Transmembrane ferricyanide reduction by cells of the yeastSaccharomyces cerevisiae

Crane, F.L.; Roberts, Henry; Linnane, Anthony W.; Löw, H.

doi:10.1007/bf00745020

Cited by 102 publications

(35 citation statements)

References 33 publications

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“…Crane et al reported a stoichiometric export of electrons and protons during ferricyanide reduction by yeast cells (12). With cultured carrot cells, however, Craig and Crane (11) observed a proton export which was 3-fold the reduction rate offerricyanide.…”

Section: Trans-plasma Membrane Electron Transfermentioning

confidence: 99%

Depolarization of Cell Membrane Potential during Trans-Plasma Membrane Electron Transfer to Extracellular Electron Acceptors in Iron-Deficient Roots of Phaseolus vulgaris L.

Sijmons

Lanfermeijer²,

Boer³

et al. 1984

Plant Physiol.

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Transfer of electrons from the cytosol of bean (Phaseolus vulgaris L.) root cells to extracellular acceptors such as ferricyanide and Fe"'EDTA causes a rapid depolarization of the membrane potential. This effect is most pronounced (3040 millivolts) with root cells of Fe-deficient plants, which have an increased capacity to reduce extracellular ferric salts.Ferrocyanide has no effect. In the state of ferricyanide reduction, H' (1H/2 electrons) and K' ions are excreted. The reduction of extracellular ferric salts by roots of Fe-deficient bean plants is driven by cellular NADPH (Sijmons, van den Briel, Bienfait 1984 Plant Physiol 75: 219-221). From this and from the membrane potential depolarization, we conclude that trans-plasma membrane electron transfer from NADPH is the primary process in the reduction of extracellular ferric salts.

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Section: Trans-plasma Membrane Electron Transfermentioning

confidence: 99%

Depolarization of Cell Membrane Potential during Trans-Plasma Membrane Electron Transfer to Extracellular Electron Acceptors in Iron-Deficient Roots of Phaseolus vulgaris L.

Sijmons

Lanfermeijer²,

Boer³

et al. 1984

Plant Physiol.

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“…In Escherichia coli, specific ferric binding compounds termed siderophores are secreted that bind and solubilize environmental iron and deliver it to specific receptors for transport across the outer and inner membranes (2). In the yeast Saccharomyces cerevisiae, the major iron uptake system under aerobic conditions depends on a transplasma membrane electron transport system (3,4) that reduces ferric iron external to the cell. Multicellular eukaryotes may also use an externally directed ferric reductase prior to transmembrane movement of ferrous iron (5)(6)(7)(8).…”

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confidence: 99%

Ferric reductase of Saccharomyces cerevisiae: molecular characterization, role in iron uptake, and transcriptional control by iron.

Dancis¹,

Roman²,

Anderson³

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

311

222

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The principal iron uptake system of Saccharomyces cerevisiae utilizes a reductase activity that acts on ferric iron chelates external to the cell. The FREI gene product is required for this activity. Iron is an essential nutrient that is required by many enzymes for cellular functions such as DNA synthesis and respiration. Ferric iron forms insoluble ferric hydroxide complexes in the presence of oxygen and water, making iron availability a biological problem under these conditions. Ferrous iron is much more soluble but is rapidly converted to ferric iron in the presence of oxygen (1). Cells have developed two major solutions to the problem of assimilation offerric iron from the environment. In Escherichia coli, specific ferric binding compounds termed siderophores are secreted that bind and solubilize environmental iron and deliver it to specific receptors for transport across the outer and inner membranes (2). In the yeast Saccharomyces cerevisiae, the major iron uptake system under aerobic conditions depends on a transplasma membrane electron transport system (3, 4) that reduces ferric iron external to the cell. Multicellular eukaryotes may also use an externally directed ferric reductase prior to transmembrane movement of ferrous iron (5-8). Our previous results indicated that the FREI gene product in S. cerevisiae is required for external ferric reduction and for ferric iron utilization, thus linking these two processes (9). However, a mutation in FREI did not affect the uptake offerrous iron (9), suggesting that the ferrous transport system is an independent component of the iron utilization apparatus in yeast. Many organisms control their rate of iron assimilation by ascertaining their requirement for iron and expressing a limiting component of the uptake system accordingly (10). Our previous results suggest that during aerobic growth of S. cerevisiae, changes in iron availability are reflected in alterations in the levels of FREI mRNA and of ferric iron uptake (9). In this paper we present the structure of the FREI gene and identify DNA sequences that mediate its regulation by ironA MATERIALS AND METHODSYeast Strains. The following yeast strains were derived from the wild-type strain F113 (MATa, can), inol-13, ura3-52): W103 (MATa, can], inol-13, ura3-52,frel-1) was derived by chemical mutagenesis of F113 and selection for a reductase-negative phenotype (9); W126 was derived by transformation of F113 with the plasmid pWDC20, which carries the FREI gene on the high-copy-number vector YEp24 (11). We used one-step gene disruption (12) to create strain N1 (MATa, can), inol-13, Afrel:: URA3), in which an 800-base-pair (bp) Xho I fragment internal to the FREI coding region was replaced with a URA3 marker gene, and strain N2 (MATa, can, inol-13, Afrel:: URA3), in which a 2.7-kilobase (kb) Cla I fragment containing the entire FREI coding region was similarly replaced. Disruption/deletion strains of the FREI locus were also constructed in the wild-type strain H1085, yielding strain W218 (MATa, leu2-3,112, ...

