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The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria.

Cell | Jun 14, 1996

http://www.ncbi.nlm.nih.gov/pubmed/8681382

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.

Pubmed ID: 8681382 RIS Download

Mesh terms: Adenosine Triphosphatases | Adenosine Triphosphate | Cell Membrane | Fungal Proteins | Hydrolysis | Membrane Proteins | Metalloendopeptidases | Mitochondria | Mitochondrial Proteins | Molecular Chaperones | Molecular Weight | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Substrate Specificity

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