Yta10p is required for the ATP-dependent degradation of polypeptides in the inner membrane of mitochondria

• Published in: FEBS letters Vol. 353; no. 2; pp. 201 - 206
• Main Authors: Pajic, Alexander, Tauer, Reimund, Feldmann, Horst, Neupert, Walter, Langer, Thomas
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 17.10.1994
• Subjects: Adenosine Triphosphatases; Adenosine Triphosphate - metabolism; Adenosine Triphosphate - pharmacology; ATP-dependent proteolysis; ATPase family; Binding Sites; Cations, Divalent; Fungal Proteins - metabolism; Hydrolysis; Intracellular Membranes - enzymology; Kinetics; Mitochondria - enzymology; Mitochondria - ultrastructure; Mitochondrial inner membrane; PCR, polymerase chain reaction; Peptides - metabolism; PMSF, phenylmethylsulfonylfluoride; Protein Folding; Saccharomyces cerevisiae; Saccharomyces cerevisiae - enzymology; Saccharomyces cerevisiae Proteins; YTA, Yeast Tat binding Analogue; YTA10; ATPase family; Mitochondrial inner membrane; PMSF, phenylmethylsulfonylfluoride; YTA10; PCR, polymerase chain reaction; ATP-dependent proteolysis; YTA, Yeast Tat binding Analogue
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(94)01046-3

Incompletely synthesized polypeptides in the mitochondrial inner membrane are subject to rapid proteolysis. We demonstrate that Yta10p, a mitochondrial homologue of a conserved family of putative ATPases in Saccharomyces cerevisiae, is essential for this proteolytic process. Yta10p-dependent degradation requires divalent metal ions and the hydrolysis of ATP. Yta 10p is an integral protein of the inner mitochondrial membrane exposing the carboxy terminus to the mitochondrial matrix space. Based on the presence of consensus binding sites for ATP, and for divalent metal ions found in a number of metal dependent endopeptidases, a direct role of Yta10p in the proteolytic breakdown of membrane-associated polypeptides in mitochondria is suggested.