Thioredoxin Peroxidase Is Required for the Transcriptional Response to Oxidative Stress in Budding Yeast

Ross, Sarah J.; Findlay, Victoria J.; Malakasi, Panagiota; Morgan, Brian A.

doi:10.1091/mbc.11.8.2631

Cited by 106 publications

(72 citation statements)

References 35 publications

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“…For this reason, because of the presence of a response regulator domain and because of its involvement in a number of important but seemingly unrelated cellular processes, the protein has attracted considerable interest. Skn7p has been implicated in cell cycle control (59,392), the oxidative stress response (90,91,267,296,297,324,325,337,390,516), the heat shock response (487), cell wall metabolism (70,282,338), and nitrogen starvation-induced diploid filamentous growth (349). Genetic and physical interactions link Skn7p not only to the HOG pathway (164, 281, 337, 591) but also to cell cycle-dependent transcription (59,391,392), the cell integrity pathway (5, 69), the heat shock transcription factor (487), the Yap1p oxidative stress transcription factor (91,324,390,516), and calcineurin-dependent signaling (648).…”

Section: Skn7p: Integrating Input From Differentmentioning

confidence: 99%

Osmotic Stress Signaling and Osmoadaptation in Yeasts

Hohmann

2002

Microbiol Mol Biol Rev

1,512

1,440

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The ability to adapt to altered availability of free water is a fundamental property of living cells. The principles underlying osmoadaptation are well conserved. The yeast Saccharomyces cerevisiae is an excellent model system with which to study the molecular biology and physiology of osmoadaptation. Upon a shift to high osmolarity, yeast cells rapidly stimulate a mitogen-activated protein (MAP) kinase cascade, the high-osmolarity glycerol (HOG) pathway, which orchestrates part of the transcriptional response. The dynamic operation of the HOG pathway has been well studied, and similar osmosensing pathways exist in other eukaryotes. Protein kinase A, which seems to mediate a response to diverse stress conditions, is also involved in the transcriptional response program. Expression changes after a shift to high osmolarity aim at adjusting metabolism and the production of cellular protectants. Accumulation of the osmolyte glycerol, which is also controlled by altering transmembrane glycerol transport, is of central importance. Upon a shift from high to low osmolarity, yeast cells stimulate a different MAP kinase cascade, the cell integrity pathway. The transcriptional program upon hypo-osmotic shock seems to aim at adjusting cell surface properties. Rapid export of glycerol is an important event in adaptation to low osmolarity. Osmoadaptation, adjustment of cell surface properties, and the control of cell morphogenesis, growth, and proliferation are highly coordinated processes. The Skn7p response regulator may be involved in coordinating these events. An integrated understanding of osmoadaptation requires not only knowledge of the function of many uncharacterized genes but also further insight into the time line of events, their interdependence, their dynamics, and their spatial organization as well as the importance of subtle effects

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Section: Skn7p: Integrating Input From Differentmentioning

confidence: 99%

Osmotic Stress Signaling and Osmoadaptation in Yeasts

Hohmann

2002

Microbiol Mol Biol Rev

1,512

1,440

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“…Unlike deletion of the thioredoxin/thioredoxin reductase encoding genes, studies have shown that deletion of the TSA1 gene has no obvious a ect on the nuclear localization of Yap1 Delaunay et al, 2000;Ross et al, 2000) or on the basal level expression of Yap1 target genes, TRX2 and TRR1 (Delaunay et al, 2000;Ross et al, 2000); although there is one con¯icting report that suggests an increase in basal level expression of Yap1-dependent genes in a tsa1 strain . In contrast, in response to very low levels of H 2 O 2 (0.1 mM), induction of TRX2 and TRR1 is much reduced in a tsa1 strain while overexpression of TSA1 results in faster than normal induction of TRX2 and TRR1 (Ross et al, 2000). Furthermore, in S. pombe, Tsa1 appears to be required for the induction of Pap1-regulated gene expression in response to H 2 O 2 (Findlay et al, 2001, unpublished observation).…”

