Yap1-regulated glutathione redox system curtails accumulation of formaldehyde and reactive oxygen species in methanol metabolism of Pichia pastoris

Eukaryotic Cell

Volumn 8, Issue 4, 2009, Pages 540-549

  Yano, Taisuke ^a   Takigami, Emiko ^a   Yurimoto, Hiroya ^a   Sakai, Yasuyoshi ^a,b  

^a KYOTO UNIVERSITY   (Japan)

^b JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

FORMALDEHYDE; FUNGAL PROTEIN; GLUTATHIONE; METHANOL; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR;

ARTICLE; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; OXIDATION REDUCTION REACTION; PICHIA;

FORMALDEHYDE; FUNGAL PROTEINS; GENE EXPRESSION REGULATION, FUNGAL; GLUTATHIONE; METHANOL; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; PICHIA; REACTIVE OXYGEN SPECIES; TRANSCRIPTION FACTORS;

PICHIA PASTORIS;

EID: 64749095823     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00007-09     Document Type: Article

References (51)

1. Bener Aksam, E., H. Jungwirth, S. D. Kohlwein, J. Ring, F. Madeo, M. Veenhuis, and I. J. van der Klei. 2008. Absence of the peroxiredoxin Pmp20 causes peroxisomal protein leakage and necrotic cell death. Free Radic. Biol. Med. 45:1115-1124.
2. Bergmeyer, H. U. 1955. Measurement of catalase activity. Biochem. Z. 327: 255-258.
3. Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
4. Charizanis, C., H. Juhnke, B. Krems, and K. D. Entian. 1999. The mitochondrial cytochrome c peroxidase Ccpl of Saccharomyces cerevisiae is involved in conveying an oxidative stress signal to the transcription factor Pos9 (Skn7). Mol. Gen. Genet. 262:437-447.
5. Coleman, S. T., E. A. Epping, S. M. Steggerda, and W. S. Moye-Rowly. 1999. Yaplp activates gene transcription in an oxidant-specific fashion. Mol. Cell. Biol. 19:8302-8313.
6. 2 sensing through oxidation of the Yapl transcription factor. EMBO J. 19:5157-5166.
7. del Río, L. A., F. J. Corpas, L. M. Sandalio, J. M. Palma, M. Gómez, and J. B. Barroso. 2002. Reactive oxygen species, antioxidant systems and nitric oxide in peroxisomes. J. Exp. Bot. 53:1255-1272.
8. 2sress conditions: the role of Yaplp in cell proliferation control in yeast. Mol. Microbiol. 36:830-845.
9. Fahey, R. C. 2001. Novel thiols of prokaryotes. Annu. Rev. Microbiol. 55: 333-556.
10. Gasch, A. P., P. T. Spellman, C. M. Kao, O. Carmel-Harel, M. B. Eisen, G. Storz, D. Botstein, and P. O. Brown. 2000. Genomic expression programs in the response of yeast cells to environmental changes. Mol. Biol. Cell 11: 4241-4257.
11. Grant, C. M., L. P. Collinson, J. Roe, and I. W. Dawes. 1996. Yeast glutathione reductase is required for the protection against oxidative stress and is a target gene for yAP-1 transcriptional regulation. Mol. Microbiol. 21:171-179.
12. Grant, C. M., F. H. Maciver, and I. W. Dawes. 1996. Stationary-phase induction of GLR1 expression is mediated by the yAP-1 transcriptional regulatory protein in the yeast Saccharomyces cerevisiae. Mol. Microbiol. 22:739-746.
13. He, X. J., and J. S. Fassler. 2005. Identification of novel Yaplp and Skn7p binding sites involved in the oxidative stress response of Saccharomyces cerevisiae. Mol. Microbiol. 58:1454-1467.
14. Horiguchi, H., H. Yurimoto, N. Kato, and Y. Sakai. 2001. Antioxidant system within yeast peroxisome. Biochemical and physiological characterization of CbPmp20 in the methylotrophic yeast Candida boidinii. J. Biol. Chem. 276: 14279-14288.
