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Titolo:
The bacterial elicitor flagellin activates its receptor in tomato cells according to the address-message concept
Autore:
Meindl, T; Boller, T; Felix, G;
Indirizzi:
Friedrich Miescher Inst, CH-4002 Basel, Switzerland Friedrich Miescher Inst Basel Switzerland CH-4002 002 Basel, Switzerland
Titolo Testata:
PLANT CELL
fascicolo: 9, volume: 12, anno: 2000,
pagine: 1783 - 1794
SICI:
1040-4651(200009)12:9<1783:TBEFAI>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
HIGH-AFFINITY BINDING; GLUCOSIDE PHYTOALEXIN ELICITOR; MOLECULAR MECHANISM; SIGNAL PERCEPTION; MEMBRANES; PROTEIN; PLANTS; IDENTIFICATION; SUPPRESSORS; RESPONSES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Felix, G Friedrich Miescher Inst, POB 2543, CH-4002 Basel, Switzerland Friedrich Miescher Inst POB 2543 Basel Switzerland CH-4002 rland
Citazione:
T. Meindl et al., "The bacterial elicitor flagellin activates its receptor in tomato cells according to the address-message concept", PL CELL, 12(9), 2000, pp. 1783-1794

Abstract

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 (I-125-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 115kD. 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 ofthe N terminus (address) is the first step and activation of responses with the C terminus (message) is the second step.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 16/07/20 alle ore 19:41:42