scholarly journals Expression of an ATP-binding cassette transporter-encoding gene (YOR1) is required for oligomycin resistance in Saccharomyces cerevisiae.

1995 ◽  
Vol 15 (12) ◽  
pp. 6875-6883 ◽  
Author(s):  
D J Katzmann ◽  
T C Hallstrom ◽  
M Voet ◽  
W Wysock ◽  
J Golin ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Fusion Gene ◽  
Sequence Similarity ◽  
Yeast Cells ◽  
Atp Binding ◽  
Zinc Cluster ◽  
Atp Binding Cassette Transporter ◽  
Transporter Family ◽  
Encoding Gene ◽  
Atp Binding Cassette

Semidominant mutations in the PDR1 or PDR3 gene lead to elevated resistance to cycloheximide and oligomycin. PDR1 and PDR3 have been demonstrated to encode zinc cluster transcription factors. Cycloheximide resistance mediated by PDR1 and PDR3 requires the presence of the PDR5 membrane transporter-encoding gene. However, PDR5 is not required for oligomycin resistance. Here, we isolated a gene that is necessary for PDR1- and PDR3-mediated oligomycin resistance. This locus, designated YOR1, causes a dramatic elevation in oligomycin resistance when present in multiple copies. A yor1 strain exhibits oligomycin hypersensitivity relative to an isogenic wild-type strain. In addition, loss of the YOR1 gene blocks the elevation in oligomycin resistance normally conferred by mutant forms of PDR1 or PDR3. The YOR1 gene product is predicted to be a member of the ATP-binding cassette transporter family of membrane proteins. Computer alignment indicates that Yor1p shows striking sequence similarity with multidrug resistance-associated protein, Saccharomyces cerevisiae Ycf1p, and the cystic fibrosis transmembrane conductance regulator. Use of a YOR1-lacZ fusion gene indicates that YOR1 expression is responsive to PDR1 and PDR3. While PDR5 expression is strictly dependent on the presence of PDR1 or PDR3, control of YOR1 expression has a significant PDR1/PDR3-independent component. Taken together, these data indicate that YOR1 provides the link between transcriptional regulation by PDR1 and PDR3 and oligomycin resistance of yeast cells.

scholarly journals A novel a-factor-related peptide of Saccharomyces cerevisiae that exits the cell by a Ste6p-independent mechanism.

1997 ◽  
Vol 8 (7) ◽  
pp. 1273-1291 ◽  
Author(s):  
P Chen ◽  
J D Choi ◽  
R Wang ◽  
R J Cotter ◽  
S Michaelis
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Culture Fluid ◽  
Proteolytic Processing ◽  
Atp Binding ◽  
Related Peptide ◽  
Atp Binding Cassette Transporter ◽  
Independent Mechanism ◽  
Cellular Machinery ◽  
Atp Binding Cassette

Many secreted signaling molecules are synthesized as precursors that undergo multiple maturation steps to generate their mature forms. The Saccharomyces cerevisiae mating pheromone a-factor is a C-terminally isoprenylated and carboxylmethylated dodecapeptide that is initially synthesized as a larger precursor containing 36 or 38 amino acids. We have previously shown that the maturation of a-factor occurs by an ordered biogenesis pathway involving 1) three C-terminal modification steps, 2) two N-terminal proteolytic processing events, and 3) a nonclassical export mechanism mediated by the ATP-binding-cassette (ABC) transporter Ste6p. In the present study, we demonstrate that an unexpected and abundant a-factor-related peptide (AFRP) exists in the culture fluid of MATa cells and that its biogenesis is integrally related to that of mature a-factor itself. We show by purification followed by mass spectrometry that AFRP corresponds to the C-terminal 7 amino acids (VFWDPAC) of mature a-factor (YIIKGVFWDPAC), including both the farnesyl- and carboxylmethylcysteine modifications. The formation and export of AFRP displays three striking features. First, we show that AFRP is produced intracellularly and that mutants (ste24 and axl1) that cannot produce mature a-factor due to an N-terminal processing defect are nevertheless normal for AFRP production. Thus, AFRP is not derived from mature a-factor but, instead, from the P1 form of the a-factor precursor. Second, fusion constructs with foreign amino acids substituted for authentic a-factor residues still yield AFRP-sized molecules; however, the composition of these corresponds to the altered residues instead of to AFRP residues. Thus, AFRP may be generated by a sequence-dependent but length-specific proteolytic activity. Third, a-factor and AFRP use distinct cellular machinery for their secretion. Whereas a-factor export is Ste6p-dependent, AFRP is secreted normally even in a ste6 deletion mutant. Thus, AFRP may exit the cell by another ATP-binding-cassette transporter, a different type of transporter altogether, or possibly by diffusion. Taken together, these studies indicate that the biogenesis of AFRP involves novel mechanisms and machinery, distinct from those used to generate mature a-factor. Because AFRP neither stimulates nor inhibits mating or a-factor halo activity, its function remains an intriguing question.

scholarly journals Selenodiglutathione uptake by the Saccharomyces cerevisiae vacuolar ATP-binding cassette transporter Ycf1p

FEBS Journal ◽  
2011 ◽  
Vol 278 (21) ◽  
pp. 4112-4121 ◽  
Author(s):  
Myriam Lazard ◽  
Nguyet-Thanh Ha-Duong ◽  
Stéphanie Mounié ◽  
Romary Perrin ◽  
Pierre Plateau ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Atp Binding ◽  
Atp Binding Cassette Transporter ◽  
Atp Binding Cassette

scholarly journals Structural and Functional Fingerprint of the Mitochondrial ATP-binding Cassette Transporter Mdl1 from Saccharomyces cerevisiae

2007 ◽  
Vol 282 (6) ◽  
pp. 3951-3961 ◽  
Author(s):  
Matthias Hofacker ◽  
Simone Gompf ◽  
Ariane Zutz ◽  
Chiara Presenti ◽  
Winfried Haase ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Atp Binding ◽  
Atp Binding Cassette Transporter ◽  
Atp Binding Cassette
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