Regulation Of Mitochondrial Thioredoxin Peroxidase I Expression By Two Different Pathways: One Dependent On Camp And The Other On Heme.

dc.creatorMonteiro, Gisele
dc.creatorPereira, Gonçalo Amarante Guimarães
dc.creatorNetto, Luis Eduardo Soares
dc.date2002-Feb
dc.date2015-11-27T12:49:09Z
dc.date2015-11-27T12:49:09Z
dc.date.accessioned2018-03-29T00:56:18Z
dc.date.available2018-03-29T00:56:18Z
dc.identifierFree Radical Biology & Medicine. v. 32, n. 3, p. 278-88, 2002-Feb.
dc.identifier0891-5849
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/11827753
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/195089
dc.identifier11827753
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1295322
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 H(2)O(2) 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 H(2)O(2) 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).
dc.description32
dc.description278-88
dc.languageeng
dc.relationFree Radical Biology & Medicine
dc.relationFree Radic. Biol. Med.
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectCyclic Amp
dc.subjectDna-binding Proteins
dc.subjectGene Expression Regulation, Enzymologic
dc.subjectGene Expression Regulation, Fungal
dc.subjectGlucose
dc.subjectHeme
dc.subjectIsoenzymes
dc.subjectMitochondria
dc.subjectNeoplasm Proteins
dc.subjectOxidative Stress
dc.subjectPeroxidases
dc.subjectPeroxides
dc.subjectPeroxiredoxins
dc.subjectRna, Messenger
dc.subjectSaccharomyces Cerevisiae
dc.subjectSaccharomyces Cerevisiae Proteins
dc.subjectTranscription Factors
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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