The Saccharomyces cerevisiae LYS7 gene is involved in oxidative stress protection

European Journal of Biochemistry

Volumn 251, Issue 3, 1998, Pages 716-723

  Gamonet, Franck ^a   Lauquin, Guy J M ^a,b  

^a CNRS   (France)

^b Institut de Biochimie et Genetique Cellulaires   (France)

Author keywords

Amyotrophic lateral sclerosis; Copper; Lysine biosynthesis; Superoxide dismutase; Yeast

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; LYSINE;

AMINO ACID SYNTHESIS; AMYOTROPHIC LATERAL SCLEROSIS; ARTICLE; CELL PROTECTION; DEHYDRATION; ENZYME ACTIVE SITE; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE;

ALLELES; AMINO ACID SEQUENCE; AMYOTROPHIC LATERAL SCLEROSIS; COPPER; CYTOSOL; FUNGAL PROTEINS; HUMANS; ISOENZYMES; LYSINE; METHIONINE; MITOCHONDRIA; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; OXIDATIVE STRESS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SUPEROXIDE DISMUTASE; SUPEROXIDES;

EID: 0032006077     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2510716.x     Document Type: Article

References (67)

1. Bilinski, T., Krawiec, Z., Liczmanski, A. & Litwinska, J. (1985) Is hydroxyl radical generated by the Fenton reaction in vivo? Biochem. Biophys. Res. Commun. 130, 533-539.
2. Fridovich, I. (1978) The biology of oxygen radicals, Science 201, 875-880.
3. +: in vitro and in vivo, Free Radical Biol. Med. 16, 29-33.
4. Jamieson, D. (1989) Oxygen toxicity and reactive oxygen metabolites in mammals, Free Radical Biol. Med. 7, 87-108.
5. Halliwell, B. & Gutteridge, J. M. (1984) Oxygen toxicity, oxygen radicals, transition metals and disease, Biochem. J. 219, 1-14.
6. Davies, K. J. (1987) Protein damage and degradation by oxygen radicals, I. General aspects, J. Biol. Chem. 262, 9895-9901.
7. Imlay, J. A. & Linn, S. (1988) DNA damage and oxygen radical toxicity, Science 240, 1302-1309.
8. Nakazono, K., Watanabe, N., Matsuno, K., Sasaki, J., Sato, T. & Inoue, M. (1991) Does superoxide underlie the pathogenesis of hypertension? Proc. Natl Acad. Sci. USA 88, 10045-10048.
9. Halliwell, B. (1987) Oxidants and human disease: some new concepts, FASEB J. 1, 358-364.
10. Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H. X., Rahmani, Z., Krizus, A., McKenna-Yasek, D., Cayabyab, A., Gaston, S. M., Berger, R., Tanzi, R. E., Halperin, J. J., Herzfeldt, B., Van den Bergh, R., Hung, W. Y., Bied, T., Deng, G., Mulder, D. W., Smyth, C., Laing, N. G., Soriano, E., Pericak-Vance, M. A., Haines, J., Rouleau, G. A., Gusella, G. F., Horvitz, H. R. & Brown, R. H. (1993) Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis, Nature 362, 59-62.
11. Trush, M. A. & Kensler, T. W. (1991) An overview of the relationship between oxidative stress and chemical carcinogenesis, Free Radical Biol. Med. 10, 201-209.
12. Jenner, P. & Olanow, C. W. (1996) Oxidative stress and the pathogenesis of Parkinson's disease, Neurology 47, S161-S170.
13. Remacle, J. & Renard, P. (1996) Role of oxidative stress in aging, Pathol. Biol. (Paris) 44, 65-76.
14. Michiels, C., Raes, M., Toussaint, O. & Remacle, J. (1994) Importance of Se-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress, Free Radical Biol. Med. 17, 235-248.
15. McCord, J. M. & Fridovich, I. (1969) Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein), J. Biol. Chem. 244, 6049-6055.
