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• W83512084 abstract "Research Article1 July 1991free access A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria. B.M. Phipps B.M. Phipps Max-Planck Institute for Biochemistry, Martinsried, Germany. Search for more papers by this author A. Hoffmann A. Hoffmann Max-Planck Institute for Biochemistry, Martinsried, Germany. Search for more papers by this author K.O. Stetter K.O. Stetter Max-Planck Institute for Biochemistry, Martinsried, Germany. Search for more papers by this author W. Baumeister W. Baumeister Max-Planck Institute for Biochemistry, Martinsried, Germany. Search for more papers by this author B.M. Phipps B.M. Phipps Max-Planck Institute for Biochemistry, Martinsried, Germany. Search for more papers by this author A. Hoffmann A. Hoffmann Max-Planck Institute for Biochemistry, Martinsried, Germany. Search for more papers by this author K.O. Stetter K.O. Stetter Max-Planck Institute for Biochemistry, Martinsried, Germany. Search for more papers by this author W. Baumeister W. Baumeister Max-Planck Institute for Biochemistry, Martinsried, Germany. Search for more papers by this author Author Information B.M. Phipps1, A. Hoffmann1, K.O. Stetter1 and W. Baumeister1 1Max-Planck Institute for Biochemistry, Martinsried, Germany. The EMBO Journal (1991)10:1711-1722https://doi.org/10.1002/j.1460-2075.1991.tb07695.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info 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. Previous ArticleNext Article Volume 10Issue 71 July 1991In this issue RelatedDetailsLoading ..." @default.
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• W83512084 title "A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria." @default.
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