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Published on May 13, 2009; 10.1104/pp.109.136697

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Received February 5, 2009
Accepted May 6, 2009

The-K segment of maize DHN1 mediates binding to anionic phospholipid vesicles and concomitant structural changes

Myong-Chul Koag , Stephan Wilkens , Raymond D. Fenton , Josh Resnik , Evanly Vo , and Timothy J. Close *

Graduate Program in Biochemistry and Molecular Biology; Department of Botany and Plant Sciences; Department of Biochemistry

* Corresponding author; email: timothy.close{at}ucr.edu.

Dehydrins (DHNs, LEA D11 family) are a family of intrinsically unstructured plant proteins that accumulate in the late stages of seed development, and in vegetative tissues subjected to water deficit, salinity, low temperature or abscisic acid (ABA) treatment. We demonstrated previously that maize (Zea mays) DHNs bind preferentially to anionic phospholipid vesicles, this binding is accompanied by an increase in {alpha}–helicity of the protein, and adoption of {alpha}–helicity can be induced by SDS. All DHNs contain at least one "K-segment", a lysine-rich 15 amino acid consensus sequence. The K-segment is predicted to form a class A2 amphipathic {alpha}–helix, a structural element known to interact with membranes and proteins. Here, three K-segment deletion proteins of maize DHN1 were produced. Lipid vesicle binding assays revealed that the K-segment is required for binding to anionic phospholipid vesicles, and adoption of {alpha}–helicity of the K-segment accounts for most of the conformational change of DHNs upon binding to anionic phospholipid vesicles or SDS. The adoption of structure may help stabilize cellular components including membranes under stress conditions.






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