Degradation of glutathione in<i>Aspergillus nidulans</i>— Short communication

Spitzmüller, Zsolt; Hajdu, Márton; Pócsi, István; Emri, Tamás

doi:10.1556/018.66.2015.2.10

Cited by 3 publications

(2 citation statements)

References 10 publications

(12 reference statements)

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“…For example, the GlrA enzyme with GR activity plays an important role in the oxidative stress defense system of the fungus [12] and also in the reduction of cytotoxic elemental sulfur [34]. Interestingly, meanwhile GstA and GstB GSTs take part in the degradation of various toxic xenobiotics [19,34] and even in the detoxification of metals (GstA, [35]), GgtA γ-glutamyl transpeptidase is not necessary for the bulk degradation of GSH [36]. Instead, the DUG pathway relying on Dug1-3 proteins is likely to be responsible for the cytosolic degradation of GSH [34].…”

Section: Discussionmentioning

confidence: 99%

“…Instead, the DUG pathway relying on Dug1-3 proteins is likely to be responsible for the cytosolic degradation of GSH [34]. It is worth mentioning that some genes coding for important GSH metabolism-related enzymes have only been characterized through transcriptional (dug1-3 [36]; gpxA [37]) or translational (gst3 [38]) changes. Therefore, a deeper characterization of GSH metabolic enzymes and GSH transporters (Figure 1, Supplementary Table S-I) using molecular genetic tools are urgently needed in A. nidulans.…”

Section: Discussionmentioning

confidence: 99%

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Study on the glutathione metabolism of the filamentous fungus Aspergillus nidulans

Bakti

Király

Orosz

et al. 2017

Acta Microbiologica et Immunologica Hungarica

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Yeast protein sequence-based homology search for glutathione (GSH) metabolic enzymes and GSH transporters demonstrated that Aspergillus nidulans has a robust GSH uptake and metabolic system with several paralogous genes. In wet laboratory experiments, two key genes of GSH metabolism, gcsA, and glrA, encoding γ-L-glutamyl-L-cysteine synthetase and glutathione reductase, respectively, were deleted. The gene gcsA was essential, and the ΔgcsA mutant required GSH supplementation at considerably higher concentration than the Saccharomyces cerevisiae gsh1 mutant (8-10 mmol l −1 vs. 0.5 μmol l −1 ). In addition to some functions known previously, both genes were important in the germination of conidiospores, and both gene deletion strains required the addition of extra GSH to reach wild-type germination rates in liquid cultures. Nevertheless, the supplementation of cultures with 10 mmol l −1 GSH was toxic for the control and ΔglrA strains especially during vegetative growth, which should be considered in future development of high GSHproducer fungal strains. Importantly, the ΔglrA strain was characterized by increased sensitivity toward a wide spectrum of osmotic, cell wall integrity and antimycotic stress conditions in addition to previously reported temperature and oxidative stress sensitivities. These novel phenotypes underline the distinguished functions of GSH and GSH metabolic enzymes in the stress responses of fungi.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Study on the glutathione metabolism of the filamentous fungus Aspergillus nidulans

Bakti

Király

Orosz

et al. 2017

Acta Microbiologica et Immunologica Hungarica

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Glutathione Degradation

Bachhawat

Kaur

2017

Antioxidants & Redox Signaling

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Glutathione degradation plays a far greater role in cellular physiology than previously envisaged. The differential regulation and differential specificities of various enzymes, each acting on distinct pools, can lead to different consequences to the cell. It is likely that the coming years will see these downstream effects being unraveled in greater detail and will lead to a better understanding and appreciation of glutathione degradation. Antioxid. Redox Signal. 27, 1200-1216.

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The DUG Pathway Governs Degradation of Intracellular Glutathione in Aspergillus nidulans

Gila

Moon

Antal

et al. 2021

Appl Environ Microbiol

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Glutathione (GSH) is an abundant tripeptide that plays a crucial role in shielding cellular macromolecules from various reactive oxygen and nitrogen species in fungi. Understanding GSH metabolism is of vital importance to deciphering redox regulation in these microorganisms. In the present study, to better understand the GSH metabolism in filamentous fungi, we investigate functions of the dugB and dugC genes in the model fungus Aspergillus nidulans. These genes are orthologues of dug2-3 involved in cytosolic GSH degradation in the yeast. The deletion (Δ) of dugB, dugC, or both resulted in a moderate increase in the GSH content in the mycelia grown on glucose, reduced conidia production, and disturbed sexual development. In agreement with these observations, transcriptome data showed that genes encoding MAP kinase pathway elements (e.g. steC, sskB, hogA, mkkA) or regulatory proteins of conidiogenesis and sexual differentiation (e.g. flbA,C,E, nosA, rosA, nsdC,D) were down-regulated in the ΔdugBΔdugC mutant. Deletion of dugB and/or dugC slowed down the depletion of GSH pools under carbon starvation. It also reduced accumulation of reactive oxygen species, decreased autolytic cell wall degradation and enzyme secretion but increased sterigmatocystin formation. Transcriptome data demonstrated that enzyme secretions - in contrast to mycotoxin production - were controlled at post-transcriptional level. We suggest that GSH connects starvation and redox regulation to each other: Cells utilize GSH as stored carbon source during starvation. The reduction of GSH content alters the redox state activating regulatory pathways responsible for carbon starvation stress responses. Importance Glutathione (GSH) is a widely distributed tripeptide in both eukaryotes and prokaryotes. Owing to its very low redox potential, antioxidative character and high intracellular concentration, GSH profoundly shapes the redox status of cells. Our observations suggest that GSH metabolism and/or the redox status of cells plays a determinative role in several important aspects of fungal life, including oxidative stress defense, protein secretion, secondary metabolite production (including mycotoxin formation) as well as sexual and asexual differentiations. We demonstrated that even a slightly elevated GSH level can substantially disturb the homeostasis of fungi. This information could be important for development of new GSH producing strains or for any biotechnologically relevant processes where the GSH content, antioxidant capacity or oxidative stress tolerance of a fungal strain is manipulated.

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Degradation of glutathione inAspergillus nidulans— Short communication

Cited by 3 publications

References 10 publications

Study on the glutathione metabolism of the filamentous fungus Aspergillus nidulans

Study on the glutathione metabolism of the filamentous fungus Aspergillus nidulans

Glutathione Degradation

The DUG Pathway Governs Degradation of Intracellular Glutathione in Aspergillus nidulans

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