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Plant Cell, Vol. 11, 251-262, February 1999, Copyright © 1999, American Society of Plant Physiologists
Pollen–Stigma Adhesion in Brassica spp Involves SLG and SLR1 Glycoproteins
Doan-Trung Luua,
Danièle Marty-Mazarsb,
Martin Trickc,
Christian Dumasa, and
Philippe Heizmanna
a Reproduction et Développement des Plantes, Unité Mixte de Recherche du Centre National de la Recherche Scientifique, Institut National de la Recherche Agronomique, Ecole Normale Supérieure de Lyon, 46 allée d'Italie, F-69364 Lyon Cedex 07, France
b Laboratoire de Phyto-Biologie Cellulaire, Unité Propre de Recherche de l'Enseignement Supérieur No. 469, Faculté des Sciences—Mirande, BP 400—Université de Bourgogne, 9 avenue Alain Savary, F-21011 Dijon Cédex, France
c Department of Brassica and Oilseeds Research, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom
Correspondence to:
Philippe Heizmann, Philippe.Heizmann{at}ens-lyon.fr (E-mail), 33-4-72-72-86-00 (fax)
The adhesion of pollen grains to the stigma is the first step of pollination in flowering plants. During this step, stigmas discriminate between pollen grains that can and cannot be permitted to effect fertilization. This selection is operated by various constituents of the cell walls of both partners. Several genes structurally related to the self-incompatibility system that prevents self-pollination in Brassica spp are known to target their products into the stigma cell wall. We proposed previously that one of these genes, the one encoding the S locus glycoprotein (SLG)–like receptor 1 (SLR1), which is coexpressed with that encoding SLG, may participate in pollen–stigma adhesion. Here, we exploit a biomechanical assay to measure the pollen adhesion force and show that it is reduced both by transgenic suppression of SLR1 expression and by pretreatment of wild-type stigmas with anti-SLR1 antibodies, anti-SLG antibodies, or pollen coat-protein extracts. Our results indicate a common adhesive function for the SLR1 and SLG proteins in the pollination process.
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