Characterization and partial purification of an oligopeptide elicitor receptor from parsley (Petroselinum crispum).
Parsley cells recognize the fungal phytopathogen Phytophthora sojae through a plasma membrane receptor. A 13 amino acid oligopeptide fragment (Pep-13) of a 42 kDa fungal cell wall glycoprotein was shown to bind to the receptor and stimulate a complex defense response in cultured parsley cells. The Pep-13 binding site solubilized from parsley microsomal membranes by non-ionic detergents exhibited the same ligand affinity and ligand specificity as the membrane-bound receptor. Chemical crosslinking and photoaffinity labeling assays with [125I]Pep-13 revealed that a monomeric 100 kDa integral plasma membrane protein is sufficient for ligand binding and may thus constitute the ligand binding domain of the receptor. Ligand affinity chromatography of solubilized microsomal membrane protein on immobilized Pep-13 yielded a 5000-fold enrichment of specific receptor activity.
Institut für Pflanzenbiochemie, Abteilung Stress- und Entwicklungsbiologie, Halle/Saale, Germany.
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D019661:Apiaceae / Q000737:chemistry*; D002846:Chromatography, Affinity; D005656:Fungal Proteins / Q000737:chemistry* / Q000302:isolation & purification; D008562:Membrane Glycoproteins / Q000737:chemistry* / Q000302:isolation & purification
D005656:Fungal Proteins; D008562:Membrane Glycoproteins; C091510:elicitor protein, Phytophthora megasperma