Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae.
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.
van Dyck
L
L
Institut für Physiologische Chemie der Universität München, Munich, Germany.
Dembowski
M
M
Neupert
W
W
Langer
T
T
D000074183:ATPases Associated with Diverse Cellular Activities; D000251:Adenosine Triphosphatases / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria / Q000378:metabolism; D049071:Endopeptidase Clp; D029968:Escherichia coli Proteins; D005656:Fungal Proteins / Q000737:chemistry*; D005800:Genes, Fungal; D008928:Mitochondria / Q000378:metabolism*; D024101:Mitochondrial Proteins; D018832:Molecular Chaperones / Q000032:analysis / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D009348:Nematoda; D010944:Plants / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D029968:Escherichia coli Proteins; D005656:Fungal Proteins; C115923:Mcx1 protein, S cerevisiae; D024101:Mitochondrial Proteins; D018832:Molecular Chaperones; D029701:Saccharomyces cerevisiae Proteins; D049071:Endopeptidase Clp; D000251:Adenosine Triphosphatases; C088072:ClpX protein, E coli; D000074183:ATPases Associated with Diverse Cellular Activities