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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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ATPases Associated with Diverse Cellular Activities
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Adenosine Triphosphatases / chemistry*
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Amino Acid Sequence
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Animals
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Bacteria / metabolism
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Endopeptidase Clp
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Escherichia coli Proteins
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Fungal Proteins / chemistry*
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Genes, Fungal
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Mitochondria / metabolism*
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Mitochondrial Proteins
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Molecular Chaperones / analysis
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Molecular Chaperones / chemistry*
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Molecular Chaperones / genetics
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Molecular Sequence Data
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Nematoda
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Plants / metabolism
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins*
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Sequence Alignment
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Sequence Homology, Amino Acid
Substances
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Escherichia coli Proteins
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Fungal Proteins
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Mcx1 protein, S cerevisiae
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Mitochondrial Proteins
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Molecular Chaperones
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Saccharomyces cerevisiae Proteins
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Endopeptidase Clp
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Adenosine Triphosphatases
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ClpX protein, E coli
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ATPases Associated with Diverse Cellular Activities