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Plant Physiol, January 2003, Vol. 131, pp. 309-316

The binding of Maize DHN1 to Lipid Vesicles. Gain of Structure and Lipid Specificity1

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

Graduate Program in Biochemistry and Molecular Biology (M.-C.K., S.W., T.J.C.) and Departments of Botany and Plant Sciences (M.-C.K., R.D.F., T.J.C.) and Biochemistry (S.W.), University of California, Riverside, California 92521-0124

Dehydrins (DHNs; late embryogenesis abundant D-11) are a family of plant proteins induced in response to abiotic stresses such as drought, low temperature, and salinity or during the late stages of embryogenesis. Spectral and thermal properties of these proteins in purified form suggest that they are "intrinsically unstructured." However, DHNs contain at least one copy of a consensus 15-amino acid sequence, the "K segment," which resembles a class A2 amphipathic alpha -helical, lipid-binding domain found in other proteins such as apolipoproteins and alpha -synuclein. The presence of the K segment raises the question of whether DHNs bind lipids, bilayers, or phospholipid vesicles. Here, we show that maize (Zea mays) DHN DHN1 can bind to lipid vesicles that contain acidic phospholipids. We also observe that DHN1 binds more favorably to vesicles of smaller diameter than to larger vesicles, and that the association of DHN1 with vesicles results in an apparent increase of alpha -helicity of the protein. Therefore, DHNs, and presumably somewhat similar plant stress proteins in the late embryogenesis abundant and cold-regulated classes may undergo function-related conformational changes at the water/membrane interface, perhaps related to the stabilization of vesicles or other endomembrane structures under stress conditions.


1 This work was supported by the National Science Foundation (grant no. IBN 92-05269), by the University of California (Biotechnology Research and Education grant no. 97-15), and by the California Agricultural Experiment Station Funds (Hatch grant no. 5306-H).

* Corresponding author; e-mail timothy.close{at}ucr.edu; fax 909-787-4437.

© 2003 American Society of Plant Biologists



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