| Budget Amount *help |
¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
Fiscal Year 2012: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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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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