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Small heat shock proteins in plants: Structure, function and role in stress adaptation
Santanu Mondal1, Md Azaharuddin1, Rakhi Dasgupta1
1Department of Biochemistry and Biophysics, University of Kalyani, Kalyani, 741235, West Bengal, India.
Biochimie
|April 12, 2026
Summary
Small heat shock proteins (sHSPs) are crucial for plant stress tolerance. This review explores their diverse classification, structure, and function, aiding in developing climate-resilient crops.
Area of Science:
- Plant biology
- Molecular chaperones
- Stress physiology
Background:
- Small heat shock proteins (sHSPs) are ATP-independent molecular chaperones vital for protein stability in plants.
- They possess a conserved α-crystallin domain and form flexible oligomers that bind misfolded proteins, preventing aggregation.
Purpose of the Study:
- To review the tissue and organelle-specific classification of plant sHSPs across lineages.
- To examine their structural diversification and functional implications.
- To explore interactions within the heat shock response (HSR) pathway.
Main Methods:
- Literature review of plant sHSP research.
- Analysis of structural features and subcellular localization.
- Investigation of sHSP roles in stress tolerance and development.
Main Results:
- Plant sHSPs are classified into families with specific subcellular targeting (cytosol, chloroplasts, mitochondria, ER, peroxisomes).
- sHSPs confer tolerance to various abiotic stresses (heat, drought, salinity, oxidative, heavy metals) and aid development (seed maturation, fruit ripening).
- Structural variations, especially in terminal regions, influence client protein interactions.
Conclusions:
- Understanding sHSP diversity and function is key to improving plant stress resilience.
- Further research on sHSP structure-oligomerization, and substrate binding mechanisms is needed.
- This knowledge can contribute to developing climate-resilient crops.
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