Abstract
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.
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© 1998 Springer Science+Business Media New York
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Furutani, M., Iida, T., Yamano, S., Maruyama, T. (1998). Chaperonin in a Thermophilic Methanogen, Methanococcus Thermolithotrophicus . In: Gal, Y.L., Halvorson, H.O. (eds) New Developments in Marine Biotechnology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-5983-9_41
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DOI: https://doi.org/10.1007/978-1-4757-5983-9_41
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4419-3300-3
Online ISBN: 978-1-4757-5983-9
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