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An amphitropic cAMP-binding protein in yeast mitochondria. 1. Synergistic control of the intramitochondrial location by calcium and phospholipid

Journal Article · · Biochemistry; (USA)
DOI:https://doi.org/10.1021/bi00452a013· OSTI ID:6921668
 [1];  [2]
  1. Institut fuer Pathologie und Rechtsmedizin der Universitaet Ulm (West Germany)
  2. Institut fuer Genetik und Mikrobiologie der Universitaet Muenchen (West Germany)

A cAMP-binding protein is found to be integrated into the inner mitochondrial membrane of the yeast Saccharomyces cerevisiae under normal conditions. It resists solubilization by high salt and chaotropic agents. The protein is, however, converted to a soluble form which ten residues in the intermembrane space, when isolated mitochondria are incubated with low concentrations of calcium. Phospholipids or diacylglycerol (or analogues) dramatically increases the efficiency of receptor release from the inner membrane, whereas these compounds alone are ineffective. Photoaffinity labeling with 8-N{sub 3}-({sup 32}P)cAMP followed by mitochondrial subfractionation and sodium dodecyl sulfate-polyacrylamide gel electrophoresis does not reveal differences in the apparent molecular weight between the membrane-bound and the soluble form of the cAMP receptor. The two forms differ, however, in the partitioning behavior in Triton X-114 as well as in their protease resistance, indicating that the release from the membrane is accompanied by a change in lipophilicity and conformation of the receptor protein. Evidence is presented that a change of the intramitochondrial location of the yeast cAMP-binding protein also occurs in vivo and leads to the activation of a mitochondrial cAMP-dependent protein kinase. The cAMP-binding protein is the first example of a mitochondrial protein with amphitropic character; i.e., it has the property to occur in two different locations as a membrane-embedded and a soluble form.

OSTI ID:
6921668
Journal Information:
Biochemistry; (USA), Journal Name: Biochemistry; (USA) Vol. 28:26; ISSN 0006-2960; ISSN BICHA
Country of Publication:
United States
Language:
English