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  1. D300 大学院環境学研究科
  2. D300a 雑誌掲載論文
  3. 学術雑誌

Compaction and self-association of megabase-sized chromatin are induced by anionic protein crowding

http://hdl.handle.net/2237/00032654
http://hdl.handle.net/2237/00032654
80792611-41ef-4981-be59-14e490bca652
名前 / ファイル ライセンス アクション
Zinchenko_2020_Soft_Matter_Accepted_Manuscript.pdf Zinchenko_2020_Soft_Matter_Accepted_Manuscript (651.7 kB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2020-09-25
タイトル
タイトル Compaction and self-association of megabase-sized chromatin are induced by anionic protein crowding
言語 en
著者 Zinchenko, Anatoly

× Zinchenko, Anatoly

WEKO 101366

en Zinchenko, Anatoly

Search repository
Chen, Qinming

× Chen, Qinming

WEKO 101367

en Chen, Qinming

Search repository
Berezhnoy, Nikolay V.

× Berezhnoy, Nikolay V.

WEKO 101368

en Berezhnoy, Nikolay V.

Search repository
Wang, Sai

× Wang, Sai

WEKO 101369

en Wang, Sai

Search repository
Nordenskiöld, Lars

× Nordenskiöld, Lars

WEKO 101370

en Nordenskiöld, Lars

Search repository
アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
抄録
内容記述 Highly compacted chromatin, a complex of DNA with cationic histone proteins, is found in the nucleus of eukaryotic cells in an environment with a high concentration of macromolecular species, many of which possess a negative charge. In the majority of previous studies, however, these crowding conditions were experimentally modelled using neutral synthetic macromolecules such as polyethylene glycol (PEG). Despite the importance of the crowding agent charge in the condensation process of chromatin, to the best of our knowledge, the behavior of chromatin under conditions of anionic protein crowding has not been studied. Here, compaction of nearly megabase-long chromatin in the presence of the anionic globular protein BSA was investigated by single-molecule fluorescent microscopy (FM). We demonstrate different effects of anionic macromolecular crowders (MMCs) on DNA and chromatin, compared to neutral MMCs. While DNA molecules undergo gradual compaction into a globular form in the presence of ca. 20% w/v of BSA, chromatin fibres complete coil to globule transition at a much lower concentration of BSA (ca. 5% w/v). Furthermore, at higher concentrations of BSA in solution (>5% w/v), chromatin fibres self-associate and form large spherical or fibrillar supramolecular microstructures characterized by a high colloidal stability and dynamic intermolecular fluctuations. Formation of such self-organized colloids from chromatin is universal and characteristic of chromatin fibres of various lengths. Our results highlight the hitherto underappreciated effect of anionic MMC environment on chromatin higher-order structures that may play an important role in self-organization of chromatin in vivo.
言語 en
内容記述タイプ Abstract
内容記述
内容記述 ファイル公開:2021/05/14
言語 ja
内容記述タイプ Other
出版者
言語 en
出版者 Royal Society of Chemistry
言語
言語 eng
資源タイプ
資源タイプresource http://purl.org/coar/resource_type/c_6501
タイプ journal article
出版タイプ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
DOI
関連タイプ isVersionOf
識別子タイプ DOI
関連識別子 https://doi.org/10.1039/D0SM00162G
ISSN(print)
収録物識別子タイプ PISSN
収録物識別子 1744-683X
書誌情報 en : Soft Matter

巻 16, 号 18, p. 4366-4372, 発行日 2020-05-14
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