Conformational stability of a hyperthermophilic protein in various conditions for denaturation

Abstract

Although hyperthermophilic proteins retain their native forms even under high temperature environments, it is not well characterized whether they show some tolerance toward other denaturing conditions. In this study, we examined tolerance of a hyperthermophilic protein to various denaturing conditions using O6-methylguanine-DNA methyltransferase from Thermococcus kodakaraensis KOD1 (Tk-MGMT) as a model protein. Tk-MGMT showed higher stability to alcohols and denaturants as well as higher melting temperature than its mesophilic counterpart protein from Escherichia coli (Ec-AdaC). High stability toward various denaturing conditions suggests that hyperthermophilic proteins can be commercially applied to use in various extreme conditions as well as high temperature environments.