Response to Iron Deprivation in
            <i>Saccharomyces cerevisiae</i>

Philpott, Caroline C.; Protchenko, Olga

doi:10.1128/ec.00354-07

Cited by 227 publications

(302 citation statements)

References 71 publications

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“…When iron is abundant in the environment, vacuoles accumulate it, and this sequestration protects cells from the toxic effect of iron and allows cells to utilize it when extracellular iron is scarce (PHILPOTT; PROTCHENKO, 2008). It could be suggested that the yeast containing intracellular iron, after 120 minutes of fermentation, might have mobilized the iron to use it in respiratory activities, explaining the increase in the volume of displaced water.…”

Section: Resultsmentioning

confidence: 99%

“…It is known that Saccharomyces cerevisiae requires certain quantity of iron that plays and important role in the reactions of citric acid cycle and in many parts of the respiratory chain (STEHLIK-THOMAS et al, 2003;PAS et al, 2007). It is also documented that the yeast Saccharomyces cerevisiae exhibits strategies to respond to iron availability fluctuations in its environment, including the mobilization of its intracellular stores (PHILPOTT; PROTCHENKO, 2008).…”

Section: Resultsmentioning

confidence: 99%

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Iron enriched Saccharomyces cerevisiae maintains its fermenting power and bakery properties

Gaensly¹,

Wille²,

Brand³

et al. 2011

Ciênc. Tecnol. Aliment.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Iron enriched Saccharomyces cerevisiae maintains its fermenting power and bakery properties

Gaensly¹,

Wille²,

Brand³

et al. 2011

Ciênc. Tecnol. Aliment.

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“…We measured both Fre1 mRNA levels and enzyme activity at 4 h after the addition of BPS and approximately threefold higher mRNA levels in both the control and Isu-UP cells (Fig. 4C, Upper), an expected response to iron limitation given that FRE1 is a target gene of the Aft transcription factor (23). However, although Fre1 enzyme activity in controls cells increased threefold in that 4-h span, the activity in Isu-UP cells did not change significantly (Fig.…”

Section: High Isu Levels Compromise Growth Under Iron-depleted Conditmentioning

confidence: 99%

Cysteine desulfurase Nfs1 and Pim1 protease control levels of Isu, the Fe-S cluster biogenesis scaffold

Song

Marszałek

Craig

2012

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

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Fe-S clusters are critical prosthetic groups for proteins involved in various critical biological processes. Before being transferred to recipient apo-proteins, Fe-S clusters are assembled on the highly conserved scaffold protein Isu, the abundance of which is regulated posttranslationally on disruption of the cluster biogenesis system. Here we report that Isu is degraded by the Lon-type AAA+ ATPase protease of the mitochondrial matrix, Pim1. Nfs1, the cysteine desulfurase responsible for providing sulfur for cluster formation, is required for the increased Isu stability occurring after disruption of cluster formation on or transfer from Isu. Physical interaction between the Isu and Nfs1 proteins, not the enzymatic activity of Nfs1, is the important factor in increased stability. Analysis of several conditions revealed that high Isu levels can be advantageous or disadvantageous, depending on the physiological condition. During the stationary phase, elevated Isu levels were advantageous, resulting in prolonged chronological lifespan. On the other hand, under iron-limiting conditions, high Isu levels were deleterious. Compared with cells expressing normal levels of Isu, such cells grew poorly and exhibited reduced activity of the heme-containing enzyme ferric reductase. Our results suggest that modulation of the degradation of Isu by the Pim1 protease is a regulatory mechanism serving to rapidly help balance the cell's need for critical ironrequiring processes under changing environmental conditions. proteolysis | Hsp70 | aging | Saccharomyces cerevisiae

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“…We wondered whether iron metabolism in insects requires the activity of a multicopper ferroxidase. Given that ferroxidases are necessary for iron metabolism in a diverse set of organisms (2,3,6,7,13,14), it seemed likely that they would exist in insects. On the contrary, the multicopper ferroxidases with known physiological functions work in conjunction with an iron permease (2-5), whereas we and others have been unable to identify an iron permease gene in any insect genome (9).…”

mentioning

confidence: 99%

“…Redox cycling between the two oxidation states is a critical aspect of iron metabolism because the two forms of iron have different properties: ferrous iron is soluble under most physiological conditions, but it participates in toxic radical formation, whereas ferric iron does not promote radical formation, but it is highly insoluble (1). Multicopper ferroxidases in yeast and algae function in the uptake of iron by oxidizing ferrous to ferric iron, which is then transported into the cell by a ferric iron permease (2,3). The mammalian ferroxidases, hephaestin and ceruloplasmin, facilitate iron efflux by oxidizing extracellular ferrous iron that has been transported out of cells by a ferrous iron permease (ferroportin) (4,5).…”

mentioning

confidence: 99%

Multicopper oxidase-1 is a ferroxidase essential for iron homeostasis in Drosophila melanogaster

Lang

Braun

Kanost

et al. 2012

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

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Multicopper ferroxidases catalyze the oxidation of ferrous iron to ferric iron. In yeast and algae, they participate in cellular uptake of iron; in mammals, they facilitate cellular efflux. The mechanisms of iron metabolism in insects are still poorly understood, and insect multicopper ferroxidases have not been identified. In this paper, we present evidence that Drosophila melanogaster multicopper oxidase-1 (MCO1) is a functional ferroxidase. We identified candidate iron-binding residues in the MCO1 sequence and found that purified recombinant MCO1 oxidizes ferrous iron. An association between MCO1 function and iron homeostasis was confirmed by two observations: RNAi-mediated knockdown of MCO1 resulted in decreased iron accumulation in midguts and whole insects, and weak knockdown increased the longevity of flies fed a toxic concentration of iron. Strong knockdown of MCO1 resulted in pupal lethality, indicating that MCO1 is an essential gene. Immunohistochemistry experiments demonstrated that MCO1 is located on the basal surfaces of the digestive system and Malpighian tubules. We propose that MCO1 oxidizes ferrous iron in the hemolymph and that the resulting ferric iron is bound by transferrin or melanotransferrin, leading to iron storage, iron withholding from pathogens, regulation of oxidative stress, and/or epithelial maturation. These proposed functions are distinct from those of other known ferroxidases. Given that MCO1 orthologues are present in all insect genomes analyzed to date, this discovery is an important step toward understanding iron metabolism in insects.

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Response to Iron Deprivation in Saccharomyces cerevisiae

Cited by 227 publications

References 71 publications

Iron enriched Saccharomyces cerevisiae maintains its fermenting power and bakery properties

Iron enriched Saccharomyces cerevisiae maintains its fermenting power and bakery properties

Cysteine desulfurase Nfs1 and Pim1 protease control levels of Isu, the Fe-S cluster biogenesis scaffold

Multicopper oxidase-1 is a ferroxidase essential for iron homeostasis in Drosophila melanogaster

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