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Characterization of the binding of α- l-Fuc (1→2)-β- d-Gal (1→), a xyloglucan signal, in blackberry protoplasts

Previous work showed that the fucose→galactose moiety of the xyloglucan nonasaccharide XXFG is responsable for its biological activity. We used this side chain of XXFG (α- l-Fuc (1→2)-β- d-Gal (1→)) in ligand-binding experiments to demonstrate its role as a signal molecule in plant cells. Proteins s...

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Bibliographic Details
Published in:Plant science (Limerick) 2000-02, Vol.151 (2), p.183-192
Main Authors: Dunand, Christophe, Gautier, Catherine, Chambat, Gérard, Liénart, Yvette
Format: Article
Language:English
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Summary:Previous work showed that the fucose→galactose moiety of the xyloglucan nonasaccharide XXFG is responsable for its biological activity. We used this side chain of XXFG (α- l-Fuc (1→2)-β- d-Gal (1→)) in ligand-binding experiments to demonstrate its role as a signal molecule in plant cells. Proteins solubilized from plasma membrane enriched fractions isolated from Rubus fruticosus protoplasts were tested for their ability to bind the side chain of XXFG, using a digoxigenin- or biotin-conjugated neoglycoprotein specific for 2′-fucosyl-lactose in blots and k-ELISA tests. A putative receptor for the signaling sugar was identified, and the ligand specificity is reported. The role of structural elements important for biological activities was investigated using compounds structurally related to xyloglucan, and a variety of phytohormones such as 2,4-D.
ISSN:0168-9452
1873-2259
DOI:10.1016/S0168-9452(99)00217-4