Characterization of peroxisome-deficient mutants of Hansenula polymorpha

Curr Genet. 1995 Aug;28(3):248-57. doi: 10.1007/BF00309784.

Abstract

In the methylotrophic yeast Hansenula polymorpha, approximately 25% of all methanol-utilization-defective (Mut-) mutants are affected in genes required for peroxisome biogenesis (PER genes). Previously, we reported that one group of per mutants, termed Pim-, are characterized by the presence of a few small peroxisomes with the bulk of peroxisomal enzymes located in the cytosol. Here, we describe a second major group of per mutants that were observed to be devoid of any peroxisome-like structure (Per-). In each Per- mutant, the peroxisomal methanol-pathway enzymes alcohol oxidase, catalase and dihydroxyacetone synthase were present and active but located in the cytosol. Together, the Pim- and Per- mutant collections involved mutations in 14 different PER genes. Two of the genes, PER5 and PER7, were represented by both dominant-negative and recessive alleles. Diploids resulting from crosses of dominant per strains and wild-type H. polymorpha were Mut- and harbored peroxisomes with abnormal morphology. This is the first report of dominant-negative mutations affecting peroxisome biogenesis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alcohol Oxidoreductases / metabolism
  • Aldehyde-Ketone Transferases*
  • Alleles
  • Catalase / metabolism
  • Crosses, Genetic
  • Cytosol / enzymology
  • Fungal Proteins / metabolism
  • Genes, Dominant
  • Genes, Fungal
  • Genes, Recessive
  • Methanol / metabolism
  • Microbodies*
  • Pichia / enzymology
  • Pichia / genetics*
  • Pichia / ultrastructure
  • Transferases / metabolism

Substances

  • Fungal Proteins
  • Alcohol Oxidoreductases
  • alcohol oxidase
  • Catalase
  • Transferases
  • Aldehyde-Ketone Transferases
  • formaldehyde transketolase
  • Methanol