| アイテムタイプ |
文献 / Documents(1) |
| 公開日 |
2022-06-14 |
| アクセス権 |
|
|
アクセス権 |
open access |
| 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 |
| 出版社版DOI |
|
|
|
関連識別子 |
https://doi.org/10.3390/biology10111106 |
|
|
関連名称 |
10.3390/biology10111106 |
| 出版タイプ |
|
|
出版タイプ |
VoR |
|
出版タイプResource |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
| タイトル |
|
|
タイトル |
Zinc-Dependent Oligomerization of Thermus thermophilus Trigger Factor Chaperone |
| 著者 |
Zhu, Haojie
松﨑, 元紀
スガワラ, タイガ
イシモリ, コウイチロウ
齋尾, 智英
|
| 抄録 |
|
|
内容記述 |
Metal ions often play important roles in biological processes. Thermus thermophilus trigger factor (TtTF) is a zinc-dependent molecular chaperone where Zn2+ has been shown to enhance its folding-arrest activity. However, the mechanisms of how Zn2+ binds to TtTF and how Zn2+ affects the activity of TtTF are yet to be elucidated. As a first step in understanding the mechanism, we performed in vitro biophysical experiments on TtTF to investigate the zinc-binding site on TtTF and unveil how Zn2+ alters the physical properties of TtTF, including secondary structure, thermal stability, and oligomeric state. Our results showed that TtTF binds Zn2+ in a 1:1 ratio, and all three domains of TtTF are involved in zinc-binding. We found that Zn2+ does not affect the thermal stability of TtTF, whereas it does induce partial structural change and promote the oligomerization of TtTF. Given that the folding-arrest activity of Escherichia coli TF (EcTF) is regulated by its oligomerization, our results imply that TtTF exploits Zn2+ to modulate its oligomeric state to regulate the activity. |
| 抄録 |
|
|
内容記述 |
Thermus thermophilus trigger factor (TtTF) is a zinc-dependent molecular chaperone whose folding-arrest activity is regulated by Zn2+. However, little is known about the mechanism of zinc-dependent regulation of the TtTF activity. Here we exploit in vitro biophysical experiments to investigate zinc-binding, the oligomeric state, the secondary structure, and the thermal stability of TtTF in the absence and presence of Zn2+. The data show that full-length TtTF binds Zn2+, but the isolated domains and tandem domains of TtTF do not bind to Zn2+. Furthermore, circular dichroism (CD) and nuclear magnetic resonance (NMR) spectra suggested that Zn2+-binding induces the partial structural changes of TtTF, and size exclusion chromatography-multi-angle light scattering (SEC-MALS) showed that Zn2+ promotes TtTF oligomerization. Given the previous work showing that the activity regulation of E. coli trigger factor is accompanied by oligomerization, the Data suggest that TtTF exploits zinc ions to induce the structural change coupled with the oligomerization to assemble the client-binding site, thereby effectively preventing proteins from misfolding in the thermal environment. |
| キーワード |
|
|
主題 |
trigger factor |
| キーワード |
|
|
主題 |
zinc-dependent chaperone |
| キーワード |
|
|
主題 |
Thermus thermophilus |
| キーワード |
|
|
主題 |
thermal stability |
| キーワード |
|
|
主題 |
secondary structure |
| キーワード |
|
|
主題 |
mass spectrometry |
| キーワード |
|
|
主題 |
oligomerization |
| キーワード |
|
|
主題 |
NMR |
| 書誌情報 |
en : Biology
巻 10,
号 11,
p. 1106,
発行日 2021-10-26
|
| 収録物ID |
|
|
収録物識別子タイプ |
ISSN |
|
収録物識別子 |
20797737 |
| 出版者 |
|
|
出版者 |
MDPI |
| 権利情報 |
|
|
権利情報 |
This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
| EID |
|
|
識別子 |
385894 |
| 言語 |
|
|
言語 |
eng |
biology_10_11_1106.pdf (1.74 MB)
.png)
