GroEL-like protein complex of thermophilic bacterium Thermus aquaticus.
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.
Mikulík
K
K
Institute of Microbiology, Academy of Sciences of the Czech Republic, Prague.
Benada
O
O
D000251:Adenosine Triphosphatases / Q000302:isolation & purification / Q000378:metabolism*; D000595:Amino Acid Sequence; D001410:Bacillus megaterium; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism / Q000648:ultrastructure; D018834:Chaperonin 60; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000648:ultrastructure; D007700:Kinetics; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D013816:Thermodynamics; D013824:Thermus / Q000378:metabolism*
D001426:Bacterial Proteins; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D010450:Endopeptidases; D000251:Adenosine Triphosphatases