16. Bannister, J. V., Bannister, W. H. & Rotilio, G. (1987) Aspects of the structure, function, and applications of superoxide dismutase, CRC Crit. Rev. Biochem. 22, 111-180.
17. Beyer, W., Imlay, J. & Fridovich, I. (1991) Superoxide dismutases, Prog. Nucleic Acid Res. Mol. Biol. 40, 221-253.
18. Marres, C. A., Van Loon, A. P., Oudshoorn, P., Van Steeg, H., Grivell, L. A. & Slater, E. C. (1985) Nucleotide sequence analysis of the nuclear gene coding for manganese superoxide dismutase of yeast mitochondria, a gene previously assumed to code for the Rieske iron-sulphur protein, Eur. J. Biochem. 147, 153-161.
19. Bermingham-McDonogh, O., Gralla, E. B. & Valentine, J. S. (1988) The copper, zinc-superoxide dismutase gene of Saccharomyces cerevisiae: cloning, sequencing, and biological activity, Proc. Natl Acad. Sci. USA 85, 4789-4793.
20. Gralla, E. B. & Kosman, D. J. (1992) Molecular genetics of superoxide dismutases in yeasts and related fungi, Adv. Genet. 30, 251-319.
21. Culotta, V. C., Joh, H. D., Lin, S. J., Slekar, K. H. & Strain, J. (1995) A physiological role for Saccharomyces cerevisiae copper/ zinc superoxide dismutase in copper buffering, J. Biol. Chem. 270, 29991-29997.
22. Gralla, E. B., Thiele, D. J., Silar, P. & Valentine, J. S. (1991) ACE1, a copper-dependent transcription factor, activates expression of the yeast copper, zinc superoxide dismutase gene, Proc. Natl Acad. Sci. USA 88, 8558-8562.
23. Thiele, D. J. (1988) ACE1 regulates expression of the Saccharomyces cerevisiae metallothionein gene, Mol. Cell. Biol. 8, 2745-2752.
24. Galiazzo, F. & Labbe-Bois, R. (1993) Regulation of Cu, Zn- and Mn-superoxide dismutase transcription in Saccharomyces cerevisiae, FEBS Lett. 315, 197-200.
25. Galiazzo, F., Ciriolo, M. R., Carri, M. T., Civitareale, P., Marcocci, L., Marmocchi, F. & Rotilio, G. (1991) Activation and induction by copper of Cu/Zn superoxide dismutase in Saccharomyces cerevisiae. Presence of an inactive proenzyme in anaerobic yeast, Eur. J. Biochem. 196, 545-549.
26. Bhattacharjee, J. K., Tucci, A. F. & Strassman, M. (1968) Accumulation of alpha-ketoglutaric acid in yeast mutants requiring lysine, Arch. Biochem. Biophys. 123, 235-239.
27. Dubois, E., Bercy, J. & Messenguy, F. (1987) Characterization of two genes, ARGRI and ARGRIII required for specific regulation of arginine metabolism in yeast, Mol. Gen. Genet. 207, 142-148.
28. Horecka, J., Kinsey, P. T. & Sprague, G. F. Jr (1995) Cloning and characterization of the Saccharomyces cerevisiae LYS7 gene: evidence for function outside of lysine biosynthesis, Gene (Amst.) 162, 87-92.
29. Gamonet, F. & Lauquin, G. J.-M. (1996) Second and third steps of lysine biosynthesis are catalyzed by a single enzyme encoded by LYS4, in Yeast genetics and molecular biology meeting. UW-Madison (Johnston, M. & Winston, F., eds) p. 284B, Genetics Society of America, Bethesda.
30. Rothstein, R. J. (1983) One-step gene disruption in yeast, Methods Enzymol. 101, 202-211.
31. Gralla, E. B. & Valentine, J. S. (1991) Null mutants of Saccharomyces cerevisiae Cu, Zn superoxide dismutase: characterization and spontaneous mutation rates, J. Bacteriol. 173, 5918-5920.
32. Dancis, A., Yuan, D. S., Haile, D., Askwith, C., Elde, D., Moehle, C., Kaplan, J. & Klausner, R. D. (1994) Molecular characterization of a copper transport protein in S. cerevisiae: an unexpected role for copper in iron transport, Cell 76, 393-402.
