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PMID: 11340183 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

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.

The Plant cell ·Vol. 13 ·No. 5 ·2001-05-00 ·Pages 1079-93

Lee J, Klessig DF, Nürnberger T

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 125I-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 125I-harpin(Psph) to its binding site. Another elicitor of the hypersensitive response and HIN1 induction in tobacco, the Phytophthora megasperma-derived beta-elicitin beta-megaspermin, 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 revealed that MAPK activity was essential for pathogenesis-related gene expression in harpin(Psph)-treated tobacco cells. Thus, a receptor-mediated MAPK-dependent signaling pathway may mediate the activation of plant defense responses induced by harpin(Psph).

MeSH Terms
Bacterial Outer Membrane Proteins/metabolism Binding Sites Binding, Competitive Cell Membrane/metabolism Fungal Proteins/pharmacology Gene Expression Regulation Gene Expression Regulation, Plant Mitogen-Activated Protein Kinases/metabolism Peptide Fragments/metabolism Plant Diseases/genetics Plant Growth Regulators/pharmacology Plant Proteins/biosynthesis,genetics Plants, Toxic Salicylic Acid/pharmacology Tobacco/genetics,metabolism
Chemicals
Bacterial Outