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Background:
To protect them from water stress induced-ROS- mediated protein
unfolding and aggregation, plants are equipped with a wide range of
antioxidant redox molecular chaperonic proteins like Protein disulphide
Isomerase (PDI) (E.C.5.3.4.1). These are a diverse group of proteins
that in vivo bind to misfolded or unfolded proteins and play an
important role to form specific three dimensional conformation of the
functional proteins. In addition, stress conditions induce altered and
intensified PDI expression in plant cell, thereby highlighting the role
of these proteins under abiotic stress conditions.
The context and purpose of the study;
The main objective of the study was to determine drought stress-
induced changes in the modulation of the boiling soluble protein
disulphide isomerase (BsPDI) in response to drought at two different
developmental stages {38 Days Post Anthesis (DPA) and 52 DPA} in
Triticum aestivum.
Results, the main findings; A
temporal regulation of BsPDI accumulation in a cultivar dependent
manner was observed under control and drought stress. SDS-PAGE and
Western blot analysis revealed strong induction of BsPDI17 under
drought conditions only in the tolerant cv. PBW 527 at 38 DPA. Contrary
to this, unchanged BsPDI17 accumulation was detected in the sensitive
cv. PBW 343 at 38 DPA under drought. However, at 52 DPA, there was a
marked decline in BsPDI17 accumulation in the sensitive cv. PBW 621
under stress conditions.
Conclusions, brief summary and potential implications:
Based upon our results, significance of BsPDI in the wheat cultivars
differing in drought resistance during stress conditions is
discussed.
