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J. Biol. Chem., Vol. 269, Issue 6, 4180-4186, 02, 1994
PH Bissinger and K Kuchler
We have cloned a yeast gene that confers a multidrug resistance phenotype
on Saccharomyces cerevisiae when present in multiple copies. The STS1 (for
Sporidesmin Toxicity Suppressor) gene encodes a 1511- residue protein whose
predicted structural organization is characterized by 12 alpha-helical
membrane segments and two domains containing consensus sites for ATP
binding, indicating that STS1 is a new yeast ATP-binding cassette (ABC)
transporter. A chromosomal deletion of STS1 leads to viable delta sts1
cells of both mating types, suggesting that STS1 is not essential for cell
growth. However, delta sts1 cells exhibit supersensitivity to sporidesmin
and to other structurally unrelated drugs such as cycloheximide.
Conversely, overexpression of STS1 leads to increased resistance to the
same drugs. Although Northern analysis showed that STS1 mRNA is present in
all yeast cell types, its drastically reduced level in alpha-factor-
arrested cells indicates that expression of STS1 is regulated by mating
pheromones. Subcellular fractionation and immunoblotting using monoclonal
antibodies, which recognize a fully functional epitope- tagged Sts1
protein, showed that Sts1 is a 175-kDa membrane protein localized mainly to
intracellular membranes.
Molecular cloning and expression of the Saccharomyces cerevisiae STS1 gene product. A yeast ABC transporter conferring mycotoxin resistance
Ag Research Ltd., Crown Research Institute of Pastoral Agricultural Research, Hamilton, New Zealand.
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T. C. Hallstrom and W. S. Moye-Rowley Multiple Signals from Dysfunctional Mitochondria Activate the Pleiotropic Drug Resistance Pathway in Saccharomyces cerevisiae J. Biol. Chem., November 22, 2000; 275(48): 37347 - 37356. [Abstract] [Full Text] [PDF]
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