Proteomics applied on plant abiotic stresses: role of heat shock proteins (HSP).

The most crucial function of plant cell is to respond against stress induced for self-defence. This defence is brought about by alteration in the pattern of gene expression: qualitative and quantitative changes in proteins are the result, leading to modulation of certain metabolic and defensive pathways. Abiotic stresses usually cause protein dysfunction. They have an ability to alter the levels of a number of proteins which may be soluble or structural in nature. Nowadays, in higher plants high-throughput protein identification has been made possible along with improved protein extraction, purification protocols and the development of genomic sequence databases for peptide mass matches. Thus, recent proteome analysis performed in the vegetal Kingdom has provided new dimensions to assess the changes in protein types and their expression levels under abiotic stress. As reported in this review, specific and novel proteins, protein-protein interactions and post-translational modifications have been identified, which play a role in signal transduction, anti-oxidative defence, anti-freezing, heat shock, metal binding etc. However, beside specific proteins production, plants respond to various stresses in a similar manner by producing heat shock proteins (HSPs), indicating a similarity in the plant's adaptive mechanisms; in plants, more than in animals, HSPs protect cells against many stresses. A relationship between ROS and HSP also seems to exist, corroborating the hypothesis that during the course of evolution, plants were able to achieve a high degree of control over ROS toxicity and are now using ROS as signalling molecules to induce HSPs.