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Free keywords:
Adenosine Triphosphatases/analysis/biosynthesis/chemistry/isolation &
purification/*metabolism
Adenosine Triphosphate/metabolism
Cell Membrane/enzymology
Fungal Proteins/analysis/chemistry/isolation & purification/*metabolism
Hydrolysis
Membrane Proteins/analysis/chemistry/isolation & purification/*metabolism
Metalloendopeptidases/chemistry/isolation & purification/*metabolism
Mitochondria/*enzymology
Mitochondrial Proteins
Molecular Chaperones/chemistry/isolation & purification/*metabolism
Molecular Weight
Saccharomyces cerevisiae
*Saccharomyces cerevisiae Proteins
Substrate Specificity
Abstract:
The mitochondrial members of the highly conserved AAA family, Yta10p and Yta12p, constitute a membrane-embedded complex of about 850 kDa. As an ATP dependent metallopeptidase (AAA protease), the YTA10-12 complex mediates the degradation of nonassembled inner membrane proteins. In contrast to nucleotide-dependent complex formation and substrate binding, proteolysis of bound polypeptides depends on the hydrolysis of ATP and the metallopeptidase activity of both subunits. Independent of its proteolytic function, the chaperone-like activity of the YTA10-12 complex is required for assembly of the membrane-associated ATP synthase. We propose that proteolytic and chaperone-like activities in the YTA10-12 complex mediate assembly and degradation processes of membrane protein complexes and thereby exert key functions in the maintenance of membrane integrity.
