| アイテムタイプ |
itemtype_ver1(1) |
| 公開日 |
2025-01-24 |
| タイトル |
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|
タイトル |
Nuclear interactions between the Pseudo-Response Regulator clock proteins and the Multi-Step Phosphorelay mediator Histidine-containing phosphotransfers in the moss Physcomitrium patens |
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言語 |
en |
| 著者 |
Anami, Shu
Yamashino, Takafumi
Kikuchi, Haruki
Suzuki, Ryo
Aoki, Setsuyuki
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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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|
権利情報 |
© 2024. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/ |
|
言語 |
en |
| 内容記述 |
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内容記述タイプ |
Abstract |
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内容記述 |
Pseudo-Response Regulator (PRR) proteins constitute a fundamental set of circadian clock components in plants. PRRs have an amino acid sequence stretch with similarity to the receiver (REC) domain of response regulators (RRs) in the Multi-Step Phosphorelay (MSP). However, it has never been elucidated whether PRRs interact with Histidine-containing Phosphotransfer (HPt) proteins, which transfer a phosphate to RRs. Here, we studied whether PRRs interact with HPts in the moss Physcomitrium patens by the Yeast Two-Hybrid system and Bimolecular Fluorescence Complementation. P. patens PRR1/2/3 interacted with HPt1/2 in the nucleus, but not with HPt3, suggesting that P. patens PRRs function as authentic RRs. We discuss these results in relation to the evolution and diversity of the plant circadian clocks. |
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言語 |
en |
| 出版者 |
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出版者 |
Elsevier |
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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resource |
http://purl.org/coar/resource_type/c_6501 |
|
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/10.1016/j.bbrc.2024.150734 |
| 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 |
0006-291X |
| 書誌情報 |
en : Biochemical and Biophysical Research Communications
巻 733,
p. 150734,
発行日 2024-11-12
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| ファイル公開日 |
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|
日付 |
2025-11-12 |
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日付タイプ |
Available |