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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1998-12-17
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
438
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
250-4
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9827555-Adenosine Triphosphatases,
pubmed-meshheading:9827555-Amino Acid Sequence,
pubmed-meshheading:9827555-Animals,
pubmed-meshheading:9827555-Bacteria,
pubmed-meshheading:9827555-Endopeptidase Clp,
pubmed-meshheading:9827555-Escherichia coli Proteins,
pubmed-meshheading:9827555-Fungal Proteins,
pubmed-meshheading:9827555-Genes, Fungal,
pubmed-meshheading:9827555-Mitochondria,
pubmed-meshheading:9827555-Mitochondrial Proteins,
pubmed-meshheading:9827555-Molecular Chaperones,
pubmed-meshheading:9827555-Molecular Sequence Data,
pubmed-meshheading:9827555-Nematoda,
pubmed-meshheading:9827555-Plants,
pubmed-meshheading:9827555-Saccharomyces cerevisiae,
pubmed-meshheading:9827555-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:9827555-Sequence Alignment,
pubmed-meshheading:9827555-Sequence Homology, Amino Acid
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pubmed:year |
1998
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pubmed:articleTitle |
Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae.
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pubmed:affiliation |
Institut für Physiologische Chemie der Universität München, Munich, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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