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The cationic nature of lysine-rich segments modulates the structural and biochemical properties of wild potato FSK3 dehydrin by Bartosz M. Szabała is a Agricultural and Biological Sciences article available to read on EtoBox.

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Dehydrins are hydrophilic stress-induced proteins that are thought to protect cellular machinery from the adverse effect of dehydration caused by low temperature, drought, or salinity. In the previous study, acidic FSK3 dehydrin DHN24 from Solanum sogarandinum was found to accumulate at multiple sites in phloem cells in response to cold treatment. This study investigated the biochemical and structural properties of recombinant DHN24. It was shown that the overexpression of DHN24 in Escherichia coli led to the inhibition of bacterial growth. The purified DHN24 was found to protect lactate dehydrogenase from freeze-induced denaturation. Circular dichroism (CD) analysis showed that DHN24 was disordered in aqueous solutions, but adopted α-helical conformation in a membrane-mimetic environment using sodium dodecyl sulfate micelles. DHN24 also interacted with anionic phosphatidic acid (PA). DHN24 contains four lysine-rich regions including three K-segments and a region upstream of the S-segment. The role of their local cationic nature is unknown. These segments are predicted to form helical structures. The CD analysis of mutant proteins in the membrane-mimetic environment matched these p

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Author

Bartosz M. Szabała

Publisher

Elsevier BV

Published

2023

Language

EN

Field

Agricultural and Biological Sciences (Life Sciences)