BMB Reports

Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
권호 표지
DOI QR코드

DOI QR Code

Transcription of Schizosaccharomyces pombe Thioltransferase-1 in Response to Stress Conditions

  • Kim, Min-Jung (Department of Genetic Engineering, Chongju University) ;
  • Lim, Chang-Jin (Division of Life Sciences, Kangwon National University) ;
  • Kim, Dae-Myung (Department of Genetic Engineering, Chongju University)
  • Published : 2002.07.31
Download PDF
⟨ Previous Next ⟩

Abstract

Thioltransferase, also known as glutaredoxin, is an enzyme that catalyzes the reduction of a variety of disulfide compounds. In Schizosaccharomyces pombe, two thioltransferases were reported and the cDNA of one of the thioltransferases (thioltransferase-1) was cloned. Using a Northern blot assay, we investigated the thioltransferase transcription in response to various stress conditions. When the culture was shifted to a high temperature, the thioltransferases transcription was not significantly changed compared to the unshifted $30^{\circ}C$ culture. Treatment of zinc chloride to exponentially-growing cells remarkably increased the thioltransferase transcription, whereas the treatment of mercury chloride greatly reduced the transcription. Treatment of hydrogen peroxide and cadmium chloride caused no significant effects on the transcription of the thioltransferase. These results suggest that the transcription of thioltransferase-1 in S. pombe is induced in response to metal stress that is caused by zinc chloride, but not in response to heat stress or oxidative stress that is caused by hydrogen peroxide.

