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A style-specific 120-kDa glycoprotein enters pollen tubes ofNicotiana alata in vivo
Authors:Jan L Lind  Ingrid Bönig  Adrienne E Clarke  Marilyn A Anderson
Institution:(1) Plant Cell Biology Research Centre, School of Botany, University of Melbourne, 3052 Parkville, Victoria, Australia;(2) Present address: Department of Biochemistry, Latrobe University, 3083 Bundoora, Victoria, Australia
Abstract:Pistils ofNicotiana alata (Link et Otto) contain an abundant, style-specific glycoprotein (120 kDa) that is rich in hydroxyproline and has both extensin-like and arabinogalactan-protein-like carbohydrate substituents. An antibody specific for the protein backbone of the glycoprotein was used to localise the glycoprotein in both unpollinated and pollinated pistils. The glycoprotein is evenly distributed in the extracellular matrix of the style transmitting tract of unpollinated pistils and, despite the presence of extensin-like carbohydrate substituents, is not associated with the walls of the transmitting tract cells. In pollinated pistils the 120-kDa glycoprotein is concentrated in the extracellular matrix adjacent to pollen tubes, and is also present in the cytoplasm and the cell walls of pollen tubes. Pollen tubes grown in vitro do not contain the 120-kDa glycoprotein unless it is added to the growth medium, suggesting that the 120kDa glycoprotein located in pistil-grown pollen tubes is derived from the extracellular matrix of the transmitting tract.
Keywords:Hydroxyproline-rich glycoprotein  Pistil  Pollen tubes  Self-incompatibility
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