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Free energy profile of eviction of H2A/H2B dimer from nucleosome

https://repo.qst.go.jp/records/77819
https://repo.qst.go.jp/records/77819
cd73cad6-e6fc-4eed-9c7e-7e32985862c3
Item type 会議発表用資料 / Presentation(1)
公開日 2019-10-24
タイトル
タイトル Free energy profile of eviction of H2A/H2B dimer from nucleosome
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_c94f
資源タイプ conference object
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 Ishida, Hisashi

× Ishida, Hisashi

WEKO 820765

Ishida, Hisashi

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Kono, Hidetoshi

× Kono, Hidetoshi

WEKO 820766

Kono, Hidetoshi

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Ishida, Hisashi

× Ishida, Hisashi

WEKO 820767

en Ishida, Hisashi

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Kono, Hidetoshi

× Kono, Hidetoshi

WEKO 820768

en Kono, Hidetoshi

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抄録
内容記述タイプ Abstract
内容記述 Nucleosome is the fundamental structural unit of chromatin and is composed of histone proteins and DNA. The individual core histones form the stable dimers of H2A/H2B and H3/H4. The H3/H4 dimers further assemble into a tetramer. In the nucleosome the H3/H4 tetramer and two H2A/H2B dimers form an octamer. The nucleosome undergoes structural changes such as DNA unwrapping and the eviction of the H2A/H2B dimer in cellular processes.
To understand how the eviction of the H2A/H2B dimer occurs, an adaptively biased molecular dynamics (ABMD) simulation was carried out with a reaction coordinate, d, which is the distance between the two H2A/H2B dimers. In the process, the interaction between the two H2As was firstly lost at d = ~40 Å. The interaction between the (H2A/H2B)a dimer and (H3/H4)a dimer then started to break. The docking domain of the H2A strongly interacted with the (H3/H4) a dimer until the interaction was lost at d = ~50 Å. This indicates that the docking domain of the H2A plays an important role in stabilizing the nucleosome and blocking the eviction of the H2A/H2B dimer. In fact, the chromatin remodeling histone chaperone FACT is known to move the docking domain away from the nucleosome. Thus, the loss of interaction with this domain would significantly facilitate the eviction of the H2A/H2B dimer. In addition to the (H2A/H2B)a – (H3/H4)a interaction, the (H2A/H2B)a – (H3/H4)b interaction was also found to be strong. We will discuss the important regions of the nucleosome for the eviction in detail.
会議概要(会議名, 開催地, 会期, 主催者等)
内容記述タイプ Other
内容記述 3rd QST International Symposium
発表年月日
日付 2019-12-04
日付タイプ Issued
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