Structural characterization of HSP101 genes and of their promoter in durum wheat

In agriculture, heat stress is one of the most important constraints on crop yield. Many efforts have been made to understand the molecular and physiological mechanisms involved in the thermotolerance process in order to find new traits to use in breeding programs. Heat shock proteins, mainly chaperones or proteases, play the essential role of preventing or minimizing the deleterious effects of heat at the cellular and molecular levels. Clear evidence of the protective role of HSP101 and its involvement in thermotolerance was previously demonstrated in yeast and Arabidopsis. In many plant species many cDNA sequences have been isolated suggesting that HSP101 is a member of a small gene family strongly induced by heat. So far in durum wheat two isoforms of HSP101(TdHSP101-B and C) with two forms for each genome, have been isolated and characterized at cDNA level (Gulli et al 2007). The oncoming rising of the temperature worldwide claimed for new traits to introduce in breeding programs therefore the complete coding sequence of candidate genes for heat resilience is necessary for functional genetics studies. In the present work the isolation and the structural characterization of the complete coding sequence and of the promoter region of TdHSP101-B and C isoforms will be presented.