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Article: Peroxiredoxin-null yeast cells are hypersensitive to oxidative stress and are genomically unstable

TitlePeroxiredoxin-null yeast cells are hypersensitive to oxidative stress and are genomically unstable
Authors
Issue Date2004
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2004, v. 279 n. 22, p. 23207-23213 How to Cite?
AbstractPeroxiredoxins are a family of abundant peroxidases found in all organisms. Although these antioxidant enzymes are thought to be critically involved in cellular defense and redox signaling, their exact physiological roles are largely unknown. In this study, we took a genetic approach to address the functions of peroxiredoxins in budding yeast. We generated and characterized a yeast mutant lacking all five peroxiredoxins. The quintuple peroxiredoxin-null mutant was still viable, though the growth rate was lower under normal aerobic conditions. Although peroxiredoxins are not essential for cell viability, peroxiredoxin-null yeast cells were more susceptible to oxidative and nitrosative stress. In the complete absence of peroxiredoxins, the expression of other antioxidant proteins including glutathione peroxidase and glutathione reductase was induced. In addition, the quintuple mutant was hypersensitive to glutathione depletion. Thus, the glutathione system might cooperate with other antioxidant enzymes to compensate for peroxiredoxin deficiency. Interestingly, the peroxiredoxin-null yeast cells displayed an increased rate of spontaneous mutations that conferred resistance to canavanine. This mutator phenotype was rescued by yeast peroxiredoxin Tsa1p, but not by its active-site mutant defective for peroxidase activity. Our findings suggest that the antioxidant function of peroxiredoxins is important for maintaining genome stability in eukaryotic cells.
Persistent Identifierhttp://hdl.handle.net/10722/68209
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWong, CMen_HK
dc.contributor.authorSiu, KLen_HK
dc.contributor.authorJin, DYen_HK
dc.date.accessioned2010-09-06T06:02:24Z-
dc.date.available2010-09-06T06:02:24Z-
dc.date.issued2004en_HK
dc.identifier.citationJournal Of Biological Chemistry, 2004, v. 279 n. 22, p. 23207-23213en_HK
dc.identifier.issn0021-9258en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68209-
dc.description.abstractPeroxiredoxins are a family of abundant peroxidases found in all organisms. Although these antioxidant enzymes are thought to be critically involved in cellular defense and redox signaling, their exact physiological roles are largely unknown. In this study, we took a genetic approach to address the functions of peroxiredoxins in budding yeast. We generated and characterized a yeast mutant lacking all five peroxiredoxins. The quintuple peroxiredoxin-null mutant was still viable, though the growth rate was lower under normal aerobic conditions. Although peroxiredoxins are not essential for cell viability, peroxiredoxin-null yeast cells were more susceptible to oxidative and nitrosative stress. In the complete absence of peroxiredoxins, the expression of other antioxidant proteins including glutathione peroxidase and glutathione reductase was induced. In addition, the quintuple mutant was hypersensitive to glutathione depletion. Thus, the glutathione system might cooperate with other antioxidant enzymes to compensate for peroxiredoxin deficiency. Interestingly, the peroxiredoxin-null yeast cells displayed an increased rate of spontaneous mutations that conferred resistance to canavanine. This mutator phenotype was rescued by yeast peroxiredoxin Tsa1p, but not by its active-site mutant defective for peroxidase activity. Our findings suggest that the antioxidant function of peroxiredoxins is important for maintaining genome stability in eukaryotic cells.en_HK
dc.languageengen_HK
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_HK
dc.relation.ispartofJournal of Biological Chemistryen_HK
dc.rightsJournal of Biological Chemistry. Copyright © American Society for Biochemistry and Molecular Biology, Inc.en_HK
dc.subject.meshGene Deletionen_HK
dc.subject.meshGene Expression Regulation, Fungalen_HK
dc.subject.meshGenomic Instabilityen_HK
dc.subject.meshOxidative Stress - geneticsen_HK
dc.subject.meshPeroxidases - geneticsen_HK
dc.subject.meshPeroxiredoxinsen_HK
dc.subject.meshSaccharomyces cerevisiae - physiologyen_HK
dc.titlePeroxiredoxin-null yeast cells are hypersensitive to oxidative stress and are genomically unstableen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-9258&volume=279&spage=23207&epage=23213&date=2004&atitle=Peroxiredoxin-null+yeast+cells+are+hypersensitive+to+oxidative+stress+and+genomially+unstableen_HK
dc.identifier.emailWong, CM:wispwong@hkucc.hku.hken_HK
dc.identifier.emailJin, DY:dyjin@hkucc.hku.hken_HK
dc.identifier.authorityWong, CM=rp01489en_HK
dc.identifier.authorityJin, DY=rp00452en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1074/jbc.M402095200en_HK
dc.identifier.pmid15051715-
dc.identifier.scopuseid_2-s2.0-2542504409en_HK
dc.identifier.hkuros95062en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-2542504409&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume279en_HK
dc.identifier.issue22en_HK
dc.identifier.spage23207en_HK
dc.identifier.epage23213en_HK
dc.identifier.isiWOS:000221570900052-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridWong, CM=18134632400en_HK
dc.identifier.scopusauthoridSiu, KL=7102312040en_HK
dc.identifier.scopusauthoridJin, DY=7201973614en_HK

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