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A more recent version of this article appeared on March 1, 2003
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Submitted on October 4, 2002
Revised on October 31, 2002
Accepted on November 6, 2002
1 Department of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada
* Corresponding author. E-mail address: rick.rachubinski{at}ualberta.ca.
Pex3p is a peroxisomal integral membrane protein required early in peroxisome biogenesis, and Pex3p-deficient cells lack identifiable peroxisomes. Two temperature-sensitive pex3 mutant strains of the yeast Yarrowia lipolytica were made to investigate the role of Pex3p in the early stages of peroxisome biogenesis. In glucose medium at 16°C, these mutants underwent de novo peroxisome biogenesis and exhibited early matrix protein sequestration into peroxisome-like structures found at the endoplasmic reticulum-rich periphery of cells or sometimes associated with nuclei. De novo peroxisome biogenesis appeared unsynchronized, with peroxisomes appearing at different stages of development both within cells and between cells. Cells with peripheral nascent peroxisomes and cells with structures morphologically distinct from peroxisomes - semi/circular tubular structures that immunostained with antibodies to peroxisomal matrix proteins and to the endoplasmic reticulum-resident protein, Kar2p, and that surrounded lipid droplets - were observed during upregulation of peroxisome biogenesis in cells incubated in oleic acid medium at 16°C. These structures were not detected in wild-type or Pex3p-deficient cells. Their role in peroxisome biogenesis remains unclear. Targeting of peroxisomal matrix proteins to these structures suggests that Pex3p directly or indirectly sequesters components of the peroxisome biogenesis machinery. Such a role is consistent with Pex3p overexpression producing cells with fewer, larger and clustered peroxisomes.
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