REFERENCES
- Baudin, A., O. Ozier-Kalogeropoulos, A. Danouel, F. Lacroute, and C. Cullin. 1993. A simple and efficient method for direct gene deletion in Saccharomyces cerevisiae. Nucleic Acids Res. 21:3329–3330.
- Becker, K., S. Gromer, R. H. Schirmer, and S. Müller. 2000. Thioredoxin reductase as a pathophysiological factor and drug target. Eur. J. Biochem. 267:6118–6125.
- Belyaeva, E. A., D. Dymkowska, M. R. Wieckowski, and L. Wojtczak. 2008. Mitochondria as an important target in heavy metal toxicity in rat hepatoma AS-30D cells. Toxicol. Appl. Pharmacol. 231:34–42.
- Boveris, A., and E. Cadenas. 1982. Production of superoxide radicals and hydrogen peroxide in mitochondria, p. 15-30. In L. W. Oberley (ed.), Superoxide dismutases, vol. 2. CRC Press, Boca Raton, FL.
- Chance, B., H. Sies, and A. Boveris. 1979. Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59:527–605.
- Chen, Y., J. Cai, T. J. Murphy, and D. P. Jones. 2002. Overexpressed human mitochondrial thioredoxin confers resistance to oxidant-induced apoptosis in human osteosarcoma cells. J. Biol. Chem. 277:33242–33248.
- Chen, Z., and L. H. Lash. 1998. Evidence for mitochondrial uptake of glutathione by dicarboxylate and 2-oxoglutarate carriers. J. Pharmacol. Exp. Ther. 285:608–618.
- Christianson, T. W., R. S. Sikorski, M. Dante, J. H. Shero, and P. Hieter. 1992. Multifunctional yeast high-copy-number shuttle vectors. Gene 110:119–122.
- Demple, B. 1998. A bridge to control. Science 279:1655–1656.
- Diekert, K., A. I. de Kroon, G. Kispal, and R. Lill. 2001. Isolation and subfractionation of mitochondria from the yeast Saccharomyces cerevisiae. Methods Cell Biol. 65:37–51.
- Fratelli, M., H. Demol, M. Puype, S. Casagrande, I. Eberini, M. Salmona, V. Bonetto, M. Mengozzi, F. Duffieux, E. Miclet, A. Bachi, J. Vandekerckhove, E. Gianazza, and P. Ghezzi. 2002. Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes. Proc. Natl. Acad. Sci. USA 99:3505–3510.
- Fratelli, M., H. Demol, M. Puype, S. Casagrande, P. Villa, I. Eberini, J. Vandekerckhove, E. Gianazza, and P. Ghezzi. 2003. Identification of proteins undergoing glutathionylation in oxidatively stressed hepatocytes and hepatoma cells. Proteomics 3:1154–1161.
- Glick, B. S., and L. A. Pon. 1995. Isolation of highly purified mitochondria from Saccharomyces cerevisiae. Methods Enzymol. 260:213–223.
- Grant, C. M., L. P. Collinson, J.-H. Roe, and I. W. Dawes. 1996. Yeast glutathione reductase is required for protection against oxidative stress and is a target gene for yAP-1 transcriptional regulation. Mol. Microbiol. 21:171–179.
- Grant, C. M., F. H. MacIver, and I. W. Dawes. 1996. Glutathione is an essential metabolite required for resistance to oxidative stress in the yeast Saccharomyces cerevisiae. Curr. Genet. 29:511–515.
- Grant, C. M., G. Perrone, and I. W. Dawes. 1998. Glutathione and catalase provide overlapping defenses for protection against hydrogen peroxide in the yeast Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 253:893–898.
- Griffith, O. W., and A. Meister. 1985. Origin and turnover of mitochondrial glutathione. Proc. Natl. Acad. Sci. USA 82:4668–4672.
- Gutteridge, J. M. C. 1993. Free radicals in disease processes: a compilation of cause and consequence. Free Radic. Res. Commun. 19:141–158.
- Halliwell, B., and J. M. C. Gutteridge. 1989. Free radicals in biology and medicine, 2nd ed. Oxford University Press, Oxford, United Kingdom.
- Holmgren, A. 1989. Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264:13963–13966.
- Hurd, T. R., N. J. Costa, C. C. Dahm, S. M. Beer, S. E. Brown, A. Filipovska, and M. P. Murphy. 2005. Glutathionylation of mitochondrial proteins. Antioxid. Redox Signal. 7:999–1010.
- Johansson, C., C. H. Lillig, and A. Holmgren. 2004. Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. J. Biol. Chem. 279:7537–7543.
- Kim, H. Y., and J. R. Kim. 2008. Thioredoxin as a reducing agent for mammalian methionine sulfoxide reductases B lacking resolving cysteine. Biochem. Biophys. Res. Commun. 371:490–494.
- Lee, J.-C., M. J. Straffon, T.-Y. Jang, C. M. Grant, and I. W. Dawes. 2001. The essential and ancillary role of glutathione in Saccharomyces cerevisiae: studies with a grande gsh1 disruptant strain. FEMS Yeast Res. 1:57–65.
- Llopis, J., J. M. McCaffery, A. Miyawaki, M. G. Farquhar, and R. Y. Tsien. 1998. Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins. Proc. Natl. Acad. Sci. USA 95:6803–6808.
- López-Mirabal, H. R., and J. R. Winther. 2008. Redox characteristics of the eukaryotic cytosol. Biochim. Biophys. Acta 1783:629–640.
- Manevich, Y., S. I. Feinstein, and A. B. Fisher. 2004. Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST. Proc. Natl. Acad. Sci. USA 101:3780–3785.
- Manevich, Y., and A. B. Fisher. 2005. Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism. Free Radic. Biol. Med. 38:1422–1432.
