Characterization and partial purification of an oligopeptide elicitor receptor from parsley (Petroselinum crispum)

FEBS Letters

Nürnberger, Thorsten¹  Nennstiel, Dirk¹  Scheel, Dierk¹ 

[1] Institut für Pflanzenbiochemie, Abteilung Stress- und Entwicklungsbiologie, Weinberg 3, D-06120 Halle/Saale, Germany

关键词: Ligand affinity chromatography;    Phytoalexin;    Phytophthora sojae;    Signal transduction;   

DOI  :  10.1016/S0014-5793(98)00800-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown