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Plant Cell, Vol. 12, 1783-1794, September 2000, Copyright © 2000, American Society of Plant Physiologists

The Bacterial Elicitor Flagellin Activates Its Receptor in Tomato Cells According to the Address–Message Concept

Thomas Meindla, Thomas Bollera, and Georg Felixa
a Friedrich Miescher-Institute, P.O. Box 2543, CH-4002 Basel, Switzerland

Correspondence to: Georg Felix, Felix{at}fmi.ch (E-mail), 41-61-697-4527 (fax)

flg22, a peptide corresponding to the most conserved domain of bacterial flagellin, acts as a potent elicitor in plants. Here, we have used an iodinated derivative of flg22 (125I-labeled Tyr-flg22) as a molecular probe for the flagellin receptor in tomato cells. This radioligand showed rapid binding to a single class of specific, saturable, high-affinity receptor sites in intact cells and membrane preparations. Binding, although essentially nonreversible under physiological conditions, was not covalent, and chemical cross-linking was required to specifically label a single polypeptide of 115 kD. Intact flagellin and elicitor-active flagellin peptides but not biologically inactive analogs efficiently competed for binding of radioligand. Peptides lacking the C terminus of the conserved domain, previously found to act as competitive antagonists of elicitor action in tomato cells, also competed for binding of radioligand. Thus, this novel, high-affinity binding site exhibited all the characteristics expected of a functional receptor of bacterial flagellin. For a model of receptor activation, we propose a two-step mechanism according to the address–message concept, in which binding of the N terminus (address) is the first step and activation of responses with the C terminus (message) is the second step.




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