A glutathione reductase mutant of yeast accumulates high levels of oxidized glutathione and requires thioredoxin for growth

Molecular Biology of the Cell

Volumn 7, Issue 11, 1996, Pages 1805-1813

  Muller, Eric G D ^a  

^a UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIAMIDE; GLUTATHIONE; GLUTATHIONE DISULFIDE; GLUTATHIONE REDUCTASE; THIOREDOXIN;

ARTICLE; FUNGUS GROWTH; FUNGUS MUTANT; LETHAL MUTANT; NONHUMAN; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE;

ESCHERICHIA COLI; FUNGI; SACCHAROMYCES CEREVISIAE;

EID: 0029948308     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.7.11.1805     Document Type: Article

References (54)

1. Adams, J.D., Jr., Wang, B., Klaidman, L.K., LeBel, C.P., Odunze, I.N., and Shah, D. (1993). New aspects of brain oxidative stress induced by tert-butylhydroperoxide. Free Radical Biol. Med. 15, 195-202.
2. Apontoweil, P., and Berends, W. (1975). Isolation and initial characterization of glutathione-deficient mutants of Escherichia coli K12. Biochim. Biophys. Acta 399, 10-22.
3. Aslund, F., Ehn, B., Miranda Vizuete, A., Pueyo, C., and Holmgren, A. (1994). Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is a hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin 1 double mutant. Proc. Natl. Acad. Sci. USA 91, 9813-9817.
4. + lymphocytes associated with disturbed intracellular redox balance in human immunodeficiency virus type 1 infection. Blood 86, 258-267.
5. Buchanan, B.B., Schurmann, P., and Jacquot, J.P. (1994). Thioredoxin and metabolic regulation. Semin. Cell Biol. 5, 285-293.
6. Chae, H.Z., Chung, S.J., and Rhee, S.G. (1994). Thioredoxin-dependent peroxide reductase from yeast. J. Biol. Chem. 269, 27670-27678.
7. Collinson, L.P., and Dawes, I.W. (1995). Isolation, characterization and overexpression of the yeast gene, GLR1, encoding glutathione reductase. Gene 156, 123-127.
8. Davis, T.N. (1992). Mutational analysis of calmodulin in Saccharomyces cerevisiae. Cell Calcium 13, 435-444.
9. Deneke, S.M., and Fanburg, B.L. (1989). Regulation of cellular glutathione. Am. J. Physiol. 257, L163-L173.
10. Derman, A.I., Prinz, W.A., Belin, D., and Beckwith, J. (1993). Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science 262, 1744-1747.
11. Fahey, R.C., and Newton, G.L. (1987). Determination of low-molecular-weight thiols using monobromobimane fluorescent labeling and high-performance liquid chromatography. Methods Enzymol. 143, 85-96.
12. Fuchs, J.A., and Warner, H.R. (1975). Isolation of an Escherichia coli mutant deficient in glutathione synthesis. J. Bacteriol. 124, 140-148.
13. Galiazzo, F., Schiesser, A., and Rotilio, G. (1987). Glutathione peroxidase in yeast. Presence of the enzyme and induction by oxidative conditions. Biochem. Biophys. Res. Commun. 147, 1200-1205.
14. Gan, Z.R. (1992). Cloning and sequencing of a gene encoding yeast thioltransferase. Biochem. Biophys. Res. Commun. 187, 949-955.
15. Geiser, J.R., Sundberg, H.A., Chang, B.H., Muller, E.G., and Davis, T.N. (1993). The essential mitotic target of calmodulin is the 110-kilodalton component of the spindle pole body in Saccharomyces cerevisiae. Mol. Cell. Biol. 13, 7913-7924.
16. Gilbert, H.F. (1995). Thiol/disulfide exchange equilibria and disulfide bond stability. Methods Enzymol. 251, 8-28.
17. Gounalaki, N., and Thireos, G. (1994). Yap1p, a yeast transcriptional activator that mediates multidrug resistance, regulates the metabolic stress response. EMBO J. 13, 4036-4041.
18. Halliwell, B. (1994). Free radicals and antioxidants: a personal view. Nutr. Rev. 52, 253-265.
19. Holmgren, A. (1979). Reduction of disulfides by thioredoxin. Exceptional reactivity of insulin and suggested functions of thioredoxin in mechanism of hormone action. J. Biol. Chem. 254, 9113-9119.
20. Holmgren, A. (1985). Thioredoxin. Annu. Rev. Biochem. 54, 237-271.
21. Holmgren, A. (1989). Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264, 13963-13966.
22. Hussain, M., and Lenard, J. (1991). Characterization of PDR4, a Saccharomyces cerevisiae gene that confers pleiotropic drug resistance in high-copy number: identity with YAP1, encoding a transcriptional activator [corrected] [published erratum appears in Gene 107, 175]. Gene 101, 149-152.
23. Hwang, C., Sinskey, A.J., and Lodish, H.F. (1992). Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257, 1496-1502.
24. Kosower, N.S., and Kosower, E.M. (1995). Diamide: an oxidant probe for thiols. Methods Enzymol. 251, 123-133.
25. Kretzschmar, M., Pfeifer, U., Machnik, G., and Klinger, W. (1992). Glutathione homeostasis and turnover in the totally hepatectomized rat: evidence for a high glutathione export capacity of extrahepatic tissues. Exp. Toxicol. Pathol. 44, 273-281.
26. Kuge, S., and Jones, N. (1994). YAP1 dependent activation of TRX2 is essential for the response of Saccharomyces cerevisiae to oxidative stress by hydroperoxides. EMBO J. 13, 655-664.
