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Titolo:
A harpin binding site in tobacco plasma membranes mediates activation of the pathogenesis-related gene HIN1 independent of extracellular calcium but dependent on mitogen-activated protein kinase activity
Autore:
Lee, J; Klessig, DF; Nurnberger, T;
Indirizzi:
Leibniz Inst Plant Biochem, Dept Stress & Dev Biol, D-06120 Halle, GermanyLeibniz Inst Plant Biochem Halle Germany D-06120 D-06120 Halle, Germany Rutgers State Univ, Dept Mol Biol & Biochem, Piscataway, NJ 08854 USA Rutgers State Univ Piscataway NJ USA 08854 chem, Piscataway, NJ 08854 USA
Titolo Testata:
PLANT CELL
fascicolo: 5, volume: 13, anno: 2001,
pagine: 1079 - 1093
SICI:
1040-4651(200105)13:5<1079:AHBSIT>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
SYSTEMIC ACQUIRED-RESISTANCE; ANTIFUNGAL PLANT DEFENSIN; DAHLIA DAHLIA-MERCKII; HIGH-AFFINITY BINDING; HYPERSENSITIVE RESPONSE; SALICYLIC-ACID; SIGNAL-TRANSDUCTION; ERWINIA-AMYLOVORA; BETA-GLUCAN; MAP KINASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
66
Recensione:
Indirizzi per estratti:
Indirizzo: Nurnberger, T Leibniz Inst Plant Biochem, Dept Stress & Dev Biol, Weinberg3, D-06120 Halle, Germany Leibniz Inst Plant Biochem Weinberg 3 Halle Germany D-06120
Citazione:
J. Lee et al., "A harpin binding site in tobacco plasma membranes mediates activation of the pathogenesis-related gene HIN1 independent of extracellular calcium but dependent on mitogen-activated protein kinase activity", PL CELL, 13(5), 2001, pp. 1079-1093

Abstract

Harpin from the bean halo-blight pathogen Pseudomonas syringae pv phaseolicola (harpin(Psph)) elicits the hypersensitive response and the accumulation of pathogenesis-related gene transcripts in the nonhost plant tobacco. Here, we report the characterization of a nonproteinaceous binding site for harpin(Psph) in tobacco plasma membranes, which is assumed to mediate the activation of plant defense responses in a receptor-like manner. Binding of I-125-harpin(Psph) to tobacco microsomal membranes (dissociation constant = 425 nM) and protoplasts (dissociation constant = 380 nM) was specific, reversible, and saturable. A close correlation was found between the abilities of harpin(Psph) fragments to elicit the transcript accumulation of the pathogenesis-related tobacco gene HIN1 and to compete for binding of I-125-harpin(Psph) to its binding site. Another elicitor of the hypersensitive response and HIN1 induction in tobacco, the Phytophthora megasperma-derived beta -elicitin beta -mesaspermin, failed to bind to the putative harpin(Psph) receptor. In contrast to activation by beta -megaspermin, harpin(Psph)-induced activation of the 48-kD salicylic acid-responsive mitogen-activated protein kinase (MAPK) and HIN1 transcript accumulation were independent of extracellular calcium. Moreover, use of the MAPK kinase inhibitor U0126 revealedthat MAPK activity was essential for pathogenesis-related gene expression in harpin(Psph)-treated tobacco cells. Thus, a receptor-mediated MARK-dependent signaling pathway may mediate the activation of plant defense responses induced by harpin(Psph).

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/20 alle ore 00:28:29