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  1. 原著論文

Split conformation of Chaetomium thermophilum Hsp104 disaggregase

https://repo.qst.go.jp/records/82736
https://repo.qst.go.jp/records/82736
a56c266b-db8b-4b7e-9436-03f64d426313
Item type 学術雑誌論文 / Journal Article(1)
公開日 2021-04-12
タイトル
タイトル Split conformation of Chaetomium thermophilum Hsp104 disaggregase
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 Inoue, Yosuke

× Inoue, Yosuke

WEKO 1004221

Inoue, Yosuke

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Yuya, Hanazono

× Yuya, Hanazono

WEKO 1004222

Yuya, Hanazono

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Noi, Kentaro

× Noi, Kentaro

WEKO 1004223

Noi, Kentaro

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Kawamoto, Akihiro

× Kawamoto, Akihiro

WEKO 1004224

Kawamoto, Akihiro

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Kimatsuka, Masato

× Kimatsuka, Masato

WEKO 1004225

Kimatsuka, Masato

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Harada, Ryuhei

× Harada, Ryuhei

WEKO 1004226

Harada, Ryuhei

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Takeda, Kazuki

× Takeda, Kazuki

WEKO 1004227

Takeda, Kazuki

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Kita, Ryoichi

× Kita, Ryoichi

WEKO 1004228

Kita, Ryoichi

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Iwamasa, Natsuki

× Iwamasa, Natsuki

WEKO 1004229

Iwamasa, Natsuki

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Shibata, Kyoka

× Shibata, Kyoka

WEKO 1004230

Shibata, Kyoka

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Noguchi, Keiichi

× Noguchi, Keiichi

WEKO 1004231

Noguchi, Keiichi

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Shigeta, Yasuteru

× Shigeta, Yasuteru

WEKO 1004232

Shigeta, Yasuteru

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Namba, Keiichi

× Namba, Keiichi

WEKO 1004233

Namba, Keiichi

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Ogura, Teru

× Ogura, Teru

WEKO 1004234

Ogura, Teru

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Miki, Kunio

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WEKO 1004235

Miki, Kunio

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Shinohara, Kyosuke

× Shinohara, Kyosuke

WEKO 1004236

Shinohara, Kyosuke

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Yohda, Masafumi

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WEKO 1004237

Yohda, Masafumi

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Yuya, Hanazono

× Yuya, Hanazono

WEKO 1004238

en Yuya, Hanazono

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抄録
内容記述タイプ Abstract
内容記述 Hsp104 and its bacterial homolog ClpB form hexameric ring structures and mediate protein disaggregation. The disaggregated polypeptide is thought to thread through the central channel of the ring. However, the dynamic behavior of Hsp104 during disaggregation remains unclear. Here, we reported the stochastic conformational dynamics and a split conformation of Hsp104 disaggregase from Chaetomium thermophilum (CtHsp104) in the presence of ADP by X-ray crystallography, cryo-electron microscopy (EM), and high-speed atomic force microscopy (AFM). ADP-bound CtHsp104 assembles into a 65 left-handed spiral filament in the crystal structure at a resolution of 2.7 Å. The unit of the filament is a hexamer of the split spiral structure. In the cryo-EM images, staggered and split hexameric rings were observed. Further, high-speed AFM observations showed that a substrate addition enhanced the conformational change and increased the split structure's frequency. Our data suggest that split conformation is an off-pathway state of CtHsp104 during disaggregation.
書誌情報 Structure

巻 29, 号 7, p. 721-730, 発行日 2021-04
ISSN
収録物識別子タイプ ISSN
収録物識別子 0969-2126
PubMed番号
識別子タイプ PMID
関連識別子 33651974
DOI
識別子タイプ DOI
関連識別子 10.1016/j.str.2021.02.002
関連サイト
識別子タイプ URI
関連識別子 https://www.sciencedirect.com/science/article/abs/pii/S0969212621000460
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