Regulation of mitochondrial thioredoxin peroxidase I expression by two different pathways: One dependent on cAMP and the other on heme

dc.creatorMonteiro, G
dc.creatorPereira, GAG
dc.creatorNetto, LES
dc.date2002
dc.dateFEB 1
dc.date2014-11-15T12:11:50Z
dc.date2015-11-26T17:19:55Z
dc.date2014-11-15T12:11:50Z
dc.date2015-11-26T17:19:55Z
dc.date.accessioned2018-03-29T00:07:33Z
dc.date.available2018-03-29T00:07:33Z
dc.identifierFree Radical Biology And Medicine. Pergamon-elsevier Science Ltd, v. 32, n. 3, n. 278, n. 288, 2002.
dc.identifier0891-5849
dc.identifierWOS:000173845700009
dc.identifier10.1016/S0891-5849(01)00801-2
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/80064
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/80064
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/80064
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1283012
dc.descriptionMitochondrial isoform of thioredoxin peroxidase (mTPx I) is an antioxidant protein recently described in Saccharomyces cerevisiae. Here we characterized pathways that lead to mTPx I induction in two situations: growth in media containing low glucose concentrations and treatment with peroxides. The induction of mTPx I by growth on low glucose concentrations was dependent on cAMP and on the transcription factors Msn2p/Msn4p as demonstrated by northern blot experiments using yeast strains with deletion of MSN2 and MSN4 genes and also using a strain permeable to cAMP. mTPx I expression was also induced by peroxides in a time- and dose-dependent manner and varied with the carbon source present in the media. Deletion of HAP1 or inhibition of heme synthesis abolished induction of mTPx I by H2O2 on cells which were grown in media containing glucose, indicating that Hap1p is involved in the regulation of this process. mTPx I was induced by H2O2 on glycerol/ethanol-containing media, but we could not associate any transcription factor with this phenomenon. Finally, mTPx I also induced by t-butyl hydroperoxide in a Hap1p-independent manner. In conclusion, mTPx I expression is under a complex regulatory network, which involves, at least, two signaling pathways: one sensing the carbon source (which is signalized by cAMP) and the other sensing the intracellular redox state (which is signalized by heme). (C) 2002 Elsevier Science Inc.
dc.description32
dc.description3
dc.description278
dc.description288
dc.languageen
dc.publisherPergamon-elsevier Science Ltd
dc.publisherOxford
dc.publisherInglaterra
dc.relationFree Radical Biology And Medicine
dc.relationFree Radic. Biol. Med.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectmitochondrial thioredoxin peroxidase
dc.subjectexpression regulation
dc.subjecttranscription activation
dc.subjectMsn2p and Msn4p activators
dc.subjectcAMP and glucose repression
dc.subjectHAP1p activator
dc.subjectheme
dc.subjectfree radicals
dc.subjectThiol-specific Antioxidant
dc.subjectYeast Saccharomyces-cerevisiae
dc.subjectOxidative Stress
dc.subjectGene-expression
dc.subjectTranscriptional Response
dc.subjectDiauxic Shift
dc.subjectBudding Yeast
dc.subjectProtein
dc.subjectOxygen
dc.subjectMsn2p
dc.titleRegulation of mitochondrial thioredoxin peroxidase I expression by two different pathways: One dependent on cAMP and the other on heme
dc.typeArtículos de revistas


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