Possible nystatin‐protein interaction in yeast plasma membrane vesicles in the presence of ergosterol. A Förster energy transfer study

Opekarová, Miroslava; Urbanova, Petra; Konopásek, Ivo; Kvasnička, P.; Strzałka, Kazimierz; Sigler, Karel; Amler, Evžen

doi:10.1016/0014-5793(96)00434-6

Cited by 7 publications

(4 citation statements)

References 21 publications

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“…We therefore speculate that the antifungal activity of fenpropimorph depends on the membrane composition, specifically on the content of very-long-chain fatty acids and/or sphingolipids, and that fenpropimorph interacts directly with these membrane components. The inhibition of fungal growth by the structurally different antifungal polyene antibiotics, such as amphotericin B and nystatin, is also due to an interaction with specific membrane components (41,42).…”

Section: Fen2 Belongs To a Gene Family Encoding Eight Putative Transpmentioning

confidence: 99%

The Fenpropimorph Resistance Gene FEN2 fromSaccharomyces cerevisiae Encodes a Plasma Membrane H+-Pantothenate Symporter

Stolz

Sauer

1999

Journal of Biological Chemistry

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The product of the FEN2 gene of Saccharomyces cerevisiae has previously been described as a protein conferring sensitivity to the antifungal agent fenpropimorph. Fen2p was postulated to act as a common regulator of carbon and nitrogen catabolite repression and of amino acid and ergosterol biosynthesis. In this paper, we present experimental evidence characterizing Fen2p as a plasma membrane-localized transporter for the vitamin pantothenate. The high affinity transport system (K m ‫؍‬ 3.5 M) is sensitive to uncouplers, suggesting a H ؉ -pantothenate cotransport. Pantothenate transport rates in yeast are modulated by extracellular pantothenate, being maximal at low pantothenate concentrations. It is demonstrated that ␤-alanine can suppress the growth defect of FEN2 wild-type and fen2 mutant cells on pantothenate-free medium. Evidence is presented that ␤-alanine is transported by the general amino acid permease Gap1p. The relation among pantothenate transport, nitrogen catabolite repression, and sensitivity to the antifungal agent fenpropimorph is discussed.

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Section: Fen2 Belongs To a Gene Family Encoding Eight Putative Transpmentioning

confidence: 99%

The Fenpropimorph Resistance Gene FEN2 fromSaccharomyces cerevisiae Encodes a Plasma Membrane H+-Pantothenate Symporter

Stolz

Sauer

1999

Journal of Biological Chemistry

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“…In several reconstitution experiments employing mammalian and higher plant plasma membrane proteins, even more specific roles of sterols have been documented [24–27]. In vitro studies of the effect of nystatin on the activity of arginine transporter in yeast suggested a close interaction of the permease with ergosterol molecules [28, 29].…”

Section: Resultsmentioning

confidence: 99%

Expression of eukaryotic plasma membrane transporter HUP1 fromChlorella kessleriinEscherichia coli

Opekarová¹,

Robl²,

Graßl³

et al. 1999

FEMS Microbiology Letters

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To study the effect of sterols on the activity of the eukaryotic plasma membrane transporter, the hexose-proton symporter HUP1 from the unicellular alga Chlorella kessleri was expressed in Escherichia coli, a prokaryotic microorganism containing virtually no sterols. Under certain conditions, the recombinant protein was partially active in this prokaryotic organism. The heterologously produced HUP1p was purified from membrane fractions of E. coli and reconstituted in an in vitro system. The presence of ergosterol during solubilization, purification and reconstitution resulted in an increased activity of the reconstituted protein. Its activity, however, was 5-6 times lower as compared to the activity of HUP1p produced in Saccharomyces cerevisiae membranes and solubilized, purified, and reconstituted under the same conditions as above.

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“…The hexose transporter from C. vulgaris, Hup1, has also been suggested to contain a native substrate leak [68]. Interestingly, coupling is fully abolished in the presence of the antibiotic nystatin, which interacts with sterols in the membrane but does not form pores [69][70][71]. This may imply the native leak of Hup1 is associated with the presence or absence of sterols.…”

Section: Alteration Of Leak Pathways In Symportersmentioning

confidence: 99%

Coupling efficiency of secondary active transporters

Henderson

Fendler

Poolman

2019

Current Opinion in Biotechnology

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Possible nystatin‐protein interaction in yeast plasma membrane vesicles in the presence of ergosterol. A Förster energy transfer study

Cited by 7 publications

References 21 publications

The Fenpropimorph Resistance Gene FEN2 fromSaccharomyces cerevisiae Encodes a Plasma Membrane H+-Pantothenate Symporter

The Fenpropimorph Resistance Gene FEN2 fromSaccharomyces cerevisiae Encodes a Plasma Membrane H+-Pantothenate Symporter

Expression of eukaryotic plasma membrane transporter HUP1 fromChlorella kessleriinEscherichia coli

Coupling efficiency of secondary active transporters

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