FKS1 mutations responsible for selective resistance of Saccharomyces cerevisiae to the novel 1,3-beta-glucan synthase inhibitor arborcandin C

Antimicrob Agents Chemother. 2004 Jan;48(1):319-22. doi: 10.1128/AAC.48.1.319-322.2004.

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

  • Amino Acid Sequence
  • Anti-Bacterial Agents / pharmacology*
  • Antifungal Agents / pharmacology*
  • DNA, Fungal / genetics
  • Drug Resistance, Fungal
  • Echinocandins
  • Enzyme Inhibitors / pharmacology*
  • Glucosyltransferases / antagonists & inhibitors*
  • Glucosyltransferases / genetics*
  • Glycopeptides
  • Membrane Proteins / genetics*
  • Molecular Sequence Data
  • Mutation / genetics
  • Peptides*
  • Plasmids / genetics
  • Saccharomyces cerevisiae / drug effects*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins / genetics*
  • Schizosaccharomyces pombe Proteins*

Substances

  • Anti-Bacterial Agents
  • Antifungal Agents
  • DNA, Fungal
  • Echinocandins
  • Enzyme Inhibitors
  • Glycopeptides
  • Membrane Proteins
  • Peptides
  • Saccharomyces cerevisiae Proteins
  • Schizosaccharomyces pombe Proteins
  • arborcandin C
  • Glucosyltransferases
  • 1,3-beta-glucan synthase
  • FKS1 protein, S cerevisiae

Associated data

  • GENBANK/AY395693
  • GENBANK/AY395694
  • GENBANK/AY395695