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          Institute: MPI für Biochemie     Collection: Structural Biology (W. Baumeister)     Display Documents



ID: 318354.0, MPI für Biochemie / Structural Biology (W. Baumeister)
Purification and structural characterization of the thermosome from the hyperthermophilic archaeum methanopyrus kandleri
Authors:Andrä, S.; Frey, G.; Nitsch, M.; Baumeister, W.; Stetter, K. O.
Date of Publication (YYYY-MM-DD):1996-01-29
Title of Journal:FEBS Letters
Volume:379
Issue / Number:2
Start Page:127
End Page:131
Audience:Not Specified
Abstract / Description:From Methanopyras kandleri, the most thermophilic methanogen known so far, we have purified to homogeneity a protein complex of high molecular mass. Image analysis of transmission electron micrographs revealed a barrel-shaped particle composed of two rings with 8-fold symmetry. Only one type of subunit could be detected, The corresponding gene has been cloned and sequenced. The deduced amino acid sequence shows high homology with the members of group II chaperonins. The structure of the projection and the sequence homology suggest that this particle is the first thermosome isolated from a methanogen. [References: 29]
Free Keywords:Archaea; Chaperonin; Thermosome; Methanopyrus.; T-complex polypeptide-1; Molecular chaperone; Thermophilic archaebacterium; Heat-shock; Proteins; Electrophoresis; 110-degrees-c; Tubulin; Gen; Nov.; Biochemistry & biophysics.
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)/
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