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タイトル: Solution Structure of Variant H2A.Z.1 Nucleosome Investigated by Small-Angle X-ray and Neutron Scatterings
著者: Sugiyama, Masaaki
Horikoshi, Naoki
Suzuki, Yuya
Taguchi, Hiroyuki
Kujirai, Tomoya
Inoue, Rintaro  kyouindb  KAKEN_id
Oba, Yojiro  KAKEN_id
Sato, Nobuhiro  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0002-6960-6567 (unconfirmed)
Martel, Anne
Porcar, Lionel
Kurumizaka, Hitoshi
著者名の別形: 杉山, 正明
大場, 洋次郎
キーワード: Nucleosome
H2A.Z.1
Small-angle X-ray scattering
Small-angle neutron scattering
Contrast variation
Stuhrmann plot
発行日: Dec-2015
出版者: Elsevier BV
誌名: Biochemistry and Biophysics Reports
巻: 4
開始ページ: 28
終了ページ: 32
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.
著作権等: © 2015 The Authors. Published by Elsevier B.V. This is an open access article under the CCBY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
URI: http://hdl.handle.net/2433/217459
DOI(出版社版): 10.1016/j.bbrep.2015.08.019
PubMed ID: 29124184
出現コレクション:学術雑誌掲載論文等

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