Elucidation of the maturation mechanism of subtilisins from hyperthermophiles and development of their potential use

分析了高温考古菌的枯草杆菌毒素TK-subtilisin和TK-SP的成熟机理。结果表明，TK-SP和TK-SP都是在N端蛋白质自身加工和降解时被激活(成熟)的，TK-枯草杆菌蛋白的折叠是在Ca^&lt；2&gt；离子与Ca^&lt；2&gt；-结合环结合时诱导的，TK-SP是在没有Ca^&lt；2&gt；离子的情况下成熟的，TK-SP需要C-末端的β-Jelly Roll结构域来实现超稳定性。研究还表明，TK-枯草杆菌毒素对异常蛋白的降解是有用的。

The maturation mechanisms of subtilisins, Tk-subtilisin and Tk-SP, from the hyperthermophilic archaeon Thermococcus kodakarensis were analyzed. The results indicate that both proteins are activated(matured) upon autoprocessing and degradation of N-terminal propeprides, folding of Tk-subtilisin is induced upon binding of the Ca^<2+> ions to the Ca^<2+>-binding loop, Tk-SP is matured in the absence of the Ca^<2+> ions, Tk-SP requires C-terminalβ-jelly roll domain for hyperstability. It was also shown that Tk-subtilisin is useful for degradation of abnormal prion proteins.