15. Horiguchi, H., H. Yurimoto, T. K. Goh, T. Nakagawa, N. Kato, and Y. Sakai. 2001. Peroxisomal catalase in the methylotrophic yeast Candida boidinii: transport efficiency and metabolic significance. J. Bacteriol. 183:6372-6383.
16. Inoue, Y., T. Matsuda, K. Sugiyama, S. Izawa, and A. Kimura. 1999. Genetic analysis of glutathione peroxidase in oxidative stress response of Saccharomyces cerevisiae. J. Biol. Chem. 274:27002-27009.
17. Jamieson, D. J. 1998. Oxidative stress responses of the yeast Saccharomyces cerevisiae. Yeast 14:1511-1527.
18. Jiménez, A., J. A. Hernández, L. A. del Río, and F. Sevilla. 1997. Evidence for the presence of the ascorbate-glutathione cycle in mitochondria and peroxisomes of pea leaves. Plant Physiol. 114:275-284.
19. Kuge, S., and N. Jones. 1994. YAP1 dependent activation of TRX2 is essential for the response of Saccharomyces cerevisiae to oxidative stress by hydroperoxides. EMBO J. 13:655-664.
20. Kuge, S., N. Jones, and A. Nomoto. 1997. Regulation of yAP-1 nuclear localization in response to oxidative stress. EMBO J. 16:1710-1720.
21. Kuge, S., T. Toda, N. Iizuka, and A. Nomoto. 1998. Crml (XpoI) dependent nuclear export of the budding yeast transcription factor yAP-1 is sensitive to oxidative stress. Genes Cells 3:521-532.
22. Kuge, S., M. Arita, A. Murayama, K. Maeta, S. Izawa, Y. Inoue, and A. Nomoto. 2001. Regulation of the yeast Yaplp nuclear export signal is mediated by redox signal-induced reversible disulfide bond formation. Mol. Cell. Biol. 21:6139-6150.
23. Lee, J., C. Godon, G. Lagniel, D. Spector, J. Garin, J. Labarre, and M. B. Toledano. 1999. Yapl and Skn7 control two specialized oxidative stress response regulons in yeast. J. Biol. Chem. 274:16040-16046.
24. Menezes, R. A., C. Amaral, L. Batista-Nascimento, C. Santos, R. B. Ferreira, F. Devaux, E. C. Eleutherio, and C. Rodrigues-Pousada. 2008. Contribution of Yapl towards Saccharomyces cerevisiae adaptation to arsenic-mediated oxidative stress. Biochem. J. 414:301-311.
25. Monosov, E. D., T. J. Wenzel, G. H. Lüers, J. A. Heyman, and S. Subramani. 1996. Labeling of peroxisomes with green fluorescent protein in living P. pastoris cells. J. Histochem. Cytochem. 44:581-589.
26. Mukaiyama, H., M. Oku, M. Baba, T. Samizo, A. T. Hammond, B. S. Glick, N. Kato, and Y. Sakai. 2002. Paz2 and 13 other PAZ gene products regulate vacuolar engulfment of peroxisomes during micropexophagy. Genes Cells 7:75-90.
27. Outten, C. E., and V. C. Culotta. 2004. Alternative start sites in the Saccharomyces cerevisiae GLR1 gene are responsible for mitochondrial and cytosolic isoforms of glutathione reductase. J. Biol. Chem. 279:7785-7791.
28. Penninckx, M. J. 2002. An overview on glutathione in Saccharomyces versus non-conventional yeasts. FEMS Yeast Res. 2:295-305.
29. Powis, G., M. Briehl, and J. Oblong. 1995. Redox signaling and the control of cell growth and death. Pharmacol. Ther. 68:149-173.
30. Rost, J., and S. Rapoport. 1964. Reduction-potential of glutathione. Nature 201:185.
31. Sahm, H. 1977. Metabolism of methanol by yeast. Adv. Biochem. Eng. 6:77-103.
32. Sakai, Y., A. Koller, L. K. Rangell, G. A. Keller, and S. Subramani. 1998. Peroxisome degradation by microautophagy in Pichia pastoris: identification of specific steps and morphological intermediates. J. Cell Biol. 141:625-636.
