A SPECIFIC, HIGH-AFFINITY BINDING-SITE FOR THE HEPTA-BETA-GLUCOSIDE ELICITOR EXISTS IN SOYBEAN MEMBRANES

被引:173
作者
CHEONG, JJ
HAHN, MG
机构
[1] UNIV GEORGIA,COMPLEX CARBOHYDRATE RES CTR,200 RIVERBEND RD,ATHENS,GA 30602
[2] UNIV GEORGIA,DEPT BIOCHEM,ATHENS,GA 30602
[3] UNIV GEORGIA,DEPT BOT,ATHENS,GA 30602
关键词
D O I
10.1105/tpc.3.2.137
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 I-125. 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 K(d) = 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.
引用
收藏
页码:137 / 147
页数:11
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