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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 381, Issue 8

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The Hepta-? -Glucoside Elicitor-Binding Proteins from Legumes Represent a Putative Receptor Family

A. Mithöfer / J. Fliegmann / G. Neuhaus-Url / H. Schwarz / J. Ebel
Published Online: 2005-07-05 | DOI: https://doi.org/10.1515/BC.2000.091

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 (K d = 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 (K d = 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.

About the article

Published Online: 2005-07-05

Published in Print: 2000-08-06


Citation Information: Biological Chemistry, Volume 381, Issue 8, Pages 705–713, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2000.091.

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