Purification and structural characterization of the thermosome from the hyperthermophilic archaeum Methanopyrus kandleri.
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.
Andrä
S
S
Lehrstuhl für Mikrobiologie, Universität Regensburg, Germany.
Frey
G
G
Nitsch
M
M
Baumeister
W
W
Stetter
K O
KO
D000595:Amino Acid Sequence; D001483:Base Sequence; D018833:Chaperonins / Q000096:biosynthesis / Q000737:chemistry / Q000648:ultrastructure*; D002850:Chromatography, Gel; D003001:Cloning, Molecular; D017931:DNA Primers; D004591:Electrophoresis, Polyacrylamide Gel; D019605:Euryarchaeota / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure*; D005798:Genes, Bacterial; D006358:Hot Temperature; D006801:Humans; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D008970:Molecular Weight; D015388:Organelles / Q000737:chemistry / Q000648:ultrastructure*; D016133:Polymerase Chain Reaction; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000648:ultrastructure; D017386:Sequence Homology, Amino Acid
D017931:DNA Primers; D011994:Recombinant Proteins; D018833:Chaperonins