Contribution of the C-Terminal Region of a Group II Chaperonin to its Interaction with Prefoldin and Substrate Transfer
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- 作者：Tamotsu Zako1 ; &dagger ; ; 4 ; Muhamad Sahlan2 ; 3 ; &dagger ; ; Sayaka Fujii2 ; &dagger ; ; Yohei Y. Yamamoto2 ; &dagger ; ; Phan The Tai2 ; Kotaro Sakai1 ; 2 ; Mizuo Maeda1 ; Masafumi Yohda2 ; yohda@cc.tuat.ac.jp" class="auth_mail" title="E-mail the corresponding author
- 关键词：CPN ; chaperonin ; T.KS-1 ; hyperthermophilic archaeon Thermococcus sp. strain KS-1 ; PFD ; prefoldin ; PFDα1β1 ; prefoldin of Thermococcus sp. strain KS-1 composed of α1 and β1 subunits ; PFDα2β2 ; prefoldin of Thermococcus sp. strain KS-1 composed of α2 and β2 subunits ; CS ; citrate synthase from porcine heart ; GFP ; green fluorescent protein ; SPR ; surface plasmon resonance ; PAGE ; polyacrylamide gel electrophoresis ; CPNβ ; T.KS-1 chaperonin β homo-oligomer ; CPNβTc1 ; T.KS-1 chaperonin β mutant with the tru
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：5 June 2016
- 年：2016
- 卷：428
- 期：11
- 页码：2405-2417
- 全文大小：1020 K
文摘
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Prefoldin (PFD) interacts with group II chaperonin (CPN) for substrate transfer.
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The flexible C-terminal region of CPN protrudes into the cavity of CPN.
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Truncation of the CPN C-terminal region decreases affinity with PFD.
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Truncation also decreases substrate transfer from PFD and folding by CPN.
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The C-terminal region of CPN is a newly found interaction site with PFD.