Amino acid transport in eucaryotic microorganisms

Horák, J.

doi:10.1016/0304-4157(86)90001-8

Cited by 132 publications

(102 citation statements)

References 200 publications

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“…This finding reflects the unidirectionality of amino acid transport observed in whole yeast cells (for review see, e.g. [12]). Addition of low concentrations of nystatin (5-10 ktg/mg lipid) to the vesicles without ergosterol did not affect the arginine fluxes whereas in ergosterol-containing vesicles it caused a massive effiux of the accumulated arginine while the magnitude of the protonmotive force in the system remained largely unaffected.…”

Section: Introductionsupporting

confidence: 64%

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

et al. 1996

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Section: Introductionsupporting

confidence: 64%

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

et al. 1996

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“…Virtually no arginine uptake into nonenergized vesicles has been observed (not shown). When membrane potential was rapidly and completely abolished by 10 PM CCCP a considerably slower arginine leak occured as compared to the nystatin induced efflux (not shown), possibly in part reflecting the unidirectional nature of amino acid transport in yeast (for review see [15]). The slow release of arginine from the vesicles after addition of 10 ,uM CCCP is in contrast to what we observed in our previous study [7].…”

Section: Resultsmentioning

confidence: 96%

Nystatin changes the properties of transporters for arginine and sugars An in vitro study

Opekarová

Tanner

1994

FEBS Letters

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In ergosterol-containing energized yeast plasma membrane vesicles nystatin (5-10 &mg total lipid) caused a massive efRux of pre-accumulated arginine while the membrane potential (the principal driving force: -110 mV) decreased by onlv IO-30 mV. Neither the substrate fluxes nor the membrane potential was influenced by nyst&in when the p&nease was reconstituted in ergoste;ol-free phospholipid vesicles. The same effect of nystatin was found with the reconstituted sugar transporter from Chlorella kessleri. It is suggested that nystatin binding to ergosterol in the vicinity of the permease releases the transport protein from its coupling to energy and converts it to a facilitator.

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“…They were therefore not true revertants. Because the trait was recessive (Table l), it was unlikely to be a partial revertant of leu2 (Horak, 1986).…”

Section: Discussionmentioning

confidence: 99%

“…Leucine is presumed to enter S. cerevisiae cells by at least three routes (Horak, 1986;Ramos e t al., 1980;Wainer e t al., 1988). The first, called the general amino acid permease (GAP1) system after the permease gene G A P I , is a low-affinity, highvelocity pathway activated in response to nitrogen starvation (Grenson e t al., 1970).…”

Section: Introductionmentioning

confidence: 99%

Isolation of a conditional suppressor of leucine auxotrophy in Saccharomyces cerevisiae

Heinemann

Ankenbauer²,

Horecka³

1994

Microbiology

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OR 97403, USAPhenotypically and genotypically (/eu2-3,112) Leu-cells of Saccharomyces cerevisiae gave rise to small colonies on medium devoid of leucine. This only occurred on plates with a high density of Leu-cells or on medium supplemented with limiting quantities of leucine. Cells from these small colonies retained a growth advantage over their parent on limiting leucine supplements even after growth in a non-selecting (rich) medium. Therefore, the growth variants had acquired a heritable change. The phenotype was recessive and due to a change in a nuclear gene unlinked to the LEU2 locus. The phenotype provided a growth advantage only during leucine starvation; growth of the variants was indistinguishable from their parent on medium lacking the other essential supplements (histidine and uracil) required for the growth of the strain.[14C]Leucine uptake assays demonstrated that the variants were better able than their parents to accumulate leucine from their environments, and this ability extended to other hydrophobic amino acids. These results suggest that in the variants an amino acid uptake system has been derepressed rather than there having been reversion or extragenic suppression of the mutation in leucine biosynthesis. We designate the mutant gene responsible for the phenotype /up1 (for leucine uptake). The transport characteristics of the /up1 mutants suggested that LUPl is a regulatory component of an ammonium-regulated hydrophobic amino acid uptake system.

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Amino acid transport in eucaryotic microorganisms

Cited by 132 publications

References 200 publications

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

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

Nystatin changes the properties of transporters for arginine and sugars An in vitro study

Isolation of a conditional suppressor of leucine auxotrophy in Saccharomyces cerevisiae

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