한국작물학회지 (KOREAN JOURNAL OF CROP SCIENCE)

  • 제48권5호
  • /
  • Pages.407-412
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  • 2003
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  • 0252-9777(pISSN)
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  • 2287-8432(eISSN)
한국작물학회 (The Korean Society of Crop Science)
권호 표지

Immunological Assays of Freezing Tolerance in Barley using Antifreeze Proteins Antisera

  • Sung, Ha-Chang (School of Bioresources Science, Dankook University) ;
  • Kim, Dae-In (School of Bioresources Science, Dankook University) ;
  • Hwang, Cheol-Ho (School of Bioresources Science, Dankook University)
  • 발행 : 2003.12.01
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초록

In order to measure an antifreezing tolerance, antifreeze proteins accumulated upon cold acclimation in apoplast were analyzed. As Dongborilho were cold-acclimated for 3 to 74 days there was an abrupt increase in apoplastic proteins up to 30 days and then decrease to the similar levels. Among the known antifreeze proteins, CLP produced in E. coli. and TLP purified from apoplast were used to generate antisera that allow to measure and localize the proteins in leaves of barley. The CLP of 27.7 kDa and TLPs of 6, 26, 27, 30, and 31 kDa were increased in their amounts in apoplast as cold treatment being longer. There was a correlation among the amounts of those proteins accumulated in apoplast and freezing tolerance as shown in field and ion leakage tests for five cultivars. The deposit of CLP was localized in the marginal area and the area adjacent to leaf vescular bundle cells in an increasing manner according to duration of cold acclimation but no variation was observed in terms of it's distribution. Based on the close correlation between levels of antifreeze proteins and degrees of freezing tolerance, the immunological methods was to develop to estimate a freezing tolerance in barley.

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참고문헌

  1. Cho, J.H, Park, M.W., Bae, and S.H. 1979. A new high yield early mature freeze tolerant barley cultivars, "Dongborilho", "Dongbori2ho". The research Reports of RDA 21(Crop) : 51-56
  2. Chun, J.U. and Griffith, M. 1998. Variation of the antifreeze proteins during cold acclimation among winter cereals and their relationship with freezing resistance. Kor. J. Crop Sci. 43(3) : 172-178
  3. Griffith, M., Ala, P.,Yang, D. S. C.. Hon, W. C, and Moffatt B. A. 1992. Antifreeze protein produced endogenously in winter rye leaves. Plant Physiol. 100 : 593-596 https://doi.org/10.1104/pp.100.2.593
  4. Griffith, M., Marentes, E., Miynarz, A., and Bruth, R. A. 1993. Protein accumulate in the apoplast of winter rye leaves during cold acclimation. Physiologia Plantarum. 87 : 499-507 https://doi.org/10.1111/j.1399-3054.1993.tb02499.x
  5. Griffith, M., Hon, W. C., Chong, P., and Yang, D. S. C. 1994. Extraction and isolation of antifreeze proteins from winter rye(Secale cereale L.) leave. Plant Physiol. 104: 971-980 https://doi.org/10.1104/pp.104.3.971
  6. Griffith, M., Hon, W. C, MIynarz, A., Kwok, Y. C, and Yang, D. S. C. 1995. Antifreeze proteins in winter rye are similar to pathogenesis-related protein. Plant Physiol. 109 : 879-889 https://doi.org/10.1104/pp.109.3.879
  7. Griffith, M. and Yu, X. M. 1999. Antifreeze proteins in winter rye leaves from oligomeric complexes. Plant Physiol. 119: 1361-1369 https://doi.org/10.1104/pp.119.4.1361
  8. Gurpreet Kalsi. and Marilynn E. Etzler. 2000. Localization of a Nod Factor-Binding Protein in Legume Roots and Factors Influencing Its Distribution and ExpressionI$^{1}$. Plant Physiol. 124: 1039-1048 https://doi.org/10.1104/pp.124.3.1039
  9. Guy, C. L., Hummer, R. L., and Haskell, D. 1987. Induction of freezing tolerance in spinach during cold acclimation. Plant Physiol. 84: 868-871 https://doi.org/10.1104/pp.84.3.868
  10. Hon, W. C, Griffith, M., Chong, P., and Yang, D. C. S. 1994. Extraction and isolation of antifreeze proteins from winter ryeleaves. Plant Physiol. 104: 971-980 https://doi.org/10.1104/pp.104.3.971
  11. Hwang, C. H. 1995. Analysis of the proteins accumulated during cold treatment in intercellular space of barley. Kor. J. Plant Tissue Culture. 22 : 25-28
  12. Hwang, C. H. 1999. Molecular analysis of freeze-tolerance enhanced by treatment of trinexapac-ethyl in Kentucky bluegrass. Kor.J. Crop Sci. 44(2) : 176-179
  13. Hwang, C. H., Park, H. W., Hwang, E. Y., Lui, J. R., and Min, S. R. 2000. Freeze tolerance enhanced by antifreeze protein in plant. Kor. J. Tissue Culture. 27(4) : 339-343
  14. Maria J. P.,Tsuyoshi K., Yvan L., Naoshi D., and Yuji K. 1998. SAdenosyl-L-Methionine:L-Methionine S-Methyltransferase from Germinating Barley1. Plant Physiol. 118 : 431-438 https://doi.org/10.1104/pp.118.2.431
  15. Mervi, A., Griffith, M., Hon, W. C., Zhang, J., Yang, S. C. and Kaarina, P. M. 1996. Immunolocalization antifreeze protein in winter rye leaves, crowns, and roots by tissue printing. Plant Physiol. 110 : 845-857 https://doi.org/10.1104/pp.110.3.845
  16. Pearce, R. S. and Ashworth, E. N. 1992. Cell shape and localization of ice in leaves of overwintering wheat during frost stress in the field. Planta. 188: 324-331
  17. Sule, R. M., Kenneth, A. 1991. Leakage of intracellular substances as an indicater of freezing injury in alfalfa. Crop Sci. 31 : 430-435 https://doi.org/10.2135/cropsci1991.0011183X003100020041x
  18. Walther-Larsen, H., Brandt, J., Collinge, D. B., and Thordal-Christensen, H. 1993. A pathogen-induced gene of barley encodes a HSP90 homologue showing striking similarity to vertebrate forms resident in the endoplasmic reticulum. Plant Mol Biol. 21(6) : 1097-108 https://doi.org/10.1007/BF00023606
  19. Thomashow, M. F. 1998. Role of cold-responsive genes in plant freezing tolerance. Plant Physiol. 118: 1-7. https://doi.org/10.1104/pp.119.1.1