Abstract
The effect of heat stress on soluble proteins extracted from leaf tissues of bread (Triticum aestivum cv. Gonen-98, tolerant; cv. Cumhuriyet-75, susceptible; genome ABD) and durum (Triticum durum cv. Ege-88, tolerant; cv. Ankara-98, susceptible; genome AB) wheat cultivars differing in sensitivity to high temperature was examined by two-dimensional gel electrophoresis. At acclimation (37°C) and acclimation→high temperature (37°C→50°C) treatments compared to control (25°C), evaluation of gels revealed 31 proteins to be differentially expressed in first leaves as a result of heat stress in heat-susceptible and heat-tolerant cultivars of bread and durum wheats. All of the increased or decreased proteins in amount, newly synthesized and/or disappeared were in low-molecular-weight (LMW, 16.1–24.0 kDa) and generally acidic character (pI 4.8–6.9). The responses of the four cultivars were compared: Twenty-two of 31 proteins were detected as newly synthesized LMW heat shock proteins (LMW HSPs = small HSPs). The number of these sHSPs was different in cultivars which have the same genome. In addition, the number of the sHSPs in heat-tolerant cultivars was higher than in heat-susceptible cultivars. Some of the sHSPs were specific to cultivar. Most of the sHSPs synthesized at 37°C were also detected at 37°C→50°C treatment. It is suggested that sHSPs have special importance in two points: Firstly, sHSPs in cultivars showed abundance and diversity. Secondly, these proteins may play an important role in the acquiring of thermal tolerance.
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