Abstract
The yeast peroxisomal adenine nucleotide carrier, Ant1p, was shown to catalyse unidirectional transport in addition to exchange of substrates. In both transport modes, proton movement occurs. Nucleotide hetero-exchange is H+-compensated and electroneutral. Furthermore, microscopic fluorescence imaging of a pH-sensitive green fluorescent protein targeted to peroxisomes shows that Ant1p is involved in the formation of a DeltapH across the peroxisomal membrane, acidic inside.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenine Nucleotides / metabolism*
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Biological Transport, Active / physiology
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Cytosol / chemistry
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Hydrogen-Ion Concentration
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Intracellular Membranes / chemistry
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Nucleotide Transport Proteins / metabolism
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Nucleotide Transport Proteins / physiology*
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Peroxisomes / chemistry*
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Peroxisomes / metabolism
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Proton-Motive Force / physiology*
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Saccharomyces cerevisiae / chemistry
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Saccharomyces cerevisiae Proteins / metabolism
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Saccharomyces cerevisiae Proteins / physiology*
Substances
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ANT1 protein, S cerevisiae
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Adenine Nucleotides
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Nucleotide Transport Proteins
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Saccharomyces cerevisiae Proteins