The thermosome from Methanopyrus kandleri possesses an NH.es+.rb.ei4.rb -dependent ATPase activity
- Resource Type
- Authors
- Karl O. Stetter; Stefan Andrä; Gerhard Frey; Rainer Jaenicke
- Source
- European Journal of Biochemistry. 255:93-99
- Subject
- biology
Protein subunit
ATPase
Methanopyrus
biology.organism_classification
medicine.disease_cause
Biochemistry
Molecular biology
Thermosome
Chaperonin
law.invention
ATP hydrolysis
law
biology.protein
Recombinant DNA
medicine
Escherichia coli
- Language
- ISSN
- 1432-1033
0014-2956
The ATPase activity of the thermosome from a methanogen, Methanopyrus kandleri, was characterized in detail. In contrast to all other known chaperonins, enzymatic ATP hydrolysis was found to be strictly dependent on high levels of ammonium salts in vitro. The ths gene encoding the thermosome subunit from the hyperthermophilic M. kandleri was functionally expressed in Escherichia coli and the overproduced polypeptide was assembled into intact thermosome complexes in the mesophilic host. The recombinant particles could be purified by a simple two-step procedure including only one chromatographic step. Structural and biochemical properties of the recombinant protein were closely similar to those of the natural complex. Western blot analysis with an antiserum against the M. kandleri thermosome indicated the presence of at least two subfamilies of archaeal chaperonins.