Heat Shock Proteins: Molecular Chaperones for Plant Immunity under Abiotic Stress Conditions
Akshay*
Division of Fruits and Horticultural Technology, ICAR-IARI, New Delhi, Delhi (110 012), India
Maya Lamba
Division of Fruits and Horticultural Technology, ICAR-IARI, New Delhi, Delhi (110 012), India
DOI: NIL
Keywords: Abiotic stress, Hydrogen peroxide, Thermotolerance, Ubiquitins
Abstract
Protein misfolding and aggregation can be triggered by abiotic stresses like drought, extreme temperatures, intense light and flooding. Heat shock proteins (HSPs) serve as molecular chaperones, aiding in protein stabilization, refolding unfolded proteins, preventing protein aggregation, facilitating protein transportation across cellular membranes and promoting protein removal. HSPs are categorized into different classes including HSP90, HSP70, HSP60, ubiquitins and low molecular weight HSPs. Specifically, the term "polypeptide chain binding proteins" refers to HSPs, particularly HSP90, HSP70 and HSP60. Moreover, reactive oxygen species (ROS) stimulate the production of HSPs by acting as signaling molecules. The activation of HSR genes and HSPs is facilitated by the crucial involvement of Heat Shock Factors (HSFs).
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Reference
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