Solution structure of variant H2A.Z.1 nucleosome investigated by small-angle X-ray and neutron scatterings

Masaaki Sugiyama*, Naoki Horikoshi, Yuya Suzuki, Hiroyuki Taguchi, Tomoya Kujirai, Rintaro Inoue, Yojiro Oba, Nobuhiro Sato, Anne Martel, Lionel Porcar, Hitoshi Kurumizaka

*この研究の対応する著者

研究成果査読

10 被引用数 (Scopus)

抄録

Solution structures of nucleosomes containing a human histone variant, H2A.Z.1, were measured by small-angle X-ray and neutron scatterings (SAXS and SANS). SAXS revealed that the outer shape, reflecting the DNA shape, of the H2A.Z.1 nucleosome is almost the same as that of the canonical H2A nucleosome. In contrast, SANS employing a contrast variation technique revealed that the histone octamer of the H2A.Z.1 nucleosome is smaller than that of the canonical nucleosome. The DNA within the H2A.Z.1 nucleosome was more susceptible to micrococcal nuclease than that within the canonical nucleosome. These results suggested that the DNA is loosely wrapped around the histone core in the H2A.Z.1 nucleosome.

本文言語English
論文番号75
ページ(範囲)28-32
ページ数5
ジャーナルBiochemistry and Biophysics Reports
4
DOI
出版ステータスPublished - 2015 12 1

ASJC Scopus subject areas

  • 生化学
  • 生物理学
  • 細胞生物学
  • 分子生物学

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