Mitochondrial and cytosolic expression of human peroxiredoxin 5 in <i>Saccharomyces cerevisiae</i> protect yeast cells from oxidative stress induced by paraquat

Nguyên-nhu, Nhu Tiên; Knoops, Bernard

doi:10.1016/s0014-5793(03)00493-9

Cited by 34 publications

(16 citation statements)

References 33 publications

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“…Transformants were selected on solid minimal media that contained yeast nitrogen base (Difco) and 2His Dropout supplement (per 20 g/L of Gal; SG-His; Clontech). Transformants grown overnight in liquid SG-His media were subjected to stress on solid SG-His media supplied with either 2 mM methyl viologen (Acros Organics) or 0.25 mM t-butyl hydroperoxide (Sigma-Aldrich) as serial dilutions (Tiên Nguyên-nhu and Knoops, 2003) or subjected to the same oxidative stress treatment in liquid SG-His media (Davies et al, 1995).…”

Section: Characterization Of Proteins With Unknown Function In Yeast mentioning

confidence: 99%

Enhanced Tolerance to Oxidative Stress in Transgenic Arabidopsis Plants Expressing Proteins of Unknown Function

Song

Ciftci-Yilmaz²,

Harper³

et al. 2008

Plant Physiology

109

131

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Over one-quarter of all plant genes encode proteins of unknown function that can be further classified as proteins with obscure features (POFs), which lack currently defined motifs or domains, or proteins with defined features, which contain at least one previously defined domain or motif. Although empirical data in the form of transcriptome and proteome profiling suggest that many of these proteins play important roles in plants, their functional characterization remains one of the main challenges in modern biology. To begin the functional annotation of proteins with unknown function, which are involved in the oxidative stress response of Arabidopsis (Arabidopsis thaliana), we generated transgenic Arabidopsis plants that constitutively expressed 23 different POFs (four of which were specific to Arabidopsis) and 18 different proteins with defined features. All were previously found to be expressed in response to oxidative stress in Arabidopsis. Transgenic plants were tested for their tolerance to oxidative stress imposed by paraquat or t-butyl hydroperoxide, or were subjected to osmotic, salinity, cold, and heat stresses. More than 70% of all expressed proteins conferred tolerance to oxidative stress. In contrast, .90% of the expressed proteins did not confer enhanced tolerance to the other abiotic stresses tested, and approximately 50% rendered plants more susceptible to osmotic or salinity stress. Two Arabidopsis-specific POFs, and an Arabidopsis and Brassica-specific protein of unknown function, conferred enhanced tolerance to oxidative stress. Our findings suggest that tolerance to oxidative stress involves mechanisms and pathways that are unknown at present, including some that are specific to Arabidopsis or the Brassicaceae.

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Section: Characterization Of Proteins With Unknown Function In Yeast mentioning

confidence: 99%

Enhanced Tolerance to Oxidative Stress in Transgenic Arabidopsis Plants Expressing Proteins of Unknown Function

Song

Ciftci-Yilmaz²,

Harper³

et al. 2008

Plant Physiology

109

131

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“…6 Human peroxiredoxin V protects S. cerevisiae from the oxidative stress induced by paraquat. 7 Tpx plays a significant role in peroxide and superoxide resistance in Helicobacter pylori. 8 Overexpression of peroxiredoxin in Leishmania chagasi parasites enhances its survival within U937 macrophage cells.…”

Section: Introductionmentioning

confidence: 99%

Functional and Structural Characterization of a Thiol Peroxidase from Mycobacterium tuberculosis

Rho

Hung

Holton

et al. 2006

Journal of Molecular Biology

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“…in systems ranging from isolated mitochondria (12)(13)(14)(15) and cultured mammalian cells (4,14,16,17), to whole organisms including Saccharomyces cerevisiae (18 -21), Caenorhabditis elegans (22,23), Drosophila melanogaster (9, 24 -26), and rodents (6,11,27). In many of these studies, PQ increases mitochondrial oxidative damage; for example, mitochondrial expression of human peroxiredoxin 5 protects yeast more effectively against PQ toxicity than expression in the cytosol (19); flies overexpressing catalase in mitochondria are resistant to PQ, whereas enhancement of cytosolic catalase was not protective (24); RNA interference silencing of MnSOD (the isoform of superoxide dismutase located in the mitochondrial matrix) in flies causes hypersensitivity to PQ (9), mice heterozygous for MnSOD show greater sensitivity to PQ than wild-type (11), and mitochondrial swelling is one of the earliest ultrastructural changes upon PQ exposure in vivo (28,29). Therefore the interaction of PQ with mitochondria is an important component of its toxicity, and PQ is used in experimental models of Parkinson disease to generate mitochondrial oxidative damage (30).…”