- Meister, A. 1995. Mitochondrial changes associated with glutathione deficiency. Biochim. Biophys. Acta 1271:35–42.
- Michelet, L., M. Zaffagnini, H. Vanacker, P. Le Marechal, C. Marchand, M. Schroda, S. D. Lemaire, and P. Decottignies. 2008. In vivo targets of S-thiolation in Chlamydomonas reinhardtii. J. Biol. Chem. 283:21571–21578.
- Monteiro, G., B. B. Horta, D. C. Pimenta, O. Augusto, and L. E. Netto. 2007. Reduction of 1-Cys peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing another function of vitamin C. Proc. Natl. Acad. Sci. USA 104:4886–4891.
- Noguera-Mazon, V., J. Lemoine, O. Walker, N. Rouhier, A. Salvador, J.-P. Jacquot, J.-M. Lancelin, and I. Krimm. 2006. Glutathionylation induces the dissociation of 1-Cys d-peroxiredoxin non-co-valent homodimer. J. Biol. Chem. 281:31736–31742.
- Nonn, L., R. R. Williams, R. P. Erickson, and G. Powis. 2003. The absence of mitochondrial thioredoxin 2 causes massive apoptosis, exencephaly, and early embryonic lethality in homozygous mice. Mol. Cell. Biol. 23:916–922.
- Olafsdottir, K., and D. J. Reed. 1988. Retention of oxidized glutathione by isolated rat liver mitochondria during hydroperoxide treatment. Biochim. Biophys. Acta 964:377–382.
- Outten, C. E., and V. C. Culotta. 2004. Alternative start sites in the S. cerevisiae GLR1 gene are responsible for mitochondrial and cytosolic isoforms of glutathione reductase. J. Biol. Chem. 279:7785–7791.
- Park, S. G., M.-K. Cha, W. Jeong, and I.-H. Kim. 2000. Distinct physiological functions of thiol peroxidase isoenzymes in Saccharomyces cerevisiae. J. Biol. Chem. 275:5723–5732.
- Pauwels, F., B. Vergauwen, F. Vanrobaeys, B. Devreese, and J. J. Van Beeumen. 2003. Purification and characterization of a chimeric enzyme from Haemophilus influenzae Rd that exhibits glutathione-dependent peroxidase activity. J. Biol. Chem. 278:16658–16666.
- Pedrajas, J. R., E. Kosmidou, A. Miranda-Vizuete, J.-A. Gustafsson, A. P. H. Wright, and G. Spyrou. 1999. Identification and functional characterization of a novel mitochondrial thioredoxin system in Saccharomyces cerevisiae. J. Biol. Chem. 274:6366–6373.
- Pedrajas, J. R., A. Miranda-Vizuete, N. Javanmardy, J.-A. Gustafsson, and G. Spyrou. 2000. Mitochondria of Saccharomyces cerevisiae contain one-conserved cysteine type peroxiredoxin with thioredoxin peroxidase activity. J. Biol. Chem. 275:16296–16301.
- Ralat, L. A., S. A. Misquitta, Y. Manevich, A. B. Fisher, and R. F. Colman. 2008. Characterization of the complex of glutathione S-transferase pi and 1-cysteine peroxiredoxin. Arch. Biochem. Biophys. 474:109–118.
- Rhee, S. G., H. Z. Chae, and K. Kim. 2005. Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radic. Biol. Med. 38:1543–1552.
- Rietsch, A., and J. Beckwith. 1998. The genetics of disulfide bond metabolism. Annu. Rev. Gen. 32:163–184.
- Spickett, C. M., N. Smirnoff, and A. R. Pitt. 2000. The biosynthesis of erythroascorbate in Saccharomyces cerevisiae and its role as an antioxidant. Free Radic. Biol. Med. 28:183–192.
- Stewart, E. J., F. Aslund, and J. Beckwith. 1998. Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins. EMBO J. 17:5543–5550.
- Sullivan, D. M., N. B. Wehr, M. M. Fergusson, R. L. Levine, and T. Finkel. 2000. Identification of oxidant-sensitive proteins: TNF-alpha; induces protein glutathiolation. Biochemistry 39:11121–11128.
- Toledano, M. B., C. Kumar, N. Le Moan, D. Spector, and F. Tacnet. 2007. The system biology of thiol redox system in Escherichia coli and yeast: differential functions in oxidative stress, iron metabolism and DNA synthesis. FEBS Lett. 581:3598–3607.
- Trotter, E. W., and C. M. Grant. 2003. Non-reciprocal regulation of the redox state of the glutathione/glutaredoxin and thioredoxin systems. EMBO Rep. 4:184–189.
- Trotter, E. W., and C. M. Grant. 2005. Overlapping roles of the cytoplasmic and mitochondrial redox regulatory systems in the yeast Saccharomyces cerevisiae. Eukaryot. Cell 4:392–400.
- Trotter, E. W., and C. M. Grant. 2002. Thioredoxins are required for protection against a reductive stress in the yeast Saccharomyces cerevisiae. Mol. Microbiol. 46:869–878.
- Valko, M., H. Morris, and M. T. Cronin. 2005. Metals, toxicity and oxidative stress. Curr. Med. Chem. 12:1161–1208.
- Valko, M., C. J. Rhodes, J. Moncol, M. Izakovic, and M. Mazur. 2006. Free radicals, metals and antioxidants in oxidative stress-induced cancer. Chem. Biol. Interact. 160:1–40.
- Wood, Z. A., E. Schroder, J. R. Harris, and L. B. Poole. 2003. Structure, mechanism and regulation of peroxiredoxins. Trends Biochem. Sci. 28:32–40.