Effect of an Intrinsically Disordered Plant Stress Protein on the Properties of Water
Document Type
Article
Publication Date
2018
Digital Object Identifier (DOI)
https://doi.org/10.1016/j.bpj.2018.09.014
Abstract
Dehydrins are plant proteins that are able to protect plants from various forms of dehydrative stress such as drought, cold, and high salinity. Dehydrins can prevent enzymes from losing activity after freeze/thaw treatments. Previous studies had suggested that the dehydrins function by a molecular shield effect, essentially preventing a denatured enzyme from aggregating with another enzyme. Therefore, the larger the dehydrin, the larger the shield and theoretically the more effective the protection. Although this relationship holds for smaller dehydrins, it fails to explain why larger dehydrins are less efficient than would be predicted from their size. Using solvatochromic dyes to probe the solvent features of water, we first confirm that the dehydrins do not bind the dyes, which would interfere with interpretation of the data. We then show that the dehydrins have an effect on three solvent properties of water (dipolarity/polarizability, hydrogen-bond donor acidity and hydrogen-bond acceptor basicity), which can contribute to the protective mechanism of these proteins. Interpretation of these data suggests that although polyethylene glycol and dehydrins have similar protective effects, dehydrins may more efficiently modify the hydrogen-bonding ability of bulk water to prevent enzyme denaturation. This possibly explains why dehydrins recover slightly more enzyme activity than polyethylene glycol.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Biophysical Journal, v. 115, issue 9, p. 1696-1706
Scholar Commons Citation
Ferreira, Luisa A.; Walczyk Mooradally, Alicyia; Zaslavsky, Boris; Uversky, Vladimir N.; and Graether, Steffen P., "Effect of an Intrinsically Disordered Plant Stress Protein on the Properties of Water" (2018). Molecular Medicine Faculty Publications. 254.
https://digitalcommons.usf.edu/mme_facpub/254
