Andrae, Stefan and Frey, Gerhard and Jaenicke, Rainer and Stetter, Karl O. (1998) The thermosome from Methanopyrus kandleri possesses an NH4+-dependent ATPase activity. EUROPEAN JOURNAL OF BIOCHEMISTRY, 255 (1). pp. 93-99. ISSN 0014-2956,
Full text not available from this repository. (Request a copy)Abstract
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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ARCHAEON SULFOLOBUS-SOLFATARICUS; MOLECULAR CHAPERONE; THERMOPHILIC ARCHAEBACTERIUM; STRUCTURAL CHARACTERIZATION; RNA-POLYMERASE; HEAT-SHOCK; IN-VITRO; COMPLEX; 110-DEGREES-C; EXPRESSION; Archaea; chaperonin; thermosome; Methanopyrus; adenosinetriphosphatase |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie (Archaeenzentrum) |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 09 May 2023 06:54 |
| Last Modified: | 09 May 2023 06:54 |
| URI: | https://pred.uni-regensburg.de/id/eprint/49691 |
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