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Titolo:
Sensitivity of different ecotypes and mutants of Arabidopsis thaliana toward the bacterial elicitor flagellin correlates with the presence of receptor-binding sites
Autore:
Bauer, Z; Gomez-Gomez, L; Boller, T; Felix, G;
Indirizzi:
Friedrich Miescher Inst, CH-4002 Basel, Switzerland Friedrich Miescher Inst Basel Switzerland CH-4002 002 Basel, Switzerland
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 49, volume: 276, anno: 2001,
pagine: 45669 - 45676
SICI:
0021-9258(200112)276:49<45669:SODEAM>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
HIGH-AFFINITY BINDING; PLANT-DISEASE RESISTANCE; PLASMA-MEMBRANES; SYRINGOLIDE ELICITORS; CLADOSPORIUM-FULVUM; TOBACCO CELLS; TOMATO CELLS; PROTEIN; KINASE; GENE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
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:
Z. Bauer et al., "Sensitivity of different ecotypes and mutants of Arabidopsis thaliana toward the bacterial elicitor flagellin correlates with the presence of receptor-binding sites", J BIOL CHEM, 276(49), 2001, pp. 45669-45676

Abstract

Flagellin, the main building block of the bacterial flagellum, acts as potent elicitor of defense responses in different plant species. Genetic analysis in Arabidopsis thaliana identified two distinct loci, termed FLS1 and FLS2, that are essential for perception of flagellin-derived elicitors. FLS2was found to encode a leucine-rich repeat transmembrane receptor-like kinase with similarities to Toll-like receptors involved in the innate immune system of mammals and insects. Here we used a radiolabeled derivative of flg22, a synthetic peptide representing the elicitor-active domain of flagellin, to probe the interaction of flagellin with its receptor in A. thaliana The high affinity binding site detected in in- tact cells and membrane preparations exhibited specificity for flagellin-derived peptides with biological activity as agonists or antagonists of the elicitor responses. Specific binding activity was measurable in all ecotypes of A. thaliana that show sensitivity to flagellin but was barely detectable in the flagellin-insensitive ecotype Ws-O affected in FLS1. A strongly impaired binding of flagellin was observed also in several independent flagellin-insensitive mutants isolated from the flagellin-sensitive ecotype La-er. In particular, no binding was found in plants carrying a mutation in the LRR domain of FLS2. These data indicate that the formation of functional receptor-binding sites depends on genes encoded by both loci, FLS1 and FLS2. The tight correlation betweenthe presence of the binding site and elicitor response provides strong evidence that this binding site acts as the physiological receptor of flagellin.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 12:18:59