Alcohol oxidase and dihydroxyacetone synthase, the abundant peroxisomal proteins of methylotrophic yeasts, assemble in different cellular compartments.

Academic Article


  • Alcohol oxidase (AO) and dihydroxyacetone synthase (DHAS) constitute the bulk of matrix proteins in methylotrophic yeasts, model organisms for the study of peroxisomal assembly. Both are homooligomers; AO is a flavin-containing octamer, whereas DHAS is a thiamine pyrophosphate-containing dimer. Experiments in recent years have demonstrated that assembly of peroxisomal oligomers can occur before import; indeed the absence of chaperones within the peroxisomal matrix calls into question the ability of this compartment to assemble proteins at all. We have taken a direct pulse-chase approach to monitor import and assembly of the two major proteins of peroxisomes in Candida boidinii. Oligomers of AO are not observed in the cytosol, consistent with the proteins inability to undergo piggyback import. Indeed, oligomerization of AO can be followed within the peroxisomal matrix, directly demonstrating the capacity of this compartment for protein assembly. By contrast, DHAS quickly dimerizes in the cytosol before import. Binding and import was slowed at 15 degrees C; the effect on AO was more dramatic. In conclusion, our data indicate that peroxisomes assemble AO in the matrix, while DHAS undergoes dimerization prior to import.
  • Authors

  • Stewart, Mary
  • Esposito, RD
  • Gowani, J
  • Goodman, JM
  • Status

    Publication Date

  • August 2001
  • Published In


  • Alcohol Oxidoreductases
  • Aldehyde-Ketone Transferases
  • Candida
  • Cell Compartmentation
  • Cell Fractionation
  • Cytosol
  • Molecular Chaperones
  • Peroxisomes
  • Protein Transport
  • Digital Object Identifier (doi)

    Pubmed Id

  • 11683419
  • Start Page

  • 2863
  • End Page

  • 2868
  • Volume

  • 114
  • Issue

  • Pt 15