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Published on January 23, 2003; 10.1104/pp.015891

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Received October 7, 2002
Returned for revision October 28, 2002
Accepted November 15, 2002

Conformation of a Group 2 Late Embryogenesis Abundant Protein from Soybean. Evidence of Poly (L-Proline)-type II Structure

Jose L. Soulages , Kangmin Kim , Estela L. Arrese , Christina Walters , and John C. Cushman *

Department of Biochemistry and Molecular Biology, 355 Noble Research Center, Oklahoma State University, Stillwater, Oklahoma 74078-0454 (J.L.S., E.L.A.); Department of Biochemistry, MS200, 311B Fleischmann Agriculture, University of Nevada, Reno, Nevada 89557-0014 (K.K., J.C.C.); and National Center for Germplasm Resources Preservation, U.S. Department of Agriculture-Agricultural Research Service, Fort Collins, Colorado 80523 (C.W.)

* Corresponding author; email: jcushman{at}unr.edu.

Late embryogenesis abundant (LEA) proteins are members of a large group of hydrophilic, glycine-rich proteins found in plants, algae, fungi, and bacteria known collectively as hydrophilins that are preferentially expressed in response to dehydration or hyperosmotic stress. Group 2 LEA (dehydrins or responsive to abscisic acid) proteins are postulated to stabilize macromolecules against damage by freezing, dehydration, ionic, or osmotic stress. However, the structural and physicochemical properties of group 2 LEA proteins that account for such functions remain unknown. We have analyzed the structural properties of a recombinant form of a soybean (Glycine max) group 2 LEA (rGmDHN1). Differential scanning calorimetry of purified rGmDHN1 demonstrated that the protein does not display a cooperative unfolding transition upon heating. Ultraviolet absorption and circular dichroism spectroscopy revealed that the protein is in a largely hydrated and unstructured conformation in solution. However, ultraviolet absorption and circular dichroism measurements collected at different temperatures showed that the protein exists in equilibrium between two extended conformational states: unordered and left-handed extended helical or poly (L-proline)-type II structures. It is estimated that 27% of the residues of rGmDHN1 adopt or poly (L-proline)-type II-like helical conformation at 12°C. The content of extended helix gradually decreases to 15% as the temperature is increased to 80°C. Studies of the conformation of the protein in solution in the presence of liposomes, trifluoroethanol, and sodium dodecyl sulfate indicated that rGmDHN1 has a very low intrinsic ability to adopt {alpha}-helical structure and to interact with phospholipid bilayers through amphipathic {alpha}-helices. The ability of the protein to remain in a highly extended conformation at low temperatures could constitute the basis of the functional role of GmDHN1 in the prevention of freezing, desiccation, ionic, or osmotic stress-related damage to macromolecular structures.




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