A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria.
We have discovered a large cylindrical protein complex which is an abundant component of the cytoplasm of extremely thermophilic archaebacteria. Structural analysis by image processing of electron micrographs suggests that the complex is composed of two stacked rings of eight subunits each; the rings enclose a central channel. The complex purified from the hyperthermophile Pyrodictium occultum is composed of equal quantities of two polypeptides of Mr 56,000 and 59,000. It exhibits an extremely thermostable ATPase activity with a temperature optimum of 100 degrees C. The basal level of the ATPase complex in the cell is high, and it becomes highly enriched as a result of heat shock (shift from 102 degrees C to 108 degrees C) or balanced growth at temperatures near the physiological upper limit. Immunoblotting results indicate that a related protein is present in most thermophilic archaebacteria and in Escherichia coli. This protein complex may play an important role in the adaptation of thermophilic archaebacteria to life at high temperature.
Phipps
B M
BM
Max-Planck Institute for Biochemistry, Martinsried, Germany.
Hoffmann
A
A
Stetter
K O
KO
Baumeister
W
W
D000251:Adenosine Triphosphatases / Q000302:isolation & purification* / Q000648:ultrastructure; D001105:Archaea / Q000201:enzymology* / Q000648:ultrastructure; D002848:Chromatography, DEAE-Cellulose; D003593:Cytoplasm / Q000648:ultrastructure; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006360:Heat-Shock Proteins / Q000302:isolation & purification* / Q000648:ultrastructure; D007091:Image Processing, Computer-Assisted; D015151:Immunoblotting; D008958:Models, Molecular; D010802:Phylogeny; D011487:Protein Conformation
D006360:Heat-Shock Proteins; D000251:Adenosine Triphosphatases