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  1. 原著論文

Function of homo- and hetero-oligomers of human nucleoplasmin/nucleophosmin family proteins NPM1, NPM2 and NPM3 during sperm chromatin remodeling.

https://repo.qst.go.jp/records/46657
https://repo.qst.go.jp/records/46657
192c352c-de71-4b88-92e3-9aa9bd7c4a35
Item type 学術雑誌論文 / Journal Article(1)
公開日 2013-12-04
タイトル
タイトル Function of homo- and hetero-oligomers of human nucleoplasmin/nucleophosmin family proteins NPM1, NPM2 and NPM3 during sperm chromatin remodeling.
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 Okuwaki, Mitsuru

× Okuwaki, Mitsuru

WEKO 465124

Okuwaki, Mitsuru

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Sumi, Ayako

× Sumi, Ayako

WEKO 465125

Sumi, Ayako

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Hisaoka, Miharu

× Hisaoka, Miharu

WEKO 465126

Hisaoka, Miharu

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Saotome, Ai

× Saotome, Ai

WEKO 465127

Saotome, Ai

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Akashi, Satoko

× Akashi, Satoko

WEKO 465128

Akashi, Satoko

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Nishimura, Yoshifumi

× Nishimura, Yoshifumi

WEKO 465129

Nishimura, Yoshifumi

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Nagata, Kyosuke

× Nagata, Kyosuke

WEKO 465130

Nagata, Kyosuke

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早乙女 愛

× 早乙女 愛

WEKO 465131

en 早乙女 愛

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抄録
内容記述タイプ Abstract
内容記述 Sperm chromatin remodeling after oocyte entry is the essential step that initiates embryogenesis. This reaction involves the removal of sperm-specific basic proteins and chromatin assembly with histones. In mammals, three nucleoplasmin/nucleophosmin (NPM) family proteins-NPM1, NPM2 and NPM3-expressed in oocytes are presumed to cooperatively regulate sperm chromatin remodeling. We characterized the sperm chromatin decondensation and nucleosome assembly activities of three human NPM proteins. NPM1 and NPM2 mediated nucleosome assembly independently of other NPM proteins, whereas the function of NPM3 was largely dependent on formation of a complex with NPM1. Maximal sperm chromatin remodeling activity of NPM2 required the inhibition of its non-specific nucleic acid-binding activity by phosphorylation. Furthermore, the oligomer formation with NPM1 elicited NPM3 nucleosome assembly and sperm chromatin decondensation activity. NPM3 also suppressed the RNA-binding activity of NPM1, which enhanced the nucleoplasm-nucleolus shuttling of NPM1 in somatic cell nuclei. Our results proposed a novel mechanism whereby three NPM proteins cooperatively regulate chromatin disassembly and assembly in the early embryo and in somatic cells.
書誌情報 Nucleic Acids Research

巻 40, 号 11, p. 4861-78, 発行日 2013-02
ISSN
収録物識別子タイプ ISSN
収録物識別子 0305-1048
DOI
識別子タイプ DOI
関連識別子 10.1093/nar/gks162.
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