A proteomic analysis to identify cold acclimation associated proteins in wild wheat (Triticum urartu L.)

  • Gharechahi J
  • Alizadeh H
  • Naghavi M
 et al. 
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To gain a better understanding of cold acclimation process in wheat, we applied a 2-DE based proteomic approach to discover changes in proteome profile of a diploid wild wheat (Triticum urartu L.) during prolonged cold stress treatment. To this end, plants were grown in pots and the growing seedlings (4-leaf stage) were exposed to cold stress. After 4 weeks of cold acclimation (4-6 °C) and subsequent treatment for 12 h at -2 °C, samples were collected from control and stressed plants and were subjected to proteome pattern analysis. Among approximately 450 reproducible protein spots displayed in each given 2-DE gels, 34 proteins changed significantly in abundance in response to cold stress. Among them, 25 and 9 proteins were up and down-regulated under stress condition, respectively. Analysis by matrix-assisted laser desorption ionization time of flight/time of flight mass spectrometry coupled with non-redundant protein database search allowed the identification of 20 cold-induced proteins. Integrated proteomic and database survey resulted in identification of several cold stress related proteins such as pathogenesis related protein, cold regulated protein, cold-responsive LEA/RAB-related COR protein, oxygen-evolving enhancer protein and oxalate oxidase. The presumed functions of the identified proteins were mostly related to cold acclimation, oxidative stress and photosynthesis. The possible implications of differentially accumulated proteins in acquiring systemic tolerance to freezing stress following exposure to prolonged low temperature will be discussed.

Author-supplied keywords

  • Cold acclimation
  • Low temperature
  • Mass spectrometry
  • Proteomics
  • Triticum urartu
  • Two-dimensional gel electrophoresis (2-DE)

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  • Javad Gharechahi

  • Houshang Alizadeh

  • Mohammad Reza Naghavi

  • Golandam Sharifi

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