Abstract
Arborcandin C is a novel antibiotic with potent antifungal activity that inhibits 1,3-beta-glucan synthase in fungi. We examined spontaneous Saccharomyces cerevisiae mutants which are selectively resistant to arborcandin C and revealed that a single amino acid replacement in Fks1p of Asn(470) with Lys or of Leu(642) with Ser confers selective resistance on Fks1p mutants.
MeSH terms
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Amino Acid Sequence
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Anti-Bacterial Agents / pharmacology*
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Antifungal Agents / pharmacology*
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DNA, Fungal / genetics
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Drug Resistance, Fungal
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Echinocandins
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Enzyme Inhibitors / pharmacology*
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Glucosyltransferases / antagonists & inhibitors*
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Glucosyltransferases / genetics*
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Glycopeptides
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Membrane Proteins / genetics*
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Molecular Sequence Data
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Mutation / genetics
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Peptides*
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Plasmids / genetics
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Saccharomyces cerevisiae / drug effects*
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae Proteins / genetics*
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Schizosaccharomyces pombe Proteins*
Substances
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Anti-Bacterial Agents
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Antifungal Agents
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DNA, Fungal
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Echinocandins
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Enzyme Inhibitors
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Glycopeptides
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Membrane Proteins
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Peptides
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Saccharomyces cerevisiae Proteins
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Schizosaccharomyces pombe Proteins
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arborcandin C
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Glucosyltransferases
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1,3-beta-glucan synthase
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FKS1 protein, S cerevisiae
Associated data
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GENBANK/AY395693
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GENBANK/AY395694
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GENBANK/AY395695