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The roles of residue position and charge in the cryoprotective behaviour of the Vitis riparia K2 and YSK2 dehydrins

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Title: The roles of residue position and charge in the cryoprotective behaviour of the Vitis riparia K2 and YSK2 dehydrins
Author: Palmer, Sharall
Department: Department of Molecular and Cellular Biology
Program: Molecular and Cellular Biology
Advisor: Graether, Steffen
Abstract: Dehydrins are group II Late Embryogenesis Abundant proteins that accumulate in plants during seed development and in response to abiotic stresses. The biological function of dehydrins remain elusive, as they are multi-functional in vitro. The contribution of sequence and charge to the cryoprotective behaviour of dehydrins was analyzed using synthetic variants of the Vitis riparia YSK2 and K2 proteins: ScYSK2, a scrambled version of YSK2; and AntiK2, a charge-reversed version of K2. Circular dichroism (CD) spectroscopy analysis revealed that dehydrin-induced changes in the structure of YFH1 was dependent on sequence and independent of residue charge. An LDH cryoprotection assay showed that the efficiency of YSK2 was unrelated to its sequence, whereas the efficiency of K2 depended on its residue charge type. CD spectroscopy analysis also suggested that the mechanism of protein stabilization by dehydrins may be more like glycerol than polyethylene glycol. Identifying functionally important residues in dehydrins would provide insight into the potential mechanism(s) of their protective behaviour.
URI: http://hdl.handle.net/10214/11598
Date: 2017-09


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