2015 Fiscal Year Final Research Report
The prokaryotic Hsp90 chaperone network
| Project/Area Number |
24580102
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Applied microbiology
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| Research Institution | Saitama University |
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Principal Investigator |
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| Project Period (FY) |
2012-04-01 – 2016-03-31
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| Keywords | 分子シャペロン / 熱ショックタンパク質 / Hsp90 / Hsp70 / シアノバクテリア |
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| Outline of Final Research Achievements |
HtpG, a bacterial heat shock protein 90 (Hsp90), is essential for thermotolerance in some prokaryotes. HtpG functioned with DnaK2 (Hsp70)/DnaJ2/GrpE to assist unfolding/folding of denatured proteins in both ATP-dependent and -independent fashions. The cooperative action of HtpG and DnaK2 might play a key role under stress. DnaJ2 and GroEL also interacted with HtpG physically. We found that a naturally occurring styryl-lactone goniothalamin activates the ATPase activity of Hsp90. Unexpectedly, it inhibited the activity of HtpG that assists refolding of a non-native protein in cooperation with the DnaK2 chaperone system. It indicates that the ATPase activity of HtpG has to be controlled so that it can co-operate with DnaK2 effectively.
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| Free Research Field |
分子生物学・生化学
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