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 Clp...
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| Published in | FEBS letters Vol. 438; no. 3; pp. 250 - 254 |
|---|---|
| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Elsevier B.V
06.11.1998
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| Subjects | |
| Online Access | Get full text |
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| 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. |
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| AbstractList | 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. 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. 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. |
| Author | Neupert, Walter van Dyck, Luc Langer, Thomas Dembowski, Markus |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/9827555$$D View this record in MEDLINE/PubMed |
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| Copyright | 1998 Federation of European Biochemical Societies FEBS Letters 438 (1998) 1873-3468 © 2015 Federation of European Biochemical Societies |
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| Snippet | Members of the Hsp100/Clp-family of molecular chaperones form regulatory subunits of ATP-dependent Clp proteases and fulfill crucial roles for cellular... Members of the Hsp100/Clp‐family of molecular chaperones form regulatory subunits of ATP‐dependent Clp proteases and fulfill crucial roles for cellular... |
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| SubjectTerms | 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 |
| Title | Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae |
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