Abstract
Thiol-disulphide redox regulation has a key role during the biogenesis of mitochondrial intermembrane space (IMS) proteins. Only the Cys-reduced form of precursor proteins can be imported into mitochondria, which is followed by disulphide bond formation in the mitochondrial IMS. In contrast to the wealth of knowledge on the oxidation process inside mitochondria, little is known about how precursors are maintained in an import-competent form in the cytosol. Here we provide the first evidence that the cytosolic thioredoxin system is required to maintain the IMS small Tim proteins in reduced forms and facilitate their mitochondrial import during respiratory growth.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cysteine / genetics
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Cytosol / enzymology*
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Gene Expression
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Glutaredoxins / genetics
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Glutaredoxins / metabolism
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Mitochondria / metabolism
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Mitochondrial Membrane Transport Proteins / metabolism*
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Mitochondrial Precursor Protein Import Complex Proteins
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Mutation
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Oxidation-Reduction
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Peroxiredoxins / genetics
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Peroxiredoxins / metabolism*
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Protein Precursors / metabolism
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Protein Transport
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Saccharomyces cerevisiae / enzymology
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism*
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Thioredoxins / genetics
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Thioredoxins / metabolism*
Substances
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Glutaredoxins
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Grx1 protein, S cerevisiae
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Grx2 protein, S cerevisiae
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Membrane Proteins
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Mitochondrial Membrane Transport Proteins
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Mitochondrial Precursor Protein Import Complex Proteins
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Protein Precursors
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Saccharomyces cerevisiae Proteins
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TIM10 protein, S cerevisiae
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TIM13 protein, S cerevisiae
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TRX1 protein, S cerevisiae
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TRX2 protein, S cerevisiae
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Tim9 protein, S cerevisiae
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Thioredoxins
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Peroxiredoxins
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Cysteine