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dc.contributor.authorSugiyama, Masaakien
dc.contributor.authorHorikoshi, Naokien
dc.contributor.authorSuzuki, Yuyaen
dc.contributor.authorTaguchi, Hiroyukien
dc.contributor.authorKujirai, Tomoyaen
dc.contributor.authorInoue, Rintaroen
dc.contributor.authorOba, Yojiroen
dc.contributor.authorSato, Nobuhiroen
dc.contributor.authorMartel, Anneen
dc.contributor.authorPorcar, Lionelen
dc.contributor.authorKurumizaka, Hitoshien
dc.contributor.alternative杉山, 正明ja
dc.contributor.alternative大場, 洋次郎ja
dc.date.accessioned2016-12-05T02:35:19Z-
dc.date.available2016-12-05T02:35:19Z-
dc.date.issued2015-12-
dc.identifier.issn2405-5808-
dc.identifier.urihttp://hdl.handle.net/2433/217459-
dc.description.abstractSolution 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.en
dc.format.mimetypeapplication/pdf-
dc.language.isoeng-
dc.publisherElsevier BVen
dc.rights© 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/).en
dc.subjectNucleosomeen
dc.subjectH2A.Z.1en
dc.subjectSmall-angle X-ray scatteringen
dc.subjectSmall-angle neutron scatteringen
dc.subjectContrast variationen
dc.subjectStuhrmann ploten
dc.titleSolution Structure of Variant H2A.Z.1 Nucleosome Investigated by Small-Angle X-ray and Neutron Scatteringsen
dc.typejournal article-
dc.type.niitypeJournal Article-
dc.identifier.jtitleBiochemistry and Biophysics Reportsen
dc.identifier.volume4-
dc.identifier.spage28-
dc.identifier.epage32-
dc.relation.doi10.1016/j.bbrep.2015.08.019-
dc.textversionpublisher-
dc.identifier.pmid29124184-
dcterms.accessRightsopen access-
dc.identifier.eissn2405-5808-
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