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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/850144df84ef4-bcd1-4831-ba07-b071cb22602c
Item type | 学術雑誌論文 / Journal Article(1) | |||||
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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× L. McKnight, Steven× Masato, Kato |
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抄録 | ||||||
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 |
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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 | |||||
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識別子タイプ | URI | |||||
関連識別子 | https://www.pnas.org/content/118/42/e2114412118 |