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  1. 原著論文

The low-complexity domain of the FUS RNA binding protein self-assembles via the mutually exclusive use of two distinct cross-β cores

https://repo.qst.go.jp/records/85014
https://repo.qst.go.jp/records/85014
4df84ef4-bcd1-4831-ba07-b071cb22602c
Item type 学術雑誌論文 / Journal Article(1)
公開日 2022-02-16
タイトル
タイトル The low-complexity domain of the FUS RNA binding protein self-assembles via the mutually exclusive use of two distinct cross-β cores
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 Masato, Kato

× Masato, Kato

WEKO 1040761

Masato, Kato

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L. McKnight, Steven

× L. McKnight, Steven

WEKO 1040762

L. McKnight, Steven

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Masato, Kato

× Masato, Kato

WEKO 1040763

en Masato, Kato

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内容記述タイプ Abstract
内容記述 The low-complexity (LC) domain of the fused in sarcoma (FUS) RNA binding protein self-associates in a manner causing phase separation from an aqueous environment. Incubation of the FUS LC domain under physiologically normal conditions of salt and pH leads to rapid formation of liquid-like droplets that mature into a gel-like state. Both examples of phase separation have enabled reductionist biochemical assays allowing discovery of an N-terminal region of 57 residues that assembles into a labile, cross-β structure. Here we provide evidence of a nonoverlapping, C-terminal region of the FUS LC domain that also forms specific cross-β interactions. We propose that biologic function of the FUS LC domain may operate via the mutually exclusive use of these N- and C-terminal cross-β cores. Neurodegenerative disease–causing mutations in the FUS LC domain are shown to imbalance the two cross-β cores, offering an unanticipated concept of LC domain function and dysfunction.
書誌情報 PNAS

巻 118, 号 42, p. e2114412118, 発行日 2022-02
ISSN
収録物識別子タイプ ISSN
収録物識別子 0027-8424
DOI
識別子タイプ DOI
関連識別子 10.1073/pnas.2114412118
関連サイト
識別子タイプ URI
関連識別子 https://www.pnas.org/content/118/42/e2114412118
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