takashi Oda, Mamoru Sato, Richard K. Heenan, Hitoshi Kurumizaka

    Research output: Contribution to journalArticle

    14 Citations (Scopus)

    Abstract

    Nucleosomes containing a human histone variant, H2A.B, in an aqueous solution were analyzed by small-angle neutron scattering utilizing a contrast variation technique. Comparisons with the canonical H2A nucleosome structure revealed that the DNA termini of the H2A.B nucleosome are detached from the histone core surface, and flexibly expanded toward the solvent. In contrast, the histone tails are compacted in H2A.B nucleosomes compared to those in canonical H2A nucleosomes, suggesting that they bind to the surface of the histone core and/or DNA. Therefore, the histone tail dynamics may function to regulate the flexibility of the DNA termini in the nucleosomes.

    Original languageEnglish
    Pages (from-to)2206-2213
    Number of pages8
    JournalBiophysical Journal
    Volume106
    Issue number10
    DOIs
    Publication statusPublished - 2014 May 20

    ASJC Scopus subject areas

    • Biophysics
    • Medicine(all)

    Fingerprint Dive into the research topics of 'Distinct features of the histone core structure in nucleosomes containing the histone h2a.b variant'. Together they form a unique fingerprint.

  • Cite this

    Sugiyama, M., Arimura, Y., Shirayama, K., Fujita, R., Oba, Y., Sato, N., Inoue, R., Oda, T., Sato, M., Heenan, R. K., & Kurumizaka, H. (2014). Distinct features of the histone core structure in nucleosomes containing the histone h2a.b variant. Biophysical Journal, 106(10), 2206-2213. https://doi.org/10.1016/j.bpj.2014.04.007