| アイテムタイプ |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2025-05-08 |
| タイトル |
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タイトル |
Translation arrest cancellation of VemP, a secretion monitor in Vibrio, is regulated by multiple cis and trans factors, including SecY |
| 言語 |
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言語 |
eng |
| キーワード |
|
|
主題Scheme |
Other |
|
主題 |
nascent polypeptide |
| キーワード |
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|
主題Scheme |
Other |
|
主題 |
periplasmic chaperone |
| キーワード |
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|
主題Scheme |
Other |
|
主題 |
protein cross-linking |
| キーワード |
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|
主題Scheme |
Other |
|
主題 |
protein complex |
| キーワード |
|
|
主題Scheme |
Other |
|
主題 |
proton motive force |
| キーワード |
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主題Scheme |
Other |
|
主題 |
ribosome |
| キーワード |
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主題Scheme |
Other |
|
主題 |
SecA |
| キーワード |
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主題Scheme |
Other |
|
主題 |
secretion |
| 資源タイプ |
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資源タイプ |
journal article |
| アクセス権 |
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アクセス権 |
open access |
| 著者 |
Ikeda, Yuki
Miyazaki, Ryoji
塚崎, 智也
Akiyama, Yoshinori
Mori, Hiroyuki
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| 抄録 |
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内容記述タイプ |
Abstract |
|
内容記述 |
VemP is a secretory protein in the Vibrio species that monitors cellular protein-transport activity through its translation arrest, allowing expression of the downstream secD2-secF2 genes in the same operon, which encode components of the protein translocation machinery. When cellular protein-transport function is fully active, secD2/F2 expression remains repressed as VemP translation arrest is canceled immediately. The VemP arrest cancellation occurs on the SecY/E/G translocon in a late stage in the translocation process and requires both trans factors, SecD/F and PpiD/YfgM, and a cis element, Arg-85 in VemP; however, the detailed molecular mechanism remains elusive. This study aimed to elucidate how VemP passing through SecY specifically monitors SecD/F function. Genetic and biochemical studies showed that SecY is involved in the VemP arrest cancellation and that the arrested VemP is stably associated with a specific site in the protein-conducting pore of SecY. VemP-Bla reporter analyses revealed that a short hydrophobic segment adjacent to Arg-85 plays a critical role in the regulated arrest cancellation with its hydrophobicity correlating with the stability of the VemP arrest. We identified Gln-65 and Pro-67 in VemP as novel elements important for the regulation. We propose a model for the regulation of the VemP arrest cancellation by multiple cis elements and trans factors with different roles. |
| 書誌情報 |
en : Journal of Biological Chemistry
巻 300,
号 10,
発行日 2024-09-02
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| 出版者 |
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出版者 |
Elsevier |
| ISSN |
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収録物識別子タイプ |
EISSN |
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収録物識別子 |
1083-351X |
| 出版者版DOI |
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関連タイプ |
isReplacedBy |
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識別子タイプ |
DOI |
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関連識別子 |
https://doi.org/10.1016/j.jbc.2024.107735 |
| 出版者版URI |
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関連タイプ |
isReplacedBy |
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|
識別子タイプ |
URI |
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関連識別子 |
https://www.sciencedirect.com/science/article/pii/S0021925824022361 |
| 権利 |
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|
権利情報Resource |
https://creativecommons.org/licenses/by/4.0/ |
|
権利情報 |
$00A9 2024 THE AUTHORS. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
| 著者版フラグ |
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出版タイプ |
NA |
| 助成情報 |
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助成機関名 |
Japan Society for the Promotion of Science (JSPS) |
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研究課題番号 |
23K23850 |
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研究課題名 |
ホロトランスロコン複合体による効率的タンパク質分泌の構造基盤 |
| 助成情報 |
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助成機関名 |
Japan Society for the Promotion of Science (JSPS) |
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研究課題番号 |
23K23835 |
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研究課題名 |
大腸菌BepAによる外膜タンパク質トリアージ機構とその制御 |
| 助成情報 |
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助成機関名 |
Japan Society for the Promotion of Science (JSPS) |
|
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研究課題番号 |
20K06556 |
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研究課題名 |
分泌モニタータンパク質VemPの翻訳アレスト解除の分子機構 |
| 助成情報 |
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助成機関名 |
Japan Society for the Promotion of Science (JSPS) |
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研究課題番号 |
23K05694 |
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研究課題名 |
タンパク質膜透過装置による分泌モニター因子VemPの翻訳アレスト解除の調節メカニズム |
