GroEL-like protein complex of thermophilic bacterium Thermus aquaticus
Language English Country United States Media print
Document type Comparative Study, Journal Article
PubMed
7903530
DOI
10.1006/bbrc.1993.2538
PII: S0006-291X(83)72538-6
Knihovny.cz E-resources
- MeSH
- Adenosine Triphosphatases isolation & purification metabolism MeSH
- Bacillus megaterium MeSH
- Bacterial Proteins chemistry isolation & purification metabolism ultrastructure MeSH
- Chaperonin 60 MeSH
- Chromatography, Ion Exchange MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Microscopy, Electron MeSH
- Endopeptidases metabolism MeSH
- Kinetics MeSH
- Molecular Sequence Data MeSH
- Heat-Shock Proteins chemistry isolation & purification ultrastructure MeSH
- Amino Acid Sequence MeSH
- Sequence Homology, Amino Acid MeSH
- Thermodynamics MeSH
- Thermus metabolism MeSH
- Publication type
- Journal Article MeSH
- Comparative Study MeSH
- Names of Substances
- Adenosine Triphosphatases MeSH
- Bacterial Proteins MeSH
- Chaperonin 60 MeSH
- Endopeptidases MeSH
- Heat-Shock Proteins MeSH
GroEL-like particles of Thermus aquaticus are homo-oligomeric complexes of two stacked seven member rings, sedimenting in the gradient at 20S. The apparent molecular mass of the native particles is 820,000 (+/- 30,000). The protein complex is composed with one polypeptide of M(r) 59,000. Immunoblotting results and N-terminal amino acid analysis indicate that the complex is significantly related to the chaperonins. No proteolytic activity was identified in the purified GroEL-like particles. In the presence of Mg2+ and K+ the complex exhibits temperature dependent ATPase activity. Under optimum temperature (75 degrees C) GroEL is stable and hydrolyze ATP with a specific activity of 0.47 mumol min-1 mg-1.
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