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

doi:10.1016/j.bbrep.2015.08.019

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

理工学術院総合研究所

研究成果: Article › 査読

11 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
巻	4
DOI	https://doi.org/10.1016/j.bbrep.2015.08.019
出版ステータス	Published - 2015 12月 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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10.1016/j.bbrep.2015.08.019

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

abstract = "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.",

keywords = "Contrast variation, H2A.Z.1, Nucleosome, Small-angle neutron scattering, Small-angle X-ray scattering, Stuhrmann plot",

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

year = "2015",

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doi = "10.1016/j.bbrep.2015.08.019",

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T1 - Solution structure of variant H2A.Z.1 nucleosome investigated by small-angle X-ray and neutron scatterings

AU - Sugiyama, Masaaki

AU - Horikoshi, Naoki

AU - Suzuki, Yuya

AU - Taguchi, Hiroyuki

AU - Kujirai, Tomoya

AU - Inoue, Rintaro

AU - Oba, Yojiro

AU - Sato, Nobuhiro

AU - Martel, Anne

AU - Porcar, Lionel

AU - Kurumizaka, Hitoshi

PY - 2015/12/1

Y1 - 2015/12/1

N2 - 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.

AB - 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.

KW - Contrast variation

KW - H2A.Z.1

KW - Nucleosome

KW - Small-angle neutron scattering

KW - Small-angle X-ray scattering

KW - Stuhrmann plot

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U2 - 10.1016/j.bbrep.2015.08.019

DO - 10.1016/j.bbrep.2015.08.019

M3 - Article

AN - SCOPUS:84940658170

SN - 2405-5808

VL - 4

SP - 28

EP - 32

JO - Biochemistry and Biophysics Reports

JF - Biochemistry and Biophysics Reports

M1 - 75

ER -

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

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