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Yta10p is required for the ATP‐dependent degradation of polypeptides in the inner membrane of mitochondria
Author(s) -
Pajic Alexander,
Tauer Reimund,
Feldmann Horst,
Neupert Walter,
Langer Thomas
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01046-3
Subject(s) - inner membrane , inner mitochondrial membrane , proteolysis , atp hydrolysis , mitochondrion , divalent , biochemistry , translocase of the inner membrane , atpase , mitochondrial carrier , chemistry , integral membrane protein , cytosol , saccharomyces cerevisiae , microbiology and biotechnology , biophysics , membrane protein , biology , membrane , mitochondrial membrane transport protein , bacterial outer membrane , enzyme , yeast , organic chemistry , escherichia coli , gene
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.