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HSP70 Mediated Stress Modulation in Plants

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Heat Shock Proteins and Stress

Part of the book series: Heat Shock Proteins ((HESP,volume 15))

Abstract

Stresses induced by abiotic and biotic factors badly effect sessile natured plants. Several innate mechanism has been established by plants during evolution. Expression of specialized proteins under harsh conditions to mitigate the effects is one of the conserved mechanisms. Heat shock proteins (hsp) are one of those conserved proteins. Among HSP, Hsp70 holds critical role in stress tolerance as well as development. HSP70 are structurally conserved across the genomes and reported to mitigate stress at cellular level. At the onset of stress, HSP70 releases HSF to translocate and transcribe HSP resulting in increased tolerance. While, abundant HSP70 bind to HSF to down-regulate the expression of HSP. Hsp70 associated with mitochondria and endoplasmic reticulum respond to accumulation of unfolded proteins (unfolded protein response) and repair them. Moreover, they are also associated to control programmed cell death in plants by interacting with BAG proteins.

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Acknowledgements

The authors would like to thank Dr. M Ishaq A Rehmani (Ghazi University, D.G. Khan, Pakistan) for useful discussion.

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Rana, R.M., Iqbal, A., Wattoo, F.M., Khan, M.A., Zhang, H. (2018). HSP70 Mediated Stress Modulation in Plants. In: Asea, A., Kaur, P. (eds) Heat Shock Proteins and Stress. Heat Shock Proteins, vol 15. Springer, Cham. https://doi.org/10.1007/978-3-319-90725-3_13

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