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PMID: 1828761 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria.

The EMBO journal ·Vol. 10 ·No. 7 ·1991-07-00 ·Pages 1711-22

Phipps BM, Hoffmann A, Stetter KO, Baumeister W

Abstract

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.

MeSH Terms
Adenosine Triphosphatases/isolation & purification,ultrastructure Archaea/enzymology,ultrastructure Chromatography, DEAE-Cellulose Cytoplasm/ultrastructure Electrophoresis, Polyacrylamide Gel Enzyme Stability Heat-Shock Proteins/isolation & purification,ultrastructure Image Processing, Computer-Assisted Immunoblotting Models, Molecular Phylogeny Protein Conformation
Chemicals
Heat-Shock Proteins Adenosine Triphosphatases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Phipps B M
Max-Planck Institute for Biochemistry, Martinsried, Germany.
Hoffmann A
Stetter K O
Baumeister W
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1991-07-00
Pages
1711-22
Language
English
Region
England
NLM ID
8208664
PMCID
PMC452842
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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