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(Received for publication, March 18, 1996, and in revised form, May 20, 1996)
From the Department of Anatomy and Cell Biology, University of
Alberta, Edmonton, Alberta T6G 2H7, Canada
We previously reported the cloning of the
PAY5 gene of the yeast Yarrowia lipolytica by
complementation of the peroxisome assembly mutant pay5-1
(Eitzen, G. A., Titorenko, V. I., Smith, J. J., Veenhuis, M., Szilard,
R. K., and Rachubinski, R. A. (1996) J. Biol. Chem.
271, 20300-20306). The peroxisomal integral membrane protein Pay5p is
a homologue of mammalian PAF-1 proteins, which are essential for
peroxisome assembly and whose mutation in humans results in peroxisome
biogenesis disorders. Mutations in the PAY5 gene result in
the accumulation of three distinct peroxisomal subpopulations. These
subpopulations are characterized by differences in 1) buoyant density,
2) the relative distribution of peroxisomal matrix and membrane
proteins, 3) the efficiency of import of several peroxisomal matrix
proteins, and 4) the phospholipid levels of peroxisomal membranes.
These data, together with the analysis of temporal changes in the
relative abundance of individual peroxisomal subpopulations in
pay5 mutants, suggest that these subpopulations represent
intermediates in a multistep peroxisome assembly pathway normally
operating in yeast cells.
Volume 271, Number 34,
Issue of August 23, 1996
pp. 20307-20314
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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