Cloning and characterization of KNR4, a yeast gene involved in (1,3)-beta-glucan synthesis

Mol Cell Biol. 1994 Feb;14(2):1017-25. doi: 10.1128/mcb.14.2.1017-1025.1994.

Abstract

k9 killer toxin from Hansenula mrakii was used to select a number of resistant mutants from Saccharomyces cerevisiae. Preliminary biochemical and genetic studies showed that some of them acquired structural defects in the cell wall. One of these mutants, the knr4-1 mutant, displays a number of cell wall defects, including osmotic sensitivity; sensitivity to cercosporamide, a known antifungal agent; and resistance to Zymolyase, a (1,3)-beta-glucanase. We report here the isolation and analysis of the KNR4 gene. DNA sequence analysis revealed an uninterrupted open reading frame which contains five potential start codons. The longest coding template encodes a protein of 505 amino acids with a calculated molecular mass of 57,044 Da. A data base search revealed 100% identity with a nuclear protein, SMI1p. Disruption of the KNR4 locus does not result in cell death; however, it leads to reduced levels of both (1,3)-beta-glucan synthase activity and (1,3)-beta-glucan content in the cell wall. The gene was mapped to the right arm of chromosome VII.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Benzofurans / toxicity
  • Blotting, Western
  • Chromosomes, Fungal
  • Cloning, Molecular / methods
  • DNA, Fungal / isolation & purification
  • DNA, Fungal / metabolism
  • Drug Resistance, Microbial / genetics*
  • Fungal Proteins / biosynthesis*
  • Fungal Proteins / genetics
  • Fungal Proteins / isolation & purification
  • Genes, Fungal*
  • Glucans / biosynthesis*
  • Glucosyltransferases / biosynthesis*
  • Glucosyltransferases / metabolism
  • Hydrolases / toxicity
  • Killer Factors, Yeast
  • Kinetics
  • Membrane Proteins*
  • Molecular Sequence Data
  • Molecular Weight
  • Open Reading Frames
  • Pichia / metabolism
  • Protein Biosynthesis
  • Proteins / toxicity
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / isolation & purification
  • Restriction Mapping
  • Saccharomyces cerevisiae / drug effects
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins*
  • Schizosaccharomyces pombe Proteins*
  • Sequence Homology, Amino Acid
  • Transcription Factors
  • beta-Glucans*

Substances

  • Benzofurans
  • DNA, Fungal
  • Fungal Proteins
  • Glucans
  • Killer Factors, Yeast
  • Membrane Proteins
  • Proteins
  • Recombinant Proteins
  • SMI1 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Schizosaccharomyces pombe Proteins
  • Transcription Factors
  • beta-Glucans
  • cercosporamide
  • zymolyase
  • beta-1,3-glucan
  • Glucosyltransferases
  • 1,3-beta-glucan synthase
  • Hydrolases

Associated data

  • GENBANK/L13164