Item type |
itemtype_ver1(1) |
公開日 |
2022-09-21 |
タイトル |
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タイトル |
Hoop-like role of the cytosolic interface helix in Vibrio PomA, an ion-conducting membrane protein, in the bacterial flagellar motor |
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言語 |
en |
著者 |
Nishikino, Tatsuro
Sagara, Yugo
Terashima, Hiroyuki
Homma, Michio
Kojima, Seiji
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アクセス権 |
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アクセス権 |
open access |
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アクセス権URI |
http://purl.org/coar/access_right/c_abf2 |
権利 |
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言語 |
en |
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権利情報 |
This is a pre-copyedited, author-produced version of an article accepted for publication in [The Journal of Biochemistry] following peer review. The version of record [Tatsuro Nishikino, Yugo Sagara, Hiroyuki Terashima, Michio Homma, Seiji Kojima, Hoop-like role of the cytosolic interface helix in Vibrio PomA, an ion-conducting membrane protein, in the bacterial flagellar motor, The Journal of Biochemistry, Volume 171, Issue 4, April 2022, Pages 443–450, https://doi.org/10.1093/jb/mvac001] is available online at: https://doi.org/10.1093/jb/mvac001. |
キーワード |
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主題Scheme |
Other |
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主題 |
supramolecular complex |
キーワード |
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主題Scheme |
Other |
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主題 |
stator |
キーワード |
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主題Scheme |
Other |
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主題 |
MotB |
キーワード |
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主題Scheme |
Other |
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主題 |
MotA |
キーワード |
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主題Scheme |
Other |
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主題 |
bacterial flagellum |
内容記述 |
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内容記述タイプ |
Abstract |
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内容記述 |
Vibrio has a polar flagellum driven by sodium ions for swimming. The force-generating stator unit consists of PomA and PomB. PomA contains four transmembrane regions and a cytoplasmic domain of approximately 100 residues, which interacts with the rotor protein, FliG, to be important for the force generation of rotation. The 3D structure of the stator shows that the cytosolic interface (CI) helix of PomA is located parallel to the inner membrane. In this study, we investigated the function of CI helix and its role as stator. Systematic proline mutagenesis showed that residues K64, F66 and M67 were important for this function. The mutant stators did not assemble around the rotor. Moreover, the growth defect caused by PomB plug deletion was suppressed by these mutations. We speculate that the mutations affect the structure of the helices extending from TM3 and TM4 and reduce the structural stability of the stator complex. This study suggests that the helices parallel to the inner membrane play important roles in various processes, such as the hoop-like function in securing the stability of the stator complex and the ion conduction pathway, which may lead to the elucidation of the ion permeation and assembly mechanism of the stator. |
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言語 |
en |
出版者 |
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出版者 |
Oxford University Press |
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言語 |
en |
言語 |
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言語 |
eng |
資源タイプ |
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資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
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資源タイプ |
journal article |
出版タイプ |
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出版タイプ |
AM |
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出版タイプResource |
http://purl.org/coar/version/c_ab4af688f83e57aa |
関連情報 |
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関連タイプ |
isVersionOf |
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識別子タイプ |
DOI |
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関連識別子 |
https://doi.org/10.1093/jb/mvac001 |
収録物識別子 |
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収録物識別子タイプ |
PISSN |
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収録物識別子 |
0021-924X |
書誌情報 |
en : The Journal of Biochemistry
巻 171,
号 4,
p. 443-450,
発行日 2022-04
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ファイル公開日 |
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日付 |
2023-04-01 |
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日付タイプ |
Available |