| アイテムタイプ |
文献 / Documents(1) |
| 公開日 |
2022-01-28 |
| アクセス権 |
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アクセス権 |
open access |
| 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 |
| 出版社版DOI |
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関連識別子 |
https://doi.org/10.1038/s41467-020-20553-x |
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関連名称 |
10.1038/s41467-020-20553-x |
| 出版タイプ |
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出版タイプ |
VoR |
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出版タイプResource |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
| タイトル |
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タイトル |
Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex |
| 著者 |
Rizzolo, Kamran
Yu, Angela Yeou Hsiung
Ologbenla, Adedeji
Kim, Sa Rang
Zhu, Haojie
イシモリ, コウイチロウ
Thibault, Guillaume
Leung, Elisa
Zhang, Yi Wen
Teng, Mona
Haniszewski, Marta
Miah, Noha
Phanse , Sadhna
Minic, Zoran
Lee, Sukyeong
Caballero, Julio Diaz
Babu, Mohan
Tsai, Francis T. F.
齋尾, 智英
Houry, Walid A.
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| 抄録 |
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内容記述 |
A functional association is uncovered between the ribosome-associated trigger factor (TF) chaperone and the ClpXP degradation complex. Bioinformatic analyses demonstrate conservation of the close proximity of tig, the gene coding for TF, and genes coding for ClpXP, suggesting a functional interaction. The effect of TF on ClpXP-dependent degradation varies based on the nature of substrate. While degradation of some substrates are slowed down or are unaffected by TF, surprisingly, TF increases the degradation rate of a third class of substrates. These include λ phage replication protein λO, master regulator of stationary phase RpoS, and SsrA-tagged proteins. Globally, TF acts to enhance the degradation of about 2% of newly synthesized proteins. TF is found to interact through multiple sites with ClpX in a highly dynamic fashion to promote protein degradation. This chaperone–protease cooperation constitutes a unique and likely ancestral aspect of cellular protein homeostasis in which TF acts as an adaptor for ClpXP. |
| 書誌情報 |
en : Nature Communications
巻 12,
p. 281,
発行日 2021-01-12
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収録物識別子タイプ |
ISSN |
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収録物識別子 |
20411723 |
| 収録物ID |
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収録物識別子タイプ |
NCID |
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収録物識別子 |
AA12645905 |
| 出版者 |
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出版者 |
Springer Nature |
| 権利情報 |
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権利情報 |
This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
| EID |
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識別子 |
381295 |
| 言語 |
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言語 |
eng |
ncomms_12_281.pdf (3.68 MB)
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