Glutaredoxin systems

Lillig, Christopher Horst; Berndt, Carsten; Holmgren, Arne

doi:10.1016/j.bbagen.2008.06.003

Cited by 557 publications

(574 citation statements)

References 192 publications

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“…6A. Different from other proteindisulfide reductases, Grx1 also operated with a so-called monothiol mechanism, besides the classic two-thiol mechanism (32). On the basis of our results in Fig.…”

Section: Discussionmentioning

confidence: 56%

Thioredoxin 1 Is Inactivated Due to Oxidation Induced by Peroxiredoxin under Oxidative Stress and Reactivated by the Glutaredoxin System

Du¹,

Zhang²,

Zhang

et al. 2013

Journal of Biological Chemistry

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Background:The Cys-62/Cys-69 dithiol of Trx1 is predicted to have a profound effect on cell signaling. Results: The Cys-62/Cys-69 dithiol of Trx1 was oxidized by Prx1, and this disulfide was reduced by the GSH/glutaredoxin system. Conclusion: Trx1 is involved in redox regulation via reversible oxidation of the Cys-62/Cys-69 dithiol of Trx1. Significance: We demonstrated the critical role of Trx1 oxidation in cell signaling.

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Section: Discussionmentioning

confidence: 56%

Thioredoxin 1 Is Inactivated Due to Oxidation Induced by Peroxiredoxin under Oxidative Stress and Reactivated by the Glutaredoxin System

Du¹,

Zhang²,

Zhang

et al. 2013

Journal of Biological Chemistry

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“…Glutaredoxin is found in all 28 cyanomyovirus genomes and is multi-copy in 10 genomes. Glutaredoxins help regulate cellular redox state (Lillig et al, 2008), suggesting that PhCOG173 is not only involved in influencing phosphate acquisition in host cells but may also alter cellular redox state. Phage may use an altered redox state to direct host metabolism toward nucleotide production (Thompson et al, 2011b).…”

Section: Pho Box Motifs In Cultured Cyanomyovirus Genomesmentioning

confidence: 99%

Genetic diversity in cultured and wild marine cyanomyoviruses reveals phosphorus stress as a strong selective agent

et al. 2013

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Viruses that infect marine cyanobacteria-cyanophages-often carry genes with orthologs in their cyanobacterial hosts, and the frequency of these genes can vary with habitat. To explore habitatinfluenced genomic diversity more deeply, we used the genomes of 28 cultured cyanomyoviruses as references to identify phage genes in three ocean habitats. Only about 6-11% of genes were consistently observed in the wild, revealing high gene-content variability in these populations. Numerous shared phage/host genes differed in relative frequency between environments, including genes related to phosphorous acquisition, photorespiration, photosynthesis and the pentose phosphate pathway, possibly reflecting environmental selection for these genes in cyanomyovirus genomes. The strongest emergent signal was related to phosphorous availability; a higher fraction of genomes from relatively low-phosphorus environments-the Sargasso and Mediterranean Sea-contained host-like phosphorus assimilation genes compared with those from the N. Pacific Gyre. These genes are known to be upregulated when the host is phosphorous starved, a response mediated by pho box motifs in phage genomes that bind a host regulatory protein. Eleven cyanomyoviruses have predicted pho boxes upstream of the phosphate-acquisition genes pstS and phoA; eight of these have a conserved cyanophage-specific gene (PhCOG173) between the pho box and pstS. PhCOG173 is also found upstream of other shared phage/host genes, suggesting a unique regulatory role. Pho boxes are found upstream of high light-inducible (hli) genes in cyanomyoviruses, suggesting that this motif may have a broader role than regulating phosphorous-stress responses in infected hosts or that these hlis are involved in the phosphorous-stress response.

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“…Grxs catalyze the reversible reduction of protein disulfides utilizing both cysteinyl residues in their active site, transferring two hydrogen atoms to protein disulfide ( Figure 1, reaction 6). As a result, the catalytic domain of Grxs forms a disulfide that would be recovered by spending two molecules of glutathione (Lillig et al, 2008). Protein deglutathionylation has received significant attention because of its regulatory roles in redox signaling transduction and sulfhydryl homeostasis (Dalle-Donne et al, 2008).…”

Section: Consumption Of Glutathionementioning

confidence: 99%

S-glutathionylation: relevance in diabetes and potential role as a biomarker

Sánchez‐Gómez

Espinosa‐Díez

Dubey

et al. 2013

Biological Chemistry

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Glutathione is considered the main regulator of redox balance in the cellular milieu due to its capacity for detoxifying deleterious molecules. The oxidative stress induced as a result of a variety of stimuli promotes protein oxidation, usually at cysteine residues, leading to changes in their activity. Mild oxidative stress, which may take place in physiological conditions, induces the reversible oxidation of cysteines to sulfenic acid form, while pathological conditions are associated with higher rates of reactive oxygen species production, inducing the irreversible oxidation of cysteines. Among these, neurodegenerative disorders, cardiovascular diseases and diabetes have been proposed to be pathogenetically linked to this state. In diabetes-associated vascular complications, lower levels of glutathione and increased oxidative stress have been reported. S-glutathionylation has been proposed as a posttranslational modification able to protect proteins from over-oxidizing environments. S-glutathionylation has been identified in proteins involved in diabetic models both in vitro and in vivo. In all of them, S-glutathionylation represents a mechanism that regulates the response to diabetic conditions, and has been described to occur in erythrocytes and neutrophils from diabetic patients. However, additional studies are necessary to discern whether this modification represents a biomarker for the early onset of diabetic vascular complications.

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Glutaredoxin systems

Cited by 557 publications

References 192 publications

Thioredoxin 1 Is Inactivated Due to Oxidation Induced by Peroxiredoxin under Oxidative Stress and Reactivated by the Glutaredoxin System

Thioredoxin 1 Is Inactivated Due to Oxidation Induced by Peroxiredoxin under Oxidative Stress and Reactivated by the Glutaredoxin System

Genetic diversity in cultured and wild marine cyanomyoviruses reveals phosphorus stress as a strong selective agent

S-glutathionylation: relevance in diabetes and potential role as a biomarker

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