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

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 degrada...