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  1. 学術雑誌論文
  2. 4 自然科学

Novel Insights into Conformational Rearrangements of the Bacterial Flagellar Switch Complex

http://hdl.handle.net/10228/00007694
http://hdl.handle.net/10228/00007694
801ac7ce-7bdb-4a25-916b-a9f78adb6b70
名前 / ファイル ライセンス アクション
10334472.pdf 10334472.pdf (2.4 MB)
アイテムタイプ 学術雑誌論文 = Journal Article(1)
公開日 2020-04-03
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
タイトル
タイトル Novel Insights into Conformational Rearrangements of the Bacterial Flagellar Switch Complex
言語
言語 eng
著者 Sakai, Tomofumi

× Sakai, Tomofumi

WEKO 27295

Sakai, Tomofumi

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Miyata, Tomoko

× Miyata, Tomoko

WEKO 27296

Miyata, Tomoko

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Terahara, Naoya

× Terahara, Naoya

WEKO 27297

Terahara, Naoya

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Mori, Koichiro

× Mori, Koichiro

WEKO 27298

Mori, Koichiro

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Inoue, Yumi

× Inoue, Yumi

WEKO 27299

Inoue, Yumi

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森本, 雄祐

× 森本, 雄祐

WEKO 28693
e-Rad 50631777
Scopus著者ID 35093011600
ORCiD 0000-0003-1573-8967
九工大研究者情報 100001002

en Morimoto, Yusuke V.

ja 森本, 雄祐

ja-Kana モリモト, ユウスケ


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Kato, Takayuki

× Kato, Takayuki

WEKO 27301

Kato, Takayuki

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Namba, Keiichi

× Namba, Keiichi

WEKO 27302

Namba, Keiichi

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Minamino, Tohru

× Minamino, Tohru

WEKO 27303

Minamino, Tohru

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抄録
内容記述タイプ Abstract
内容記述 The flagellar motor can spin in both counterclockwise (CCW) and clockwise (CW) directions. The flagellar motor consists of a rotor and multiple stator units, which act as a proton channel. The rotor is composed of the transmembrane MS ring made of FliF and the cytoplasmic C ring consisting of FliG, FliM, and FliN. The C ring is directly involved in rotation and directional switching. The Salmonella FliF-FliG deletion fusion motor missing 56 residues from the C terminus of FliF and 94 residues from the N terminus of FliG keeps a domain responsible for the interaction with the stator intact, but its motor function is reduced significantly. Here, we report the structure and function of the FliF-FliG deletion fusion motor. The FliF-FliG deletion fusion not only resulted in a strong CW switch bias but also affected rotor-stator interactions coupled with proton translocation through the proton channel of the stator unit. The energy coupling efficiency of the deletion fusion motor was the same as that of the wild-type motor. Extragenic suppressor mutations in FliG, FliM, or FliN not only relieved the strong CW switch bias but also increased the motor speed at low load. The FliF-FliG deletion fusion made intersubunit interactions between C ring proteins tighter compared to the wild-type motor, whereas the suppressor mutations affect such tighter intersubunit interactions. We propose that a change of intersubunit interactions between the C ring proteins may be required for high-speed motor rotation as well as direction switching.
書誌情報 mBio

巻 10, 号 2, p. e00079-19-1-e00079-19-14, 発行日 2019-04-02
出版社
出版者 American Society for Microbiology
DOI
関連タイプ isIdenticalTo
識別子タイプ DOI
関連識別子 https://doi.org/10.1128/mBio.00079-19
ISSN
収録物識別子タイプ ISSN
収録物識別子 2150-7511
著作権関連情報
権利情報 Copyright (c) 2019 Sakai et al.
著作権関連情報
権利情報 Creative Commons Attribution 4.0 International license.
著作権関連情報
権利情報 https://creativecommons.org/licenses/by/4.0/
出版タイプ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
査読の有無
値 yes
研究者情報
URL https://hyokadb02.jimu.kyutech.ac.jp/html/100001002_ja.html
論文ID(連携)
値 10334472
連携ID
値 8193
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