title: The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria.
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.
authors.affiliation: Institut für Physiologische Chemie, Universität München, Federal Republic of Germany.
authors.forename: H
authors.initials: H
authors.lastname: Arlt
authors.forename: R
authors.initials: R
authors.lastname: Tauer
authors.forename: H
authors.initials: H
authors.lastname: Feldmann
authors.forename: W
authors.initials: W
authors.lastname: Neupert
authors.forename: T
authors.initials: T
authors.lastname: Langer
mesh_terms: D000251:Adenosine Triphosphatases / Q000032:analysis / Q000096:biosynthesis / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology; D005656:Fungal Proteins / Q000032:analysis / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D006868:Hydrolysis; D008565:Membrane Proteins / Q000032:analysis / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008666:Metalloendopeptidases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008928:Mitochondria / Q000201:enzymology*; D024101:Mitochondrial Proteins; D018832:Molecular Chaperones / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight; D012441:Saccharomyces cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D013379:Substrate Specificity
chemical_list: D005656:Fungal Proteins; D008565:Membrane Proteins; D024101:Mitochondrial Proteins; D018832:Molecular Chaperones; D029701:Saccharomyces cerevisiae Proteins; D000255:Adenosine Triphosphate; D008666:Metalloendopeptidases; D000251:Adenosine Triphosphatases; C102166:YTA12 protein, S cerevisiae; C090045:AFG3 protein, S cerevisiae