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  1. 原著論文

Structural Studies of Overlapping Dinucleosomes in Solution

https://repo.qst.go.jp/records/78475
https://repo.qst.go.jp/records/78475
504ec8d6-dc40-4e0e-bcce-e3dbab6e824b
Item type 学術雑誌論文 / Journal Article(1)
公開日 2019-08-29
タイトル
タイトル Structural Studies of Overlapping Dinucleosomes in Solution
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
アクセス権
アクセス権 metadata only access
アクセス権URI http://purl.org/coar/access_right/c_14cb
著者 Matsumoto, Atsushi

× Matsumoto, Atsushi

WEKO 868539

Matsumoto, Atsushi

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Sugiyama, Masaaki

× Sugiyama, Masaaki

WEKO 868540

Sugiyama, Masaaki

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Li, Zhenhai

× Li, Zhenhai

WEKO 868541

Li, Zhenhai

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Martel, Anne

× Martel, Anne

WEKO 868542

Martel, Anne

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Porcar, Lionel

× Porcar, Lionel

WEKO 868543

Porcar, Lionel

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Inoue, Rintaro

× Inoue, Rintaro

WEKO 868544

Inoue, Rintaro

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Kato, Daiki

× Kato, Daiki

WEKO 868545

Kato, Daiki

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Osakabe, Akihisa

× Osakabe, Akihisa

WEKO 868546

Osakabe, Akihisa

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Kurumizaka, Hitoshi

× Kurumizaka, Hitoshi

WEKO 868547

Kurumizaka, Hitoshi

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Kono, Hidetoshi

× Kono, Hidetoshi

WEKO 868548

Kono, Hidetoshi

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Matsumoto, Atsushi

× Matsumoto, Atsushi

WEKO 868549

en Matsumoto, Atsushi

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Li, Zhenhai

× Li, Zhenhai

WEKO 868550

en Li, Zhenhai

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Kono, Hidetoshi

× Kono, Hidetoshi

WEKO 868551

en Kono, Hidetoshi

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抄録
内容記述タイプ Abstract
内容記述 An overlapping dinucleosome (OLDN) is a structure composed of one hexasome and one octasome and appears to be formed through nucleosome collision promoted by nucleosome remodeling factor(s). In the present study, the solution structure of the OLDN was investigated through integration of small-angle X-ray and neutron scattering (SAXS and SANS, respectively), computer modeling, and molecular dynamics simulations. Starting from the crystal structure, we generated a conformational ensemble based on normal mode analysis, and searched for the conformations that well reproduced the SAXS and SANS scattering curves. We found that inclusion of histone tails, which are not observed in the crystal structure, greatly improved model quality. The obtained structural models suggest that OLDNs adopt a variety of conformations stabilized by histone tails situated at the interface between the hexasome and octasome, simultaneously binding to both the hexasomal and octasomal DNA. In addition, our models define a possible direction for the conformational changes or dynamics, which may provide important information that furthers our understanding of the role of chromatin dynamics in gene regulation.
書誌情報 Biophysical journal

巻 118, 号 9, p. 2209-2219, 発行日 2020-01
出版者
出版者 Cell Press
ISSN
収録物識別子タイプ ISSN
収録物識別子 0006-3495
DOI
識別子タイプ DOI
関連識別子 10.1016/j.bpj.2019.12.010
関連サイト
識別子タイプ URI
関連識別子 https://www.biorxiv.org/content/10.1101/753327v1
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