Abstract
Peroxisomal alcohol oxidase (AO) from Hansenula polymorpha is inactive and partially mislocalized to the cytosol upon synthesis in Saccharomyces cerevisiae. Co-production with H. polymorpha pyruvate carboxylase (HpPyc1p) resulted in AO activation, but did not improve import into peroxisomes. We show that import of AO mediated by S. cerevisiae Pex5p is strictly dependent on the peroxisomal targeting signal 1 (PTS1) of AO and independent of HpPyc1p. In contrast, HpPex5p-mediated sorting of AO into S. cerevisiae peroxisomes is independent of the PTS1, but requires an alternative PTS that is only formed when HpPyc1p is co-produced and most likely involves folding and co-factor binding to AO.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alcohol Oxidoreductases / genetics
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Alcohol Oxidoreductases / metabolism*
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Fungal Proteins / genetics
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Fungal Proteins / metabolism*
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Membrane Transport Proteins / genetics
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Membrane Transport Proteins / metabolism*
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Peroxisome-Targeting Signal 1 Receptor
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Peroxisomes / enzymology*
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Peroxisomes / genetics
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Pichia / enzymology*
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Pichia / genetics
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Protein Folding
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Protein Sorting Signals / genetics
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Protein Transport / physiology
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Receptors, Cytoplasmic and Nuclear
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Saccharomyces cerevisiae / enzymology*
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism
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Species Specificity
Substances
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Fungal Proteins
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Membrane Proteins
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Membrane Transport Proteins
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PEX5 protein, S cerevisiae
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Peroxisome-Targeting Signal 1 Receptor
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Protein Sorting Signals
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Receptors, Cytoplasmic and Nuclear
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Saccharomyces cerevisiae Proteins
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Alcohol Oxidoreductases
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alcohol oxidase