PAID ACCESS | Published on : 13-Mar-2025 | Pages: 46-55 | Doi : 10.37446/edibook242025/46-55
Molecular chaperones, including heat shock proteins (HSPs), chaperonins, and co-chaperones are essential for maintaining cellular integrity under abiotic stress conditions such as heat, drought, salinity and oxidative stress. These proteins play a critical role in protein folding, stabilization and degradation, thereby protecting cells from the damaging effects of misfolded proteins and contributing to cellular resilience. Heat shock factors (HSFs), key regulators of the heat shock response, activate the transcription of HSPs by binding to heat shock elements (HSEs) in gene promoters. This activation helps cells adapt to and survive stress conditions by ensuring protein homeostasis. In addition to their cellular functions, molecular chaperones and HSFs have significant applications in agriculture, biotechnology, and medicine. Genetic manipulation of HSFs has shown the potential to improve stress tolerance in crops and microorganisms, offering a valuable tool for developing resilient crop varieties. HSFs are also critical in stress-responsive breeding programs aimed at improving crop resilience under changing climatic conditions. Ongoing research into the molecular mechanisms governing chaperone function and HSF activation promises to enhance stress tolerance and provide solutions for environmental, medical, and industrial challenges.
Molecular Chaperones, Chaperonins, Co-chaperones, Abiotic Stress, Oxidative Stress, Protein, Heat shock Proteins, Heat Shock Factors, Stabilization, Resilience
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