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Catalase modifies yeast Saccharomyces cerevisiae response towards S-nitrosoglutathione-induced stress.
Redox Rep. 2008; 13(6):283-91.RR

Abstract

Nitric oxide is known to be a messenger in animals and plants. Catalase may regulate the concentration of intracellular *NO. In this study, yeast Saccharomyces cerevisiae cells were treated with 1-20 mM S-nitrosoglutathione (GSNO), a nitric oxide donor, which decreased yeast survival in a concentration-dependent manner. In the wild-type strain (YPH250), 20 mM GSNO reduced survival by 32%. The strain defective in peroxisomal catalase behaved like the wild-type strain, while a mutant defective in cytosolic catalase showed 10% lower survival. Surprisingly, survival of the double catalase mutant was significantly higher than that of the other strains used. Incubation of yeast with GSNO increased the activities of both superoxide dismutase (SOD) and catalase. Pre-incubation with cycloheximide prevented the activation of catalase, but not SOD. The concentrations of oxidized glutathione increased in the wild-type strain, as well as in the mutants defective in peroxisomal catalase and an acatalasaemic strain; it failed to do this in the mutant defective in cytosolic catalase. The activity of aconitase was reduced after GSNO treatment in all strains studied, except for the mutant defective in peroxisomal catalase. The content of protein carbonyls and activities of glutathione reductase and S-nitrosoglutathione reductase were unchanged following GSNO treatment. The increase in catalase activity due to incubation with GSNO was not found in a strain defective in Yap1p, a master regulator of yeast adaptive response to oxidative stress. The obtained data demonstrate that exposure of yeast cells to the *NO-donor S-nitrosoglutathione induced mild oxidative/nitrosative stress and Yap1p may co-ordinate the up-regulation of antioxidant enzymes under these conditions.

Authors+Show Affiliations

Department of Biochemistry, Vassyl Stefanyk Precarpathian National University, Ivano-Frankivsk, Ukraine. lushchak@pu.if.uaNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19017469

Citation

Lushchak, Oleh V., and Volodymyr I. Lushchak. "Catalase Modifies Yeast Saccharomyces Cerevisiae Response Towards S-nitrosoglutathione-induced Stress." Redox Report : Communications in Free Radical Research, vol. 13, no. 6, 2008, pp. 283-91.
Lushchak OV, Lushchak VI. Catalase modifies yeast Saccharomyces cerevisiae response towards S-nitrosoglutathione-induced stress. Redox Rep. 2008;13(6):283-91.
Lushchak, O. V., & Lushchak, V. I. (2008). Catalase modifies yeast Saccharomyces cerevisiae response towards S-nitrosoglutathione-induced stress. Redox Report : Communications in Free Radical Research, 13(6), 283-91. https://doi.org/10.1179/135100008X309037
Lushchak OV, Lushchak VI. Catalase Modifies Yeast Saccharomyces Cerevisiae Response Towards S-nitrosoglutathione-induced Stress. Redox Rep. 2008;13(6):283-91. PubMed PMID: 19017469.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Catalase modifies yeast Saccharomyces cerevisiae response towards S-nitrosoglutathione-induced stress. AU - Lushchak,Oleh V, AU - Lushchak,Volodymyr I, PY - 2008/11/20/pubmed PY - 2009/3/20/medline PY - 2008/11/20/entrez SP - 283 EP - 91 JF - Redox report : communications in free radical research JO - Redox Rep VL - 13 IS - 6 N2 - Nitric oxide is known to be a messenger in animals and plants. Catalase may regulate the concentration of intracellular *NO. In this study, yeast Saccharomyces cerevisiae cells were treated with 1-20 mM S-nitrosoglutathione (GSNO), a nitric oxide donor, which decreased yeast survival in a concentration-dependent manner. In the wild-type strain (YPH250), 20 mM GSNO reduced survival by 32%. The strain defective in peroxisomal catalase behaved like the wild-type strain, while a mutant defective in cytosolic catalase showed 10% lower survival. Surprisingly, survival of the double catalase mutant was significantly higher than that of the other strains used. Incubation of yeast with GSNO increased the activities of both superoxide dismutase (SOD) and catalase. Pre-incubation with cycloheximide prevented the activation of catalase, but not SOD. The concentrations of oxidized glutathione increased in the wild-type strain, as well as in the mutants defective in peroxisomal catalase and an acatalasaemic strain; it failed to do this in the mutant defective in cytosolic catalase. The activity of aconitase was reduced after GSNO treatment in all strains studied, except for the mutant defective in peroxisomal catalase. The content of protein carbonyls and activities of glutathione reductase and S-nitrosoglutathione reductase were unchanged following GSNO treatment. The increase in catalase activity due to incubation with GSNO was not found in a strain defective in Yap1p, a master regulator of yeast adaptive response to oxidative stress. The obtained data demonstrate that exposure of yeast cells to the *NO-donor S-nitrosoglutathione induced mild oxidative/nitrosative stress and Yap1p may co-ordinate the up-regulation of antioxidant enzymes under these conditions. SN - 1743-2928 UR - https://www.unboundmedicine.com/medline/citation/19017469/Catalase_modifies_yeast_Saccharomyces_cerevisiae_response_towards_S_nitrosoglutathione_induced_stress_ L2 - https://www.tandfonline.com/doi/full/10.1179/135100008X309037 DB - PRIME DP - Unbound Medicine ER -