33. Sakai, Y., T. Nakagawa, M. Shimase, and N. Kato. 1998. Regulation and physiological role of the DAS1 gene, encoding dihydroxyacetone synthase, in the methylotrophic yeast Candida boidinii. J. Bacteriol. 180:5885-5890.
34. Sakai, Y., H. Yurimoto, H. Matsuo, and N. Kato. 1998. Regulation of peroxisomal proteins and organelle proliferation by multiple carbon sources in the methylotrophic yeast Candida boidinii. Yeast 14:1175-1187.
35. Schnell, N, B. Krems, and K. D. Entian. 1992. The PAR1 (YAP1/SNQ3) gene of Saccharomyces cerevisiae, a c-jun homologue, is involved in oxygen metabolism. Curr. Genet. 21:269-273.
36. Sears, I. B., J. O'Connor, O. W. Rossanese, and B. S. Glick. 1998. A versatile set of vectors for constitutive and regulated gene expression in Pichia pastoris. Yeast 14:783-790.
37. 2 are non-essential for energy supply of yeast methylotrophic growth. Arch. Microbiol. 154:566-575.
38. Smith, I. K., T. L. Vierheller, and C. A. Thorne. 1988. Assay of glutathione reductase in crude tissue homogenates using 5,5'-dithiobis(2- nitrobenzoic acid). Anal. Biochem. 175:408-413.
39. Song, J., J. Cha, J. Lee, and J. Roe. 2006. Glutathione reductase and a mitochondrial thioredoxin play overlapping roles in maintaining iron-sulfur enzymes in fission yeast. Eukaryot. Cell 5:1857-1865.
40. Stephen, D. W., S. L. Rivers, and D. J. Jamieson. 1995. The role of the YAP1 and YAP2 genes in the regulation of the adaptive oxidative stress responses of Saccharomyces cerevisiae. Mol. Microbiol. 16:415-423.
41. Tietze, F. 1969. Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal. Biochem. 27:502-506.
42. Tolbert, N. E. 1974. Isolation of subcellular organelles of metabolism on isopycnic sucrose gradients. Methods Enzymol. 31:734-746.
43. Toone, W. M, B. A. Morgan, and N. Jones. 2001. Redox control of AP-1-like factors in yeast and beyond. Oncogene 20:2336-2346.
44. van der Klei, I. J., H. Yurimoto, Y. Sakai, and M. Veenhuis. 2006. The significance of peroxisomes in methanol metabolism in methylotrophic yeast. Biochim. Biophys. Acta 1763:1453-1462.
45. Veenhuis, M., F. A. Salomons, and I. J. van der Klei. 2000. Peroxisome biogenesis and degradation in yeast: a structure/function analysis. Microsc. Res. Tech. 51:584-600.
46. 2 and diamide. J. Biol. Chem. 272:7908-7914.
47. Wheeler, G. L., E. W. Trotter, I. W. Dawes, and C. M. Grant. 2003. Coupling of the transcriptional regulation of glutathione biosynthesis to the availability of glutathione and methionine via the Met4 and Yapl transcription factors. J. Biol. Chem. 278:49920-49928.
48. Wu, A.-L., and W. S. Moye-Rowley. 1994. GSH1, which encodes 7-glutamylcysteine synthetase, is a target gene for yAP-1 transcriptional regulation. Mol. Cell. Biol. 14:5832-5839.
49. Yamada, K., C. W. Nakagawa, and N. Mutoh. 1999. Schizosaccharomyces pombe homologue of glutathione peroxidase, which does not contain selenocysteine, is induced by several stresses and works as an antioxidant. Yeast 15:1125-1132.
50. Yan, C., L. H. Lee, and L. I. Davis. 1998. Crmlp mediates regulated nuclear export of a yeast AP-1-like transcription factor. EMBO J. 17:7416-7429.
51. Yurimoto, H., N. Kato, and Y. Sakai. 2005. Assimilation, dissimilation, and detoxification of formaldehyde, a central metabolic intermediate of methylotrophic metabolism. Chem. Rec. 5:367-375.