27. Lundstrom, J., and Holmgren, A. (1995). Glutaredoxin accelerates glutathione-dependent folding of reduced ribonuclease A together with protein disulfide-isomerase. J. Biol. Chem. 270, 7822-7828.
28. Lundstrom, J., Krause, G., and Holmgren, A. (1992). A Pro to His mutation in active site of thioredoxin increases its disulfide-isomerase activity 10-fold. New refolding systems for reduced or randomly oxidized ribonuclease. J. Biol. Chem. 267, 9047-9052.
29. Lyles, M.M., and Gilbert, H.F. (1991). Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer. Biochemistry 30, 613-619.
30. Massey, V., and Williams, C.H. (1965). On the reaction mechanism of yeast glutathione reductase. J. Biol. Chem. 240, 4470-4480.
31. Meister, A. (1989). Metabolism and function of glutathione. In: Coenzymes and Cofactors: Glutathione, ed. D. Dolphin, O. Avramovíc, and R. Poulson, Malabar, FL: Krieger Publishing, 367-462.
32. Meister, A. (1995). Glutathione metabolism. Methods Enzymol. 251, 3-7.
33. Michiels, C., Raes, M., Toussaint, O., and Remade, J. (1994). Importance of Se-giutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress. Free Radical Biol. Med. 17, 235-248.
34. Miranda Vizuete, A., Martinez Galisteo, E., Aslund, F., Lopez Barea, J., Pueyo, C., and Holmgren, A. (1994). Null thioredoxin and glutaredoxin Escherichia coli K-12 mutants have no enhanced sensitivity to mutagens due to a new GSH-dependent hydrogen donor and high increases in ribonucleotide reductase activity. J. Biol. Chem. 269, 16631-16637.
35. Moye Rowley, W.S., Harshman, K.D., and Parker, C.S. (1989). Yeast YAP1 encodes a novel form of the jun family of transcriptional activator proteins. Genes Dev 3, 283-292.
36. Muller, E.G. (1992). Thioredoxin genes in Saccharomyces cerevisiae: map positions of TRX1 and TRX2. Yeast 8, 117-120.
37. 1 interval of the cell cycle. J. Biol. Chem. 266, 9194-9202.
38. Muller, E.G.D. (1994). Deoxyribonucleotides are maintained at normal levels in a yeast thioredoxin mutant defective in DNA synthesis. J. Biol. Chem. 269, 24466-24471.
39. Muller, E.G.D. (1995). A redox-dependent function of thioredoxin is necessary to sustain a rapid rate of DNA synthesis in yeast. Arch. Biochem. Biophys. 318, 356-361.
40. Muller, S., Senn, H., Gsell, B., Vetter, W., Baron, C., and Bock, A. (1994). The formation of diselenide bridges in proteins by incorporation of selenocysteine residues: biosynthesis and characterization of (Se)2-thioredoxin. Biochemistry 33, 3404-3412.
41. Newton, G.L., Aguilera, J.A., Fahey, R.C., Ward, J.F., Radkowsky, A.E., and Kosower, E.M. (1992). para-sulfobenzoyloxybromobimane: a new membrane-impermeable reagent useful for the analysis of thiols and their export from cells. Anal. Biochem. 201, 30-42.
42. Nicotera, P., Moore, M., Bellomo, G., Mirabelli, F., and Orrenius, S. (1985). Demonstration and partial characterization of glutathione disulfide-stimulated ATPase activity in the plasma membrane fraction from rat hepatocytes. J. Biol. Chem. 260, 1999-2002.
43. Perham, R.N. (1987). Glutathione reductase from Escherichia coli: mutation, cloning and sequence analysis of the gene. Biochem. Soc. Trans. 15, 730-733.
44. Russel, M., and Holmgren, A. (1988). Construction and characterization of glutaredoxin-negative mutants of Escherichia coli. Proc. Natl. Acad. Sci. USA 85, 990-994.
45. Russel, M., and Model, P. (1985). Direct cloning of the trxB gene that encodes thioredoxin reductase. J. Bacteriol. 163, 238-242.
46. Russel, M., Model, P., and Holmgren, A. (1990). Thioredoxin or glutaredoxin in Escherichia coli is essential for sulfate reduction but not for deoxyribonucleotide synthesis. J. Bacteriol. 172, 1923-1929.
47. Schenk, H., Klein, M., Erdbrugger, W., Droge, W., and Schulze Osthoff, K. (1994). Distinct effects of thioredoxin and antioxidants on the activation of transcription factors NF-kappa B and AP-1. Proc. Natl. Acad. Sci. USA 91, 1672-1676.
48. Schnell, N., Krems, B., and Entian, K.D. (1992). The PARI (YAP1/ SNQ3) gene of Saccharomyces cerevisiae, a c-jun homologue, is involved in oxygen metabolism. Curr. Genet. 21, 269-273.
49. Sherman, F., Fink, G.R., and Hicks, J.B. (1986). Methods in Yeast Genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
50. Sikorski, R.S., and Hieter, P. (1989). A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27.
51. Tuggle, C.K., and Fuchs, J.A. (1985). Glutathione reductase is not required for maintenance of reduced glutathione in Escherichia coli K-12. J. Bacteriol. 162, 448-450.
52. Wallis, J.W., Chrebet, G., Brodsky, G., Rolfe, M., and Rothstein, R. (1989). A hyper-recombination mutation in S. cerevisiae identifies a novel eukaryotic topoisomerase. Cell 58, 409-419.
53. Wells, W.W., Yang, Y., Deits, T.L., and Gan, Z.R. (1993). Thioltransferases. Adv. Enzymol. Relat. Areas Mol. Biol. 66, 149-201.
54. Wu, A.L., and Moye Rowley, W.S. (1994). GSH1, which encodes gamma-glutamylcysteine synthetase, is a target gene for yAP-1 transcriptional regulation. Mol. Cell. Biol. 14, 5832-5839.