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Title: Solution Structure of Variant H2A.Z.1 Nucleosome Investigated by Small-Angle X-ray and Neutron Scatterings
Authors: Sugiyama, Masaaki
Horikoshi, Naoki
Suzuki, Yuya
Taguchi, Hiroyuki
Kujirai, Tomoya
Inoue, Rintaro
Oba, Yojiro  kyouindb  KAKEN_id
Sato, Nobuhiro
Martel, Anne
Porcar, Lionel
Kurumizaka, Hitoshi
Author's alias: 杉山, 正明
大場, 洋次郎
Keywords: Nucleosome
Small-angle X-ray scattering
Small-angle neutron scattering
Contrast variation
Stuhrmann plot
Issue Date: Dec-2015
Publisher: Elsevier B.V.
Journal title: Biochemistry and Biophysics Reports
Volume: 4
Start page: 28
End page: 32
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.
Rights: © 2015 The Authors. Published by Elsevier B.V. This is an open access article under the CCBY-NC-ND license (
DOI(Published Version): 10.1016/j.bbrep.2015.08.019
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