Keywords

References

  1. Alfa, C., Fantes, P., Hyams, J., McLeod, M. and Warbrick, E. (1993) Experiments with Fission Yeast, pp. 133-136, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
  2. Cho, Y. -W., Kim, H. -G., Park, E. -H., Fuchs, J. A and Lim, C. -J. (2000a) Cloning, expression and regulation of Schizosacclwmmyces pombe gene encoding thioltransferase. Biochim Biophys. Acta 1517, 171-175. https://doi.org/10.1016/S0167-4781(00)00242-6
  3. Cho, Y. -W., Park, E. -H. and Lim, C. -J. (2000b) Regulation of thioltransferase activity from Schizosacchammyces pombe. J. Biochem. Mol. Biol. 33, 422-425.
  4. Cho, Y. -W .. Park, E. -H. and Lim, C. -J. (2000c) Catalase, glutathione S-transferase and thioltransferase respond differently to oxidative stress in Schizosacclwmmyces pombe. J Biochem. Mol. BioI. 33. 344-348.
  5. Chrestensen. C. A, Eckma, C. B., Starke, D. W. and Mieyal, J. J. (1995) Cloning. expression and characterization of human thioltransferase (glutaredoxin) in E. coli. FEBS Left. 374, 25-28. https://doi.org/10.1016/0014-5793(95)01066-N
  6. Davis, D. A, Newcomb, F. M., Starke, D. w., Ott, D. E., Mieyal, J. J. and Yarchoan, R. (1997) Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitm. J. BioI. Chem. 272, 25935-25940 https://doi.org/10.1074/jbc.272.41.25935
  7. Fuchs, J. A (1977) Isolation of an Escherichia coli mutant deficient in thioredoxin reductase. J. Bacteriol. 129, 967-972.
  8. Grant, C. M., Luikenhuis, S .. Beckhouse, A, Soderbergh, M. and Dawes, l. W. (2000) Differential regulation of glutaredoxin gene expression in response to stress conditions in the yeast Sacchammyces cerevisiae. Biochim. Biophys. Acta 1490, 33-42. https://doi.org/10.1016/S0167-4781(99)00234-1
  9. Holmgren, A. (1989) Thioredoxin and glutaredoxin systems. J Biot. Chem. 264, 13963-13966.
  10. Holmgren, A (1990) Glutathione: Structure and function; in Glutathione: metabolism and physiological .functions, Vina, J. (ed.), pp. 146-154, CRC Press, Boca Raton, Florida.
  11. Holmgren, A. and Aslund, F. (1995) Glutaredoxin. Methods Enzymol. 252. 283-292. https://doi.org/10.1016/0076-6879(95)52031-7
  12. Hoog, J. 0., Jomvall, H., Holmgren, A, Carlquist, M. and Persson, M. (1983) The primary structure of Escherichia coli glutaredoxin; distant homology with thioredoxins in a superfamily of small proteins with a redox-active cystine disulfide/cysteine dithiol J. Biochem. 136, 223-232.
  13. Kim. H. -G .. Park, E. -H. and Lim, C. -J. (1998) Thioltransferase from Schizosacchammyces pombe; purification to homogeneity and some properties. Mol. Cells 8, 431-437.
  14. Kim. H. -G., Park, E. -H. and Lim, C. -J. (l999a) A second thioltransferase of Schizosacchammyces pombe contains glutathione S-transferase activity. J. Biochem. Mol. Biol. 32, 535-540.
  15. Kim, H. -G., Cho, Y. -W, Park, E. -H., Park, S. -S., Ahn, K. -S. and Lim, C. -J. (l999b) Cloning, nucleotide sequence and expression of thioltransferase (glutaredoxin) cDNA from Schizosaccharomyces pombe. Mol. Cells 9, 668-672.
  16. Kunitomo, H., Higuchi, T., lino, Y and Yamamoto, M. (2000) A zinc-finger protein, Rst2p, regulates transcription of the fission yeast $ste11^{+}$ gene, which encodes a pivotal transcription factor for sexual development. Mol. Biol. Cell 11, 3205-3217 https://doi.org/10.1091/mbc.11.9.3205
  17. Luikenhuis, S., Perrone, G., Dawes, I. W. and Grant, C. M. (1998) The Yeast Saccharomyces cerevisiae contains two glutaredoxin gene that are required for protection against reactive oxygen species. Mol. BioI. Cell 9, 1081-1091. https://doi.org/10.1091/mbc.9.5.1081
  18. Nischt, R., Thuroff, E. and Kaufer, M. E (1986) Molecular cloning of a ribosomal protein gene from the fission yeast Schizosaccharomyces pombe. Curr. Genet. 10, 365-370. https://doi.org/10.1007/BF00418408
  19. Raghavachari, N. and Lou, M. E (1996) Evidence for the presence of thioltransferase in the lens. Exp. Eye Res. 63, 433-441. https://doi.org/10.1006/exer.1996.0133
  20. Rodriguez-Manzaneque, M. T., Ros, J.. Cabiscol, E., Sorribas, A and Herrero, E. (1999) Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae. Mol. Cell. BioI. 19, 8180-8190 https://doi.org/10.1128/MCB.19.12.8180
  21. Shi, J., Vlamis-Gardikas, A, Aslund, E, Holmgren, A and Rosen, B. P. (1999) Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction. J BioI. Chem. 274, 36039-36042. https://doi.org/10.1074/jbc.274.51.36039
  22. Terada, T. (1994) Thioltransfera~e can utilize cysteamine the same as glutathione as a reductant during the restoration of cysteamine-treated glucose 6-phosphate dehydrogenase activity. Biochem. Mol. Bioi. Int. 34, 723-727.
  23. Terada, T., Oshida, T., Nishimura, M., Maeda, H., Hara, T., Hosomi, S., Mizoguchi, T. and Nishimura, T. (1992) Study on human erythrocyte thioltransferase; comparative characterization with bovine enzyme and its physiological role under oxidative stress. J. Biochem. 111, 688-692. https://doi.org/10.1093/oxfordjournals.jbchem.a123819
  24. Tsang, M. L.-S. (1981) Assimilatory sulfate reduction in Escherichia coli; identification of the alternate cofactor for adenosine 3' -phosphate 5' -phosphosulfate reductase as glutaredoxin. J. Bacteriol. 146, 1059-1066.
  25. Washbum, M. P. and Wells, W. W. (1997) Glutathione dependent reduction of alloxan to dialuric acid catalyzed by thioltransferase (glutaredoxin); a possible role for thioltransferase in alloxan toxicity. Free Radic. BioI. Med. 23, 563-570. https://doi.org/10.1016/S0891-5849(97)00001-4
  26. Wells, W. W., Xu, D. P., Yang, Y and Rocque, P. A (1990) Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity. J. Biol. Chem. 265, 15361-15364.
  27. Yoshitake, S., Nanri, H., Fernando, M. R., and Minakimi, S. (1994) Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins. J. Biochem. 116, 42-46. https://doi.org/10.1093/oxfordjournals.jbchem.a124500
  28. Zheng, M., Aslund, F., Storz, G. (1998) Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279, 1718-1721. https://doi.org/10.1126/science.279.5357.1718

Cited by

  1. Carbon source-dependent regulation of a second gene encoding glutaredoxin from the fission yeast Schizosaccharomyces pombe vol.32, pp.1, 2005, https://doi.org/10.1007/s11033-004-3213-0
  2. Isolation and characterization of methyl jasmonate‐inducible genes in chinese cabbage vol.7, pp.4, 2003, https://doi.org/10.1080/12265071.2003.9647725
  3. Characterization of a Salicylic Acid- and Pathogen-induced Lipase-like Gene in Chinese Cabbage vol.36, pp.5, 2003, https://doi.org/10.5483/BMBRep.2003.36.5.433
  4. Methods for monitoring oxidative stress response in yeasts vol.19, pp.4, 2005, https://doi.org/10.1002/jbt.20091
  5. The Gene Encoding γ-Glutamyl Transpeptidase II in the Fission Yeast Is Regulated by Oxidative and Metabolic Stress vol.38, pp.5, 2005, https://doi.org/10.5483/BMBRep.2005.38.5.609