Abstract
Expression of the pro-apoptotic protein Bax in yeast Saccharomyces cerevisiae induces a release of cytochrome c accompanied by a decrease of the amount of cytochrome c oxidase. Here we show that the decrease of cytochrome c oxidase is due to the activation of mitochondrial protease Yme1p, of which cytochrome c oxidase subunit 2 (Cox2p) is a substrate. The absence of Yme1p slightly delays Bax-induced cell death, suggesting a role of this protease in yeast cell death and thus of its mammalian homologue in apoptosis.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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ATP-Dependent Proteases
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Adenosine Triphosphatases / genetics
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Adenosine Triphosphatases / metabolism*
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Apoptosis / physiology
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Cell Respiration
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Electron Transport Complex IV / metabolism*
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Genes, Fungal
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Genes, myc
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Humans
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In Vitro Techniques
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Mitochondria / enzymology
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Phenotype
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Proto-Oncogene Proteins / genetics
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Proto-Oncogene Proteins / metabolism*
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Proto-Oncogene Proteins c-bcl-2*
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Saccharomyces cerevisiae / cytology
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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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bcl-2-Associated X Protein
Substances
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BAX protein, human
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Proto-Oncogene Proteins
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Proto-Oncogene Proteins c-bcl-2
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Saccharomyces cerevisiae Proteins
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bcl-2-Associated X Protein
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Electron Transport Complex IV
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ATP-Dependent Proteases
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YME1 protein, S cerevisiae
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Adenosine Triphosphatases