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Titolo:
Both the extracellular leucine-rich repeat domain and the kinase activity of FLS2 are required for flagellin binding and signaling in arabidopsis
Autore:
Gomez-Gomez, L; Bauer, Z; Boller, T;
Indirizzi:
Friedrich Miescher Inst, CH-4002 Basel, Switzerland Friedrich Miescher Inst Basel Switzerland CH-4002 002 Basel, Switzerland Univ Basel, Inst Bot, CH-4056 Basel, Switzerland Univ Basel Basel Switzerland CH-4056 nst Bot, CH-4056 Basel, Switzerland
Titolo Testata:
PLANT CELL
fascicolo: 5, volume: 13, anno: 2001,
pagine: 1155 - 1163
SICI:
1040-4651(200105)13:5<1155:BTELRD>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLANT-DISEASE RESISTANCE; CLAVATA1 RECEPTOR-KINASE; FOR-GENE SPECIFICITY; TGF-BETA RECEPTOR; PROTEIN PHOSPHATASE; BACTERIAL FLAGELLIN; LOCUS; TRANSDUCTION; TOMATO; THALIANA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: Gomez-Gomez, L IDR, Secc Biotecnol, Campus Univ S-N, E-02071 Alicante, Spain IDR Campus Univ S-N Alicante Spain E-02071 Alicante, Spain
Citazione:
L. Gomez-Gomez et al., "Both the extracellular leucine-rich repeat domain and the kinase activity of FLS2 are required for flagellin binding and signaling in arabidopsis", PL CELL, 13(5), 2001, pp. 1155-1163

Abstract

In Arabidopsis, activation of defense responses by flagellin is triggered by the specific recognition of the most conserved domain of flagellin, represented by the peptide flg22, in a process involving the FLS2 gene, which encodes a leucine-rich repeat serine/threonine protein kinase, We shaw here that the two fls2 mutant alleles, fls2-24 and fls2-17, which were shown previously to confer insensitivity to flg22, also cause impaired flagellin binding. These features are rescued when a functional FLS2 gene is expressed as a transgene in each of the fls2 mutant plants, indicating that FLS2 is necessary for flagellin binding. The point mutation of the fls2-17; allele lies in the kinase domain. A kinase carrying this missense mutation lacked autophosphorylation activity when expressed in Escherichia coli, This indicates that kinase activity is required for binding and probably affects the stability of the flagellin receptor complex. We further show that overexpression of the kinase-associated protein phosphatase (KAPP) in Arabidopsis results in plants that are insensitive to flagellin treatment, and we show reduced flg22 binding in these plants. Furthermore, using the yeast two-hybrid system, we show physical interaction of KAPP with the kinase domain of FLS2. These results suggest that KAPP functions as a negative regulator of the FLS2 signal transduction pathway and that the phosphorylation of FLS2 is necessary for proper binding and signaling of the flagellin receptor complex.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 23:00:10