33. Ausubel, F., Brent, R., Kingston, R., Moore, D., Seidman, J., Smith, J. & Struhl, K. (1992) Current protocols in molecular biology, John Wiley & Sons, Inc., New York.
34. Sherman, F., Fink, G. & Lawrence, C. (1974) Methods in yeast genetics, Cold Spring Harbor Laboratory, Cold Spring Harbor NY.
35. Nishida, C. R., Gralla, E. B. & Valentine, J. S. (1994) Characterization of three yeast copper-zinc superoxide dismutase mutants analogous to those coded for in familial amyotrophic lateral sclerosis, Proc. Natl Acad. Sci. USA 91, 9906-9910.
36. Christianson, T. W., Sikorski, R. S., Dante, M., Shero, J. H. & Hieter, P. (1992) Multifunctional yeast high-copy-number shuttle vectors, Gene (Amst.) 110, 119-122.
37. Rose, M. D., Novick, P., Thomas, J. H., Botstein, D. & Fink, G. R. (1987) A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector, Gene (Amst.) 60, 237-243.
38. Botstein, D., Falco, S. C., Stewart, S. E., Brennan, M., Scherer, S., Stinchcomb, D. T., Struhl, K. & Davis, R. W. (1979) Sterile host yeasts (SHY): a eukaryotic system of biological containment for recombinant DNA experiments, Gene (Amst.) 8, 17-24.
39. Dancis, A., Haile, D., Yuan, D. S. & Klausner, R. D. (1994) The Saccharomyces cerevisiae copper transport protein (Ctr1p). Biochemical characterization, regulation by copper, and physiologic role in copper uptake, J. Biol. Chem. 269, 25660-25667.
40. Boucherie, H., Dujardin, G., Kermorgant, M., Monribot, C., Slonimski, P. & Perrot, M. (1995) Two-dimensional protein map of Saccharomyces cerevisiae: construction of a gene-protein index. Yeast 11, 601-613.
41. Beauchamp, C. & Fridovich, I. (1971) Superoxide dismutase: improved assays and an assay applicable to acrylamide gels, Anal. Biochem. 44, 276-287.
42. Wang, X., Culotta, V. C. & Klee, C. B. (1996) Superoxide dismutase protects calcineurin from inactivation, Nature 383, 434-437.
43. Miller, J. (1972) Experiments in molecular genetics, Cold Spring Harbor Laboratory, Cold Spring Harbor NY.
44. Maniatis, T., Fritsch, E. F. & Sambrook, J. (1982) Molecular cloning: a laboratory manual, Cold Spring Harbor Laboratory, Cold Spring Harbor NY.
45. Gallwitz, D. & Sures, I. (1980) Structure of a split yeast gene : complete nucleotide sequence of the actin gene in Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 77, 2546-2550.
46. Feinberg, A. P. & Vogelstein, B. (1984) A technique for radiolabeling DNA restriction endonuclease fragments to high specific-activity. Anal. Biochem. 137, 266-267.
47. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
48. Mendoza, I., Rubio, F., Rodriguez-Navarro, A. & Pardo, J. M. (1994) The protein phosphatase calcineurin is essential for NaCl tolerance of Saccharomyces cerevisiae, J. Biol. Chem. 269, 8792-8796.
49. 2+/calmodulin-dependent phosphoprotein phosphatase (calcineurin) and cAMP-dependent protein kinase, Mol. Gen. Genet. 249, 257-264.
50. Yuan, D. S., Stearman, R., Dancis, A., Dunn, T., Beeler, T. & Klausner, R. D. (1995) The Menkes/Wilson disease gene homologue in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake, Proc. Natl Acad. Sci. USA 92, 2632-2636.
51. Butt, T. R., Sternberg, E. J., Gorman, J. A., Clark, P., Hamer, D., Rosenberg, M. & Crooke, S. T. (1984) Copper metallothionein of yeast, structure of the gene, and regulation of expression, Proc. Natl Acad. Sci. USA 81, 3332-3336.
