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

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

Authors

  • Arlt H
  • Tauer R
  • Feldmann H
  • Neupert W
  • Langer T

Journal

Cell

Publication Data

June 14, 1996

Associated Grants

None

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