Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae

• Published in: FEBS letters Vol. 438; no. 3; pp. 250 - 254
• Main Authors: van Dyck, Luc, Dembowski, Markus, Neupert, Walter, Langer, Thomas
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 06.11.1998
• Subjects: Adenosine Triphosphatases - chemistry; Amino Acid Sequence; Animals; ATPases Associated with Diverse Cellular Activities; Bacteria - metabolism; ClpX; Endopeptidase Clp; Escherichia coli Proteins; Fungal Proteins - chemistry; Genes, Fungal; Hsp100; Mitochondria - metabolism; Mitochondrial Proteins; Mitochondrion; Molecular chaperone; Molecular Chaperones - analysis; Molecular Chaperones - chemistry; Molecular Chaperones - genetics; Molecular Sequence Data; Nematoda; Plants - metabolism; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Mitochondrion; ClpX; Hsp100; Molecular chaperone
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(98)01310-6

Members of the Hsp100/Clp-family of molecular chaperones form regulatory subunits of ATP-dependent Clp proteases and fulfill crucial roles for cellular thermotolerance. We have identified a Clp-like protein in Saccharomyces cerevisiae, Mcx1p, which shares approximately 30% sequence identity with ClpX-proteins in bacteria, plants and nematodes. Mcx1p localizes to the matrix space of mitochondria and is peripherally associated with the inner membrane. A homologue of E. coli ClpP protease was not identified when screening the yeast genome. We therefore propose that Mcx1p represents a novel molecular chaperone of mitochondria with non-proteolytic function.