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Free keywords:
ATPases Associated with Diverse Cellular Activities
Adenosine Triphosphatases/*chemistry
Amino Acid Sequence
Animals
Bacteria/metabolism
Endopeptidase Clp
Escherichia coli Proteins
Fungal Proteins/*chemistry
Genes, Fungal
Mitochondria/*metabolism
Mitochondrial Proteins
Molecular Chaperones/analysis/*chemistry/genetics
Molecular Sequence Data
Nematoda
Plants/metabolism
Saccharomyces cerevisiae/genetics/*metabolism
*Saccharomyces cerevisiae Proteins
Sequence Alignment
Sequence Homology, Amino Acid
Abstract:
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.
