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Chaperonin in a Thermophilic Methanogen, Methanococcus Thermolithotrophicus

  • Masahiro Furutani
  • Toshii Iida
  • Shigeyuki Yamano
  • Tadashi Maruyama
Chapter

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.

Keywords

ATPase Activity Molecular Chaperone Malachite Green Methanococcus Jannaschii Sensus Amino Acid 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Masahiro Furutani
    • 1
  • Toshii Iida
    • 1
  • Shigeyuki Yamano
    • 2
  • Tadashi Maruyama
    • 1
  1. 1.Marine Biotechnology InstituteKamaishi, IwateJapan
  2. 2.Marine Biotechnology InstituteShimizu, ShizuokaJapan

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