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Chaperonin in a thermophilic methanogen, methanococcus thermolithotrophicus

机译:伴侣蛋白在嗜热产甲烷菌中,嗜热甲烷球菌

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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 colled 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 (Andra et al., 1996), biochemical and functional characteris of chaperonins in methanogens have remained to be clarified. We report here characteristics of chaperonin of a thermophilic methanogen, Methanococcus thermolithotrophicus.
机译:分子伴侣在体内蛋白质折叠中起重要作用。伴侣蛋白是分子伴侣中60 kDa的主要成员,具有两种类型,第一类和第二类。 I类伴侣蛋白是真细菌,线粒体和叶绿体中的GroEL样复合物。而古细菌伴侣蛋白,即嗜热菌和真核细胞质TCP-1蛋白,则属于第二类(Trent等,1991)。尽管从高嗜热性产甲烷菌中纯化出了伴侣蛋白,但其产甲烷蛋白的生化和功能特性仍有待澄清。我们在这里报告嗜热产甲烷菌伴侣嗜热甲烷球菌的伴侣蛋白的特征。

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