52. Massey, V., Strickland, S., Mayhew, S. G., Howell, L. G., Engel, P. C., Matthews, R. G., Schuman, M. & Sullivan, P. A. (1969) The production of superoxide anion radicals in the reaction of reduced flavins and flavoproteins with molecular oxygen, Biochem. Biophys. Res. Commun. 36, 891-897.
53. Glerum, D. M., Shtanko, A. & Tzagoloff, A. (1996) Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase, J. Biol. Chem. 271, 14504-14509.
54. Capaldi, R. A. (1990) Structure and function of cytochrome c oxidase, Annu. Rev. Biochem. 59, 569-596.
55. Beinert, H. & Kennedy, M. C. (1993) Aconitase, a two-faced protein: enzyme and iron regulatory factor. FASEB J. 7, 1442-1449.
56. Tamai, K. T., Gralla, E. B., Ellerby, L. M., Valentine, J. S. & Thiele, D. J. (1993) Yeast and mammalian metallothioneins functionally substitute for yeast copper-zinc superoxide dismutase, Proc. Natl Acad. Sci. USA 90, 8013-8017.
57. Djinovic, K., Gatti, G., Coda, A., Antolini, L., Pelosi, G., Desideri, A., Falconi, M., Marmocchi, F., Rotilio, G. & Bolognesi, M. (1992) Crystal structure of yeast Cu, Zn superoxide dismutase. Crystallographic refinement at 2.5 Å resolution, J. Mol. Biol. 225, 791-809.
58. Lin, S. J., Pufahl, R. A., Dancis, A., O'Halloran, T. V. & Culotta, V. C. (1997) A role for the Saccharomyces cerevisiae ATXI gene in copper trafficking and iron transport, J. Biol. Chem. 272, 9215-9220.
59. Glerum, D. M., Shtanko, A. & Tzagoloff, A. (1996) SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae, J. Biol. Chem. 271, 20531-20535.
60. Culotta, V. C., Klomp, L. W., Strain, J., Casareno, R. L., Krems, B. & Gitlin, J. D. (1997) The copper chaperone for superoxide dismutase, J. Biol. Chem. 272, 23469-23472.
61. Weidner, G., Steffan, B. & Brakhage, A. A. (1997) The Aspergillus nidulans lysF gene encodes homoaconitase, an enzyme involved in the fungus-specific lysine biosynthesis pathway, Mol. Gen. Genet. 255, 237-247.
62. Liu, X. F., Elashvili, I., Gralla, E. B., Valentine, J. S., Lapinskas, P. & Culotta, V. C. (1992) Yeast lacking superoxide dismutase. Isolation of genetic suppressors, J. Biol. Chem. 267, 18298-18302.
63. Brown, R. H. Jr (1995) Amyotrophic lateral sclerosis: recent insights from genetics and transgenic mice, Cell 80, 687-692.
64. Siddique, T., Nijhawan, D. & Hentati, A. (1996) Molecular genetic basis of familial ALS, Neurology 47, S27-S35.
65. Siddique, T., Pericak-Vance, M. A., Brooks, B. R., Roos, R. P., Hung, W. Y., Antel, J. P., Munsat, T. L., Phillips, K., Warner, K., Speer, M., Bias, W. B., Siddique, N. A. & Ross, A. D. (1989) Linkage analysis in familial amyotrophic lateral sclerosis, Neurology 39, 919-925.
66. Siddique, T., Figlewicz, D. A., Pericak-Vance, M. A., Haines, J. L., Rouleau, G., Jeffers, A. J., Sapp, P., Hung, W. Y., Bebout, J., McKenna-Yasek, D., Deng, G., Horwitz, H. R., Gusella, J. F., Brown, R. H. Jr & Roses, A. D. (1991) Linkage of a gene causing familial amyotrophic lateral sclerosis to chromosome 21 and evidence of genetic-locus heterogeneity, N. Engl. J. Med. 324, 1381-1384.
67. Hentati, A., Bejaoui, K., Pericak-Vance, M. A., Hentati, F., Speer, M. C., Hung, W. Y., Figlewicz, D. A., Haines, J., Rimmler, J., Ben Hamida, C., Ben Hamida, M., Brown, R. H. Jr & Siddique, T. (1994) Linkage of recessive familial amyotrophic lateral sclerosis to chromosome 2q33-q35, Nat. Genet. 7, 425-428.