Isolation and characterization of Schizosaccharomyces pombe mutants defective in cell wall (1-3)beta-D-glucan

J Bacteriol. 1991 Jun;173(11):3456-62. doi: 10.1128/jb.173.11.3456-3462.1991.

Abstract

Schizosaccharomyces pombe thermosensitive mutants requiring the presence of an osmotic stabilizer to survive and grow at a nonpermissive temperature were isolated. The mutants were genetically and biochemically characterized. In all of them, the phenotype segregated in Mendelian fashion as a single gene which coded for a recessive character. Fourteen loci were defined by complementation analysis. Studies of cell wall composition showed a reduction in the amount of cell wall beta-glucan in three strains (JCR1, JCR5, and JCR10) when growing at 37 degrees C. Galactomannan was diminished in two others. Strains JCR1 and JCR5, with mutant alleles cwg1-1 and cwg2-1, respectively, were further studied. The cwg1 locus was mapped on the right arm of chromosome III, 18.06 centimorgans (cM) to the left of the ade5 marker; cwg2 was located on the left arm of chromosome I, 34.6 cM away from the aro5 marker. (1-3)beta-D-Glucan synthase activities from cwg1-1 and cwg2-1 mutant strains grown at 37 degrees C were diminished, as measured in vitro, compared with the wild-type strain; however, Km values and activation by GTP were similar to the wild-type values. Mutant synthases behaved like the wild-type enzyme in terms of thermostability. Analyses of round shape, lytic behavior, and low (1-3)beta-D-glucan synthase activity in cultures derived from ascospores of the same tetrad showed cosegregation of all these characters. Detergent dissociation of (1-3)beta-D-glucan synthase into soluble and particulate fractions and subsequent reconstitution demonstrated that the cwg1-1 mutant was affected in the particulate fraction of the enzymatic activity while cwg2-1 was affected in the soluble component. The antifungal agents Papulacandin B and Aculeacin A had similar effects on the enzymatic activities of the wild type and the cwg2-1 mutant strain, whereas the cwg1-1 mutant, when growing at 37 degrees C, had a more inhibitor-resistant (1,3)beta-D-glucan synthase. It is concluded that the cwg1+ and cwg2+ genes are related to (1,3)beta-D-glucan biosynthesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aminoglycosides*
  • Anti-Bacterial Agents / pharmacology
  • Antifungal Agents / pharmacology
  • Antineoplastic Agents / metabolism*
  • Cell Division / drug effects
  • Cell Wall / chemistry
  • Cell Wall / metabolism*
  • Chromosome Mapping
  • Genetic Complementation Test
  • Genotype
  • Glucans / biosynthesis*
  • Glucosyltransferases / metabolism
  • Hot Temperature / adverse effects
  • Membrane Proteins*
  • Microscopy, Phase-Contrast
  • Mutagenesis
  • Peptides, Cyclic*
  • Schizosaccharomyces / genetics*
  • Schizosaccharomyces pombe Proteins*
  • Sorbitol / pharmacology
  • beta-Glucans*

Substances

  • Aminoglycosides
  • Anti-Bacterial Agents
  • Antifungal Agents
  • Antineoplastic Agents
  • Glucans
  • Membrane Proteins
  • Peptides, Cyclic
  • Schizosaccharomyces pombe Proteins
  • beta-Glucans
  • Sorbitol
  • aculeacin A
  • papulacandin B
  • beta-1,3-glucan
  • Glucosyltransferases
  • 1,3-beta-glucan synthase