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Purification and structural characterization of the thermosome from the hyperthermophilic archaeum Methanopyrus kandleri
Author(s) -
Andrä Stefan,
Frey Gerhard,
Nitsch Michael,
Baumeister Wolfgang,
Stetter Karl O.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01493-4
Subject(s) - methanogen , biology , thermophile , homology (biology) , protein subunit , methanomicrobiales , molecular mass , peptide sequence , homogeneity (statistics) , protein primary structure , genetics , gene , crystallography , biochemistry , archaea , bacteria , chemistry , enzyme , statistics , mathematics , methanosarcina
From Methanopyrus 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.