Chaperonin in a Thermophilic Methanogen, Methanococcus Thermolithotrophicus
Molecular chaperones play an important role in the protein foldings in vivo. Chaperonin is a 60 kDa major member of molecular chaperones and has two types, Group I and Group II. The Group I chaperonin is GroEL-like complex in eubacteria, mitochondria and chloroplasts. Whereas archaeral chaperonin which is coiled thermosomc and eukaryotic cytosol TCP- I protein belong to Group II (Trent et al., 1991). While a chaperonin was purified from a hyperthermophilic methanogen, Methanopyrus kandleri (Andrä et al., 1996), biochemical and functional characters of chaperonins in methanogens have remained to be clarified. We report here characteristics of chaperonin of a thermophilic methanogen, Methanococcus thermolithotrophicus.
KeywordsATPase Activity Molecular Chaperone Malachite Green Methanococcus Jannaschii Sensus Amino Acid
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- Trent, J.D., Kagawa, H., Yaoi, T., 011e, E., and Zaluzec, N.J., 1997, Proc. Natl. Acad Sci. USA 94: 5383–5388Google Scholar