The Hepta-? -Glucoside Elicitor-Binding Proteins from Legumes Represent a Putative Receptor Family
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A. Mithöfer
Abstract
The ability of legumes to recognize and respond to β-glucan elicitors by synthesizing phytoalexins is consistent with the existence of a membrane-bound β-glucan-binding site. Related proteins of approximately 75 kDa and the corresponding mRNAs were detected in various species of legumes which respond to β-glucans. The cDNAs for the β-glucan-binding proteins of bean and soybean were cloned. The deduced 75-kDa proteins are predominantly hydrophilic and constitute a unique class of glucan-binding proteins with no currently recognizable functional domains. Heterologous expression of the soybean β-glucan-binding protein in tomato cells resulted in the generation of a high-affinity binding site for the elicitor-active hepta-β-glucoside conjugate (Kd = 4.5nM). Ligand competition experiments with the recombinant binding sites demonstrated similar ligand specificities when compared with soybean. In both soybean and transgenic tomato, membrane-bound, active forms of the glucan-binding proteins coexist with immunologically detectable, soluble but inactive forms of the proteins. Reconstitution of a soluble protein fraction into lipid vesicles regained β-glucoside-binding activity but with lower affinity (Kd = 130 nM). We conclude that the β-glucan elicitor receptors of legumes are composed of the 75 kDa glucan-binding proteins as the critical components for ligand-recognition, and of an as yet unknown membrane anchor constituting the plasma membrane-associated receptor complex.
Copyright © 2000 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
- To Our Authors, Readers and Subscribers
- Highlight: Plant Biological Chemistry
- The Structural Properties of Plant Peroxisomes and Their Metabolic Significance
- Active Oxygen Species as Mediators of Plant Immunity: Three Case Studies
- Post-Transcriptional Regulation of Phenylalanine Ammonia-Lyase Expression in Tobacco Following Recovery from Gene Silencing
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- IAA-Synthase, an Enzyme Complex from Arabidopsis thaliana Catalyzing the Formation of Indole-3-Acetic Acid from (S)-Tryptophan
- Topology Studies of the Chloroplast Protein Import Channel Toc75
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- Metabolic Activity Decreases as an Adaptive Response to Low Internal Oxygen in Growing Potato Tubers
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