GroEL-like Protein Complex of Thermophilic Bacterium Thermus aquaticus

• Published in: Biochemical and biophysical research communications Vol. 197; no. 2; pp. 716 - 721
• Main Authors: Mikulik, K., Benada, O.
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 15.12.1993; Elsevier
• Subjects: Adenosine Triphosphatases - isolation & purification; Adenosine Triphosphatases - metabolism; Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Bacillus megaterium; Bacterial Proteins - chemistry; Bacterial Proteins - isolation & purification; Bacterial Proteins - metabolism; Bacterial Proteins - ultrastructure; Biological and medical sciences; Chaperonin 60; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; Endopeptidases - metabolism; Fundamental and applied biological sciences. Psychology; Heat-Shock Proteins - chemistry; Heat-Shock Proteins - isolation & purification; Heat-Shock Proteins - ultrastructure; Kinetics; Microscopy, Electron; Miscellaneous; Molecular Sequence Data; Proteins; Sequence Homology, Amino Acid; Thermodynamics; Thermus - metabolism; Chaperonin; Purification; Enzymatic activity; Thermus aquaticus; Analog; Bacteria; Structural analysis
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1993.2538

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 Mr 59 000. lmmunoblotting 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°C) GroEL is stable and hydrolyze ATP with a specific activity of 0.47 μmol min−1 mg−1.