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Vol. 9, Issue 2, 375-386, February 1998
and
*Institut für Biochemie und Lebensmittelchemie and SFB
Biomembrane Research Center, Squalene epoxidase, encoded by the ERG1 gene in
yeast, is a key enzyme of sterol biosynthesis. Analysis of subcellular
fractions revealed that squalene epoxidase was present in the
microsomal fraction (30,000 × g) and also
cofractionated with lipid particles. A dual localization of Erg1p was
confirmed by immunofluorescence microscopy. On the basis of the
distribution of marker proteins, 62% of cellular Erg1p could be
assigned to the endoplasmic reticulum and 38% to lipid particles in
late logarithmic-phase cells. In contrast, sterol
Institut für Mikrobiologie,
24-methyltransferase (Erg6p), an enzyme catalyzing a
late step in sterol biosynthesis, was found mainly in lipid particles
cofractionating with triacylglycerols and steryl esters. The relative
distribution of Erg1p between the endoplasmic reticulum and lipid
particles changes during growth. Squalene epoxidase (Erg1p) was absent
in an erg1 disruptant strain and was induced fivefold in
lipid particles and in the endoplasmic reticulum when the
ERG1 gene was overexpressed from a multicopy plasmid.
The amount of squalene epoxidase in both compartments was also induced
approximately fivefold by treatment of yeast cells with terbinafine, an
inhibitor of the fungal squalene epoxidase. In contrast to the
distribution of the protein, enzymatic activity of squalene epoxidase
was only detectable in the endoplasmic reticulum but was absent from
isolated lipid particles. When lipid particles of the wild-type strain
and microsomes of an erg1 disruptant were mixed,
squalene epoxidase activity was partially restored. These findings
suggest that factor(s) present in the endoplasmic reticulum are
required for squalene epoxidase activity. Close contact between lipid
particles and endoplasmic reticulum may be necessary for a concerted
action of these two compartments in sterol biosynthesis.
Molecular Biology of the Cell
Vol. 9, 375-386, February 1998
Copyright © 1998 by The American Society for Cell Biology
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