Section: Thioredoxin Dependent Deactivation Of Yap-1mentioning

confidence: 99%

Redox control of AP-1-like factors in yeast and beyond

2001

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Cells have evolved complex and e cient strategies for dealing with variable and often-harsh environments. A key aspect of these stress responses is the transcriptional activation of genes encoding defense and repair proteins. In yeast members of the AP-1 family of proteins are required for the transcriptional response to oxidative stress. This sub-family of AP-1 (called yAP-1) proteins are sensors of the redox-state of the cell and are activated directly by oxidative stress conditions. yAP-1 proteins are bZIP-containing factors that share homology to the mammalian AP-1 factor complex and bind to very similar DNA sequence sites. The generation of reactive oxygen species and the resulting potential for oxidative stress is common to all aerobically growing organisms. Furthermore, many of the features of this response appear to be evolutionarily conserved and consequently the study of model organisms, such as yeast, will have widespread utility. The important structural features of these factors, signaling pathways controlling their activity and the nature of the target genes they control will be discussed. Oncogene (2001) 20, 2336 ± 2346.

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“…TPx is not only involved in direct detoxification of reactive peroxides. In yeast it was found that at least one TPx-1 orthologue is essential for launching off the cellular response to oxidative stress (30), a process that is based on up-and downregulation of numerous gene activities. DmTPx-1 belongs to a group of proteins in Drosophila that are differentially expressed in the developmental stages of Drosophila (21).…”

Section: Fig 1 Western Blot Of Recombinant and Wild-type Dmtrx-2mentioning

confidence: 99%

Thioredoxin-2 but Not Thioredoxin-1 Is a Substrate of Thioredoxin Peroxidase-1 from Drosophila melanogaster

Bauer

Kanzok

Schirmer

2002

Journal of Biological Chemistry

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As Drosophila melanogaster does not contain glutathione reductase, the thioredoxin system has a key function for glutathione disulfide reduction in insects (Kanzok, S. M., Fechner, A., Bauer, H., Ulschmid, J. K., Mü ller, H. M., Botella-Munoz, J., Schneuwly, S., Schirmer, R. H., and Becker, K. (2001) Science 291, 643-646). In view of these unique conditions, the protein systems participating in peroxide metabolism and in redox signaling are of special interest. The genes for a second thioredoxin (DmTrx-2) and a thioredoxin peroxidase (DmTPx-1) were cloned and expressed, and the proteins were characterized. In its disulfide form, the 13-kDa protein thioredoxin-2 is a substrate of thioredoxin reductase-1 (K m ‫؍‬ 5.2 M, k cat ‫؍‬ 14.5 s ؊1 ) and in its dithiol form, an electron donor for TPx-1 (K m ‫؍‬ 9 M, k cat ‫؍‬ 5.4 s ؊1 ). DmTrx-2 is capable of reducing glutathione disulfide with a second order rate constant of 170 M ؊1 s ؊1 at pH 7.4 and 25°C. Western blot analysis indicated that this thioredoxin represents up to 1% of the extractable protein of D. melanogaster Schneider cells or whole fruit flies. Recombinant thioredoxin peroxidase-1 (subunit molecular mass ‫؍‬ 23 kDa) was found to be a decameric protein that can efficiently use Trx-2 but not Trx-1 as a reducing substrate. The new electron pathway found in D. melanogaster is also representative for insects that serve as vectors of disease. As a first step we have cloned and functionally expressed the gene that is the orthologue of DmTrx-2 in the malaria mosquito Anopheles gambiae.Aerobic life conditions that are based on metabolizing molecular oxygen are linked inseparably to the occurrence of reactive oxygen species. These compounds are cytotoxic for the organism but even more so for invaders such as microorganisms and tumor cells. The oxidative challenge is counteracted by a shield of enzymatic and non-enzymatic defense systems including superoxide dismutase (2 O 2

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Thioredoxin Peroxidase Is Required for the Transcriptional Response to Oxidative Stress in Budding Yeast

Cited by 106 publications

References 35 publications

Osmotic Stress Signaling and Osmoadaptation in Yeasts

Osmotic Stress Signaling and Osmoadaptation in Yeasts

Redox control of AP-1-like factors in yeast and beyond

Thioredoxin-2 but Not Thioredoxin-1 Is a Substrate of Thioredoxin Peroxidase-1 from Drosophila melanogaster

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