BMB Reports

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

The Effect of NaCI Treatment on the Freezing Tolerance and Protein Patterns of Carrot Callus Suspension Culture

  • Moon, Soon-Ok (Department of Genetic Engineering, The University of Suwon) ;
  • Park, Sook-Hee (Department of Genetic Engineering, The University of Suwon) ;
  • Cho, Bong-Heuy (Division of Life Science, The University of Suwon)
  • Received : 1996.10.16
  • Published : 1997.01.31
Download PDF
⟨ Previous Next ⟩

Abstract

The growth. freezing resistance and electrophoretic protein patterns of carrot callus cultures were investigated following treatment with NaCl for various' intervals at 20$^{\circ}C$. Following 7 day exposure to 250 mM NaCl. freezing tolerance increased, which was measured by 2.3.5-triphenyl tetrazolium chloride (TTC) assay and fresh weight was reduced compared to control cells. Changes of electrophoretic patterns of total and boiling stable proteins were investigated using one or two dimensional gel system. Several proteins with molecular weight of 43 and 21 kDa increased by NaCl treatment. The most prominent change was detected in 21 kDa protein. The steady state level of this protein increased in NaCl treated cells, but decreased in control cells. Twenty one kDa protein was detected only in the NaCl treated cell when boiling stable protein was analyzed. The isoelectric point of 21 kDa protein was identified as 5.7. The timing of increase of 21 kDa protein was correlated to freezing resistance which implied the role of this protein in the induction of freezing resistance of the cell.

Keywords

References

  1. Plant Physiol. v.73 Chen, Y.H.H.;Gusta, L.V. https://doi.org/10.1104/pp.73.1.71
  2. Plant Mol. Biol. v.13 Close, T.J.;Fenton Kortt, A.A.;Chandler, P.M. https://doi.org/10.1007/BF00027338
  3. Plant Physiol. v.101 Close, T.J.;Lammers, P.J. https://doi.org/10.1104/pp.101.3.773
  4. Can. J. Bot. v.62 Cloutier, Y. https://doi.org/10.1139/b84-055
  5. Plant Physiol. v.57 Cox, W. https://doi.org/10.1104/pp.57.4.553
  6. Plant Mol. Biol. v.12 Dure, L. III;Crouch, M.;Harada, J.;Ho, T.H.D.;Mundy, J.;Quatrano, R.;Thomas, T.;Sung, Z.R. https://doi.org/10.1007/BF00036962
  7. Plant Mol. Biol. v.18 Gilmour, S.J.;Artus, N.N.;Thomashow, M.F. https://doi.org/10.1007/BF00018452
  8. Plant Physiol. v.87 Gilmour, S.J.;Hajela, R.K.;Tomashow, M.F. https://doi.org/10.1104/pp.87.3.745
  9. Plant Physiol. v.84 Guy, C.L.;Haskell, D. https://doi.org/10.1104/pp.84.3.872
  10. Ann. Bot. v.54 Henson, I.E. https://doi.org/10.1093/oxfordjournals.aob.a086827
  11. J. Exp. Bot. v.47 Hughes, M.A.;Dunn, M.A. https://doi.org/10.1093/jxb/47.3.291
  12. Plant Cell Physiol. v.33 Kazuoka, T.;Oeda, K.
  13. Plant Mol. Biol. v.15 Kurkela, S.;Franck, M. https://doi.org/10.1007/BF00017731
  14. J. Exp. Bot. v.40 Larsson, M.;Larsson, C.M.;Whitford, P.N.;Clarkson, D.T. https://doi.org/10.1093/jxb/40.11.1265
  15. Plant Physiol. v.96 Lee, T.M.;Liao, C.K.;Lur, H.S.;Chu, C.
  16. Plant Physiol. v.94 Lin, C.;Guo, W.W.;Everson, E.;Tomashow, M.F. https://doi.org/10.1104/pp.94.3.1078
  17. Korean Biochem. J. (presently J. Biochem. Mol. Biol.) v.27 Moon, S.O.;Lim, K.L.;Cho, B.H.
  18. Plant Mol. Biol. v.21 Neven, L.G.;Haskell, D.W.;Hofig, A.;Li, Q.B.;Guy, C.L. https://doi.org/10.1007/BF00019945
  19. Cell v.12 O'Farrell, P.Z.;Goodman, H.M.;O'Farrell, P.H. https://doi.org/10.1016/0092-8674(77)90176-3
  20. J. Plant Physiol. v.126 Orr, W.;Keller, W.A.;Singh, J. https://doi.org/10.1016/S0176-1617(86)80212-7
  21. Plant Mol. Biol. v.28 Orr, W.;White, T.C.;Iu, B.;Robert, L.;Singh, J. https://doi.org/10.1007/BF00042078
  22. Plant Physiol. v.69 Siminovich, D.;Coultier, Y. https://doi.org/10.1104/pp.69.1.250
  23. Plant Cell v.2 Skriver, K.;Mundy, J. https://doi.org/10.1105/tpc.2.6.503
  24. Aust. J. Plant Physiol. v.8 Smith, M.K.;McComb, J.A. https://doi.org/10.1071/PP9810267
  25. Plant Cell v.6 Yamaguchi-Shinozaki, K.;Shinozaki, K. https://doi.org/10.1105/tpc.6.2.251