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confidence: 99%

Complex I Is the Major Site of Mitochondrial Superoxide Production by Paraquat

Cochemé

Murphy

2008

Journal of Biological Chemistry

509

375

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Paraquat (1,1-dimethyl-4,4-bipyridinium dichloride) is widely used as a redox cycler to stimulate superoxide production in organisms, cells, and mitochondria. This superoxide production causes extensive mitochondrial oxidative damage, however, there is considerable uncertainty over the mitochondrial sites of paraquat reduction and superoxide formation. Here we show that in yeast and mammalian mitochondria, superoxide production by paraquat occurs in the mitochondrial matrix, as inferred from manganese superoxide dismutase-sensitive mitochondrial DNA damage, as well as from superoxide assays in isolated mitochondria, which were unaffected by exogenous superoxide dismutase. This paraquat-induced superoxide production in the mitochondrial matrix required a membrane potential that was essential for paraquat uptake into mitochondria. This uptake was of the paraquat dication, not the radical monocation, and was carrier-mediated. Experiments with disrupted mitochondria showed that once in the matrix paraquat was principally reduced by complex I (mammals) or by NADPH dehydrogenases (yeast) to form the paraquat radical cation that then reacted with oxygen to form superoxide. Together this membrane potential-dependent uptake across the mitochondrial inner membrane and the subsequent rapid reduction to the paraquat radical cation explain the toxicity of paraquat to mitochondria.Paraquat (1,1Ј-dimethyl-4,4Ј-bipyridinium dichloride; PQ) 2 is used to increase superoxide (O 2 . ) flux when investigating oxidative stress (reviewed in Refs. 1 and 2). The paraquat dication (PQ 2ϩ ) accepts an electron from a reductant to form the paraquat monocation radical (PQ . . and regenerate PQ 2ϩ (Fig. 1A). This redox cycling is a proximal cause of PQ toxicity, as indicated by the protection against PQ by superoxide dismutase (SOD) overexpression or administration of SOD mimetics (4 -8), and by the PQ hypersensitivity caused by SOD deficiency (9 -11).PQ has been used to generate O 2 . in systems ranging from isolated mitochondria (12-15) and cultured mammalian cells (4,14,16,17), to whole organisms including Saccharomyces cerevisiae (18 -21), Caenorhabditis elegans (22, 23), Drosophila melanogaster (9, 24 -26), and rodents (6,11,27). In many of these studies, PQ increases mitochondrial oxidative damage; for example, mitochondrial expression of human peroxiredoxin 5 protects yeast more effectively against PQ toxicity than expression in the cytosol (19); flies overexpressing catalase in mitochondria are resistant to PQ, whereas enhancement of cytosolic catalase was not protective (24); RNA interference silencing of MnSOD (the isoform of superoxide dismutase located in the mitochondrial matrix) in flies causes hypersensitivity to PQ (9), mice heterozygous for MnSOD show greater sensitivity to PQ than wild-type (11), and mitochondrial swelling is one of the earliest ultrastructural changes upon PQ exposure in vivo (28,29). Therefore the interaction of PQ with mitochondria is an important component of its toxicity, and PQ is used in expe...

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Mitochondrial and cytosolic expression of human peroxiredoxin 5 in Saccharomyces cerevisiae protect yeast cells from oxidative stress induced by paraquat

Cited by 34 publications

References 33 publications

Enhanced Tolerance to Oxidative Stress in Transgenic Arabidopsis Plants Expressing Proteins of Unknown Function

Enhanced Tolerance to Oxidative Stress in Transgenic Arabidopsis Plants Expressing Proteins of Unknown Function

Functional and Structural Characterization of a Thiol Peroxidase from Mycobacterium tuberculosis

Complex I Is the Major Site of Mitochondrial Superoxide Production by Paraquat

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