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“…An alternative mechanism has been proposed in which environmental ferric iron is initially solubilized by reduction, and the ferrous iron is then transported across the plasma membrane (9,25). A plasma membrane reductase activity able to reduce ferric iron has been observed in some bacterial strains, fungi, and plant and animal cells (3,5,16,19,22,29,30); however, it has not been possible to link the observed reductase activities with iron uptake. The latter is important because ferric reductase can be utilized in the plasma membrane for functions other than iron uptake.…”

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confidence: 99%

“…These cells have an externally directed ferric reductase activity in the plasma membrane that is regulated by the concentration of iron in the growth medium (5,15). We isolated a mutant lacking this plasma membrane reductase activity.…”

mentioning

confidence: 99%

Genetic evidence that ferric reductase is required for iron uptake in Saccharomyces cerevisiae.

Dancis¹,

Klausner²,

Hinnebusch³

et al. 1990

Mol. Cell. Biol.

267

217

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The requirement for a reduction step in cellular iron uptake has been postulated, and the existence of plasma membrane ferric reductase activity has been described in both procaryotic and eucaryotic cells. In the yeast Saccharomyces cerevisiae, there is an externally directed reductase activity that is regulated by the concentration of iron in the growth medium; maximal activity is induced by iron starvation. We report here the isolation of a mutant of S. cerevisiae lacking the reductase activity. This mutant is deficient in the uptake of ferric iron and is extremely sensitive to iron deprivation. Genetic analysis of the mutant demonstrates that the reductase and ferric uptake deficiencies are due to a single mutation that we designate frel-1. Both phenotypes cosegregate in meiosis, corevert with a frequency of 10-7, and are complemented by a 3.5-kilobase fragment of genomic DNA from wild-type S. cerevisiae. This fragment contains FREI, the wild-type allele of the mutant gene. The level of the gene transcript is regulated by iron in the same was as the reductase activity. The ferrous ion product of the reductase must traverse the plasma membrane. A high-affinity (Km = 5 ,uM) ferrous uptake system is present in both wild-type and mutant cells. Thus, iron uptake in S. cerevisiae is mediated by two plasma membrane components, a reductase and a ferrous transport system.

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Transmembrane ferricyanide reduction by cells of the yeastSaccharomyces cerevisiae

Cited by 102 publications

References 33 publications

Depolarization of Cell Membrane Potential during Trans-Plasma Membrane Electron Transfer to Extracellular Electron Acceptors in Iron-Deficient Roots of Phaseolus vulgaris L.

Depolarization of Cell Membrane Potential during Trans-Plasma Membrane Electron Transfer to Extracellular Electron Acceptors in Iron-Deficient Roots of Phaseolus vulgaris L.

Ferric reductase of Saccharomyces cerevisiae: molecular characterization, role in iron uptake, and transcriptional control by iron.

Genetic evidence that ferric reductase is required for iron uptake in Saccharomyces cerevisiae.

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