Resistance of Saccharomyces cerevisiae to Fungicide Chlorothalonil

  • Shin, Jae-Ho (Department of Agricultural Chemistry, Kyungpook National University) ;
  • Kim, Young-Mog (Institute of Agricultural Science & Technology, Kyungpook National University) ;
  • Park, Jong-Woo (Department of Agricultural Chemistry, Kyungpook National University) ;
  • Kim, Jang-Eok (Department of Agricultural Chemistry, Kyungpook National University) ;
  • Rhee, In-Koo (Department of Agricultural Chemistry, Kyungpook National University)
  • Published : 2003.09.01

Abstract

The toxicity of chlorothalonil on the growth of yeasts was investigated using several yeast strains. An alcohol tolerant yeast, Saccharomyces cerevisiae F38-1, was the most chlorothalonil-tolerant. The glutathione content and the glutathione S-transferase activity were related to the chlorothalonil-tolerant phenotype. Several thiol compounds affect the dissipation of chlorothalonil. However, there was no significant difference on the effects of chlorothalonil dissipation among the thiol compounds tested. The growth of yeast cells was arrested by chlorothalonil. It took about 13 h to dissipate 1 mg/l of chlorothalonil, and the growth was restored as the chlorothalonil content decreased. The glutathione content and glutathione S-transferase are suggested to be among the most important factors of yeast resistance to chlorothalonil.

Keywords

References

  1. Agric. Biol. Chem. v.52 Glutathione transferases from Mucor Javanicus Ando,K.;M.Honma;S.Chiba;S.Tahara;J.Mizutani https://doi.org/10.1271/bbb1961.52.135
  2. Biochem. J. v.147 Purification of two glutathione-S-transferase activities from rat liver Askelof,P.;C.Guthenberg;I.Jacobson;B.Mannervik https://doi.org/10.1042/bj1470513
  3. Appl. Environ. Microbiol. v.58 Unique and overlapping pollutant stress proteins of Escherichia coli Blom,A.;W.Harder;A.Martin
  4. Anal. Biochem. v.72 A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Bradford,M. https://doi.org/10.1016/0003-2697(76)90527-3
  5. Weed Sci. v.35 Initial metabolism of acetochlor in tolerant and susceptible seedlings Breaux,E.J.
  6. J. Biol. Chem. v.273 A novel membranebound glutathione S-transferase functions in the stationary phase of the yeast Saccharomyces cerevisiae Choi,J.H.;W.Lou;A.Vancura https://doi.org/10.1074/jbc.273.45.29915
  7. Biochem. Biophys. Res. Commun. v.248 Hsp104 responds to heat and oxidative stress with different intracellular localization in Saccharomyces cerevisiae Fujita,K.;R.Kawai;H.Iwahashi;Y.Komatsu https://doi.org/10.1006/bbrc.1998.9008
  8. Ann. Rev. Biochem. v.55 Metallothionein Hamer,D. https://doi.org/10.1146/annurev.bi.55.070186.004405
  9. J. Microbiol. Biotechnol. v.4 Characterization of cadmium-resistant yeast strain in response to cadmium or heat shock stress Huh,N.E.;N.S.Choi;Y.K.SEO;T.S.Yu;H.S.Lee
  10. J. Biol. Chem. v.274 Genetics analysis of glutathione peroxidase in oxidative stress response of Saccharomyces cerevisiae Inoue,Y.;T.Matsuda;K.Sugiyama;S.Izawa;A.Kimura https://doi.org/10.1074/jbc.274.38.27002
  11. Biochim. Biophys. Acta v.993 Cadmium-binding protein in a cadmium-resistant strain of Saccharomyces cerevisiae Inouhe,M.;M.Hiyama;H.Tohoyama;M.Joho;T.Murayama https://doi.org/10.1016/0304-4165(89)90142-6
  12. FEBS Lett. v.368 Oxidative stress response in yeast: effect of glutathione on adaptation to hydrogen peroxide stress in Saccharomyces cerevisiae Izawa,S.;Y.Inoue;A.Kimura https://doi.org/10.1016/0014-5793(95)00603-7
  13. Agric. Biol. Chem. v.52 Distribution, formation and stabilization of yeast glutathione S-transferase Kumagai,H.;H.Tamaki;Y.Koshino;H.Suzuki;T.Tochikura https://doi.org/10.1271/bbb1961.52.1377
  14. J. Agric. Food Chem. v.19 Metabolism of 2-chloro-n-isopropylacetanilide (propachlor) in the leaves of corn, sorghum, sugarcane, and barley Lamoureaux,G.L.;L.E.Stafford;F.S.Tanaka https://doi.org/10.1021/jf60174a011
  15. J. Agric. Food Chem. v.27 In vitro conjugation of glutathione and other thiols with acetanilide herbicides and EPTC sulfoxide and the action of the herbicide antidote R-25788 Leavitt,J.R.C.;D.Penner https://doi.org/10.1021/jf60223a004
  16. Ann. Rev. Genet. v.22 The heat-shock proteins Lindquist,S.;E.A.Craig https://doi.org/10.1146/annurev.ge.22.120188.003215
  17. Methods Enzymol. v.113 Methods for the selective modification of glutathione metabolism and study of glutathione transport Meister,A. https://doi.org/10.1016/S0076-6879(85)13077-6
  18. Annu. Rev. Biochem. v.52 Glutathione Meister,A.;M.E.Anderson https://doi.org/10.1146/annurev.bi.52.070183.003431
  19. Biochim. Biophys. Acta v.582 Levels of glutathione, glutathione reductase and glutathione-S-transferase activities in rat lung and liver Moron,M.S.;J.W.Depierre;B.Mannervik https://doi.org/10.1016/0304-4165(79)90289-7
  20. Metabolic pathways of agrochemicals. Part 2: Insecticides and fungicides Roberts,T.;D.Hutson
  21. J. Agric. Food. Chem. v.39 Conjugation of 2-chloroacetanilide herbicides with glutathione: Role of molecular structures and of glutathione S-transferase enzymes Scarponi,L.;P.Perucci;L.Martinetti https://doi.org/10.1021/jf00011a027
  22. J. Biol. Chem. v.265 Heat shock proteins Schlesinger,M.J.
  23. J. Biol. Chem. v.276 A genetic investigation of the essential role of glutathione: mutations in the proline biosynthesis pathway are the only suppressors of glutathione auxotrophy in yeast Spector,D.;J.Labarre;M.B.Toledano https://doi.org/10.1074/jbc.M009814200
  24. Anal. Biochem. v.27 Enzymatic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Application to mammalian blood and other tissue Tietze,F.