| Item type |
学術雑誌論文 / Journal Article(1) |
| 公開日 |
2023-02-23 |
| タイトル |
|
|
タイトル |
Physicochemical Properties of the Mammalian Molecular Chaperone HSP60 |
|
言語 |
en |
| 言語 |
|
|
言語 |
eng |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
molecular chaperone |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
chaperonin |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
HSP60 |
| 主題 |
|
|
主題Scheme |
Other |
|
主題 |
GroEL |
| 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 |
| アクセス権 |
|
|
アクセス権 |
open access |
|
アクセス権URI |
http://purl.org/coar/access_right/c_abf2 |
| 作成者 |
Ishida, Ryuichi
Okamoto, Tomoya
Motojima, Fumihiro
Kubota, Hiroshi
Takahashi, Hiroki
Tanabe, Masako
Oka, Toshihiko
Kitamura, Akira
Kinjo, Masataka
Yoshida, Masasuke
Otaka, Michiro
Grave, Ewa
Itoh, Hideaki
|
| 内容記述 |
|
|
内容記述タイプ |
Abstract |
|
内容記述 |
The E. coli GroEL/GroES chaperonin complex acts as a folding cage by producing a bullet-like asymmetric complex, and GroEL exists as double rings regardless of the presence of adenosine triphosphate (ATP). Its mammalian chaperonin homolog, heat shock protein, HSP60, and co-chaperonin, HSP10, play an essential role in protein folding by capturing unfolded proteins in the HSP60/HSP10 complex. However, the structural transition in ATPase-dependent reaction cycle has remained unclear. We found nucleotide-dependent association and dissociation of the HSP60/HSP10 complex using various analytical techniques under near physiological conditions. Our results showed that HSP60 exist as a significant number of double-ring complexes (football- and bullet-type complexes) and a small number of single-ring complexes in the presence of ATP and HSP10. HSP10 binds to HSP60 in the presence of ATP, which increased the HSP60 double-ring formation. After ATP is hydrolyzed to Adenosine diphosphate (ADP), HSP60 released the HSP10 and the dissociation of the double-ring to single-rings occurred. These results indicated that HSP60/HSP10 undergoes an ATP-dependent transition between the single- and double-rings in their system that is highly distinctive from the GroEL/GroES system particularly in the manner of complex formation and the roles of ATP binding and hydrolysis in the reaction cycle. |
|
言語 |
en |
| 出版タイプ |
|
|
出版タイプ |
VoR |
|
出版タイプResource |
http://purl.org/coar/version/c_970fb48d4fbd8a85 |
| 書誌情報 |
en : INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
巻 19,
号 2,
発行日 2018
|
| 収録物識別子 |
|
|
収録物識別子タイプ |
ISSN |
|
収録物識別子 |
1422-0067 |
| 出版者 |
|
|
出版者 |
MDPI |
| 関連情報 |
|
|
関連タイプ |
isIdenticalTo |
|
|
識別子タイプ |
DOI |
|
|
関連識別子 |
https://doi.org/10.3390/ijms19020489 |
|
|
言語 |
ja |
| 権利情報 |
|
|
権利情報 |
© 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access
article distributed under the terms and conditions of the Creative Commons Attribution
(CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
iA_2022_60.pdf (3.6 MB)
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