2017年8月
Fusion protein analysis reveals the precise regulation between Hsp70 and Hsp100 during protein disaggregation
SCIENTIFIC REPORTS
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- 巻
- 7
- 号
- 1
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1038/s41598-017-08917-8
- 出版者・発行元
- NATURE PUBLISHING GROUP
ClpB, a bacterial Hsp100, is a ring-shaped AAA+ chaperone that can reactivate aggregated proteins in cooperation with DnaK, a bacterial Hsp70, and its co-factors. ClpB subunits comprise two AAA+ modules with an interstitial rod-shaped M-domain. The M-domain regulates ClpB ATPase activity and interacts directly with the DnaK nucleotide-binding domain (NBD). Here, to clarify how these functions contribute to the disaggregation process, we constructed ClpB, DnaK, and aggregated YFP fusion proteins in various combinations. Notably, i) DnaK activates ClpB only when the DnaK substratebinding domain (SBD) is in the closed conformation, affording high DnaK-peptide affinity; ii) although NBD alone can activate ClpB, SBD is required for disaggregation; and iii) tethering aggregated proteins to the activated ClpB obviates SBD requirements. These results indicate that DnaK activates ClpB only when the SBD tightly holds aggregated proteins adjacent to ClpB for effective disaggregation.
- リンク情報
- ID情報
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- DOI : 10.1038/s41598-017-08917-8
- ISSN : 2045-2322
- ORCIDのPut Code : 45542790
- Web of Science ID : WOS:000407864400029