Glutaredoxin

Holmgren, Arne; Arn��r, E.S.J.; Berndt, Kurt D.

doi:10.1002/0471203076.emm0336

Cited by 20 publications

(24 citation statements)

References 41 publications

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“…The assay was performed as described21 by monitoring the absorbance at 340 nm, at 25°C. The mixed disulfide formed by hydroxyethyl‐disulfide (HED) and GSH was reduced by SmTGR to produce GSSG which in turn is reduced by GR with the consumption of NADPH.…”

Section: Methodsmentioning

confidence: 99%

Glutathione reductase and thioredoxin reductase at the crossroad: The structure of Schistosoma mansoni thioredoxin glutathione reductase

et al. 2008

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Thioredoxin glutathione reductase (TGR) is a key flavoenzyme expressed by schistosomes that bridges two detoxification pathways crucial for the parasite survival in the host's organism. In this article we report the crystal structure (at 2.2 A resolution) of TGR from Schistosoma mansoni (SmTGR), deleted in the last two residues. The structure reveals the peculiar architecture of this chimeric enzyme: the small Glutaredoxin (Grx) domain at the N-terminus is joined to the large thioredoxin reductase (TR) one via an extended complementary surface, involving residues not conserved in the Grx superfamily; the TR domain interacts with an identical partner via its C-terminal domain, forming a dimer with a twisted "W" shape. Although lacking the penultimate Selenocysteine residue (Sec), the enzyme is still able to reduce oxidized glutathione. These data update the interpretation of the interdomain communication in TGR enzymes. The possible function of this enzyme in pathogenic parasites is discussed.

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Section: Methodsmentioning

confidence: 99%

Glutathione reductase and thioredoxin reductase at the crossroad: The structure of Schistosoma mansoni thioredoxin glutathione reductase

et al. 2008

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“…Studies have implicated these enzymes in many cellular processes including protein folding and regulation, reduction of dehydroascorbate, repair of oxidatively damaged proteins and sulphur metabolism (Holmgren 1989,Rietsch and Beckwith 1998). Glutaredoxins and thioredoxins are structurally similar and have been conserved throughout evolution (Holmgren and Aslund 1995). However, despite considerable functional overlap, they are differentially regulated.…”

Section: Redox Regulation In Yeastmentioning

confidence: 99%

Regulation of redox homeostasis in the yeast Saccharomyces cerevisiae

Wheeler

Grant

2004

Physiologia Plantarum

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An increasingly important area of research is based on sulphydryl chemistry, since the oxidation of -SH groups is one of the earliest observable events during oxidant-mediated damage and -SH groups play a critical role in the function of many macromolecular structures including enzymes, transcription factors and membrane proteins. Glutaredoxins and thioredoxins are small heat-stable oxidoreductases, conserved throughout evolution, which play key roles in maintaining the cellular redox balance. Much progress has been made in analysing these systems in the yeast Saccharomyces cerevisiae which is a very useful model eukaryote due to its ease of genetic manipulation, its compact genome, the availability of the entire genome sequence, and the current rate of progress in gene function research. Yeast, like all eukaryotes, contains a number of glutaredoxin and thioredoxin isoenzymes located in both the cytoplasm and the mitochondria. This review describes recent findings made in yeast that are leading to a better understanding of the regulation and role of redox homeostasis in eukaryotic cell metabolism.

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“…Roles have been proposed for them in many cellular processes including protein folding and regulation, reduction of dehydroascorbate, repair of oxidatively damaged proteins, and sulphur metabolism (Holmgren, 1989; Rietsch & Beckwith, 1998). Glutaredoxins and thioredoxins are structurally similar and have been conserved throughout evolution, particularly in the region of their active site (Holmgren & Aslund, 1995). They are thought to be differentially regulated, although both systems obtain reducing power from NADPH.…”

Section: Introductionmentioning

confidence: 99%

Non‐reciprocal regulation of the redox state of the glutathione–glutaredoxin and thioredoxin systems

2003

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Our studies in yeast show that there is an essential requirement for either an active thioredoxin or an active glutathione (GSH)-glutaredoxin system for cell viability. Glutathione reductase (Glr1) and thioredoxin reductase (Trr1) are key regulatory enzymes that determine the redox state of the GSH-glutaredoxin and thioredoxin systems, respectively. Here we show that Trr1 is required during normal cell growth, whereas there is no apparent requirement for Glr1. Analysis of the redox state of thioredoxins and glutaredoxins in glr1 and trr1 mutants reveals that thioredoxins are maintained independently of the glutathione system. In contrast, there is a strong correlation between the redox state of glutaredoxins and the oxidation state of the GSSG/2GSH redox couple. We suggest that independent redox regulation of thioredoxins enables cells to survive in conditions under which the GSH-glutaredoxin system is oxidized.

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Glutaredoxin

Cited by 20 publications

References 41 publications

Glutathione reductase and thioredoxin reductase at the crossroad: The structure of Schistosoma mansoni thioredoxin glutathione reductase

Glutathione reductase and thioredoxin reductase at the crossroad: The structure of Schistosoma mansoni thioredoxin glutathione reductase

Regulation of redox homeostasis in the yeast Saccharomyces cerevisiae

Non‐reciprocal regulation of the redox state of the glutathione–glutaredoxin and thioredoxin systems

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