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THE PLANT CELL, Vol 3, Issue 2 137-147, Copyright © 1991 by American Society of Plant Biologists

RESEARCH ARTICLES

A Specific, High-Affinity Binding Site for the Hepta-[beta]-glucoside Elicitor Exists in Soybean Membranes

J. J. Cheong and M. G. Hahn
Complex Carbohydrate Research Center and Departments of Biochemistry and Botany, University of Georgia, 220 Riverbend Road, Athens, Georgia 30602

The presence of a specific binding site for a hepta-[beta]-glucoside elicitor of phytoalexin accumulation has been demonstrated in soybean microsomal membranes. A tyramine conjugate of the elicitor-active hepta-[beta]-glucoside was prepared and radiolabeled with 125l. The labeled hepta-[beta]-glucoside-tyramine conjugate was used as a ligand in binding assays with a total membrane fraction prepared from soybean roots. Binding of the radiolabeled hepta-[beta]-glucoside elicitor was saturable, reversible, and with an affinity (apparent Kd= 7.5 x 10-10 M) comparable with the concentration of hepta-[beta]-glucoside required for biological activity. A single class of hepta-[beta]-glucoside binding sites was found. The binding site was inactivated by proteolysis and by heat treatment, suggesting that the binding site is a protein or glycoprotein. Competitive inhibition of binding of the radiolabeled hepta-[beta]-glucoside elicitor by a number of structurally related oligoglucosides demonstrated a direct correlation between the binding affinities and the elicitor activities of these oligoglucosides. Thus, the hepta-[beta]-glucoside-binding protein fulfills criteria expected of a bona fide receptor for the elicitor-active oligosaccharin.


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Copyright © 1991 by the American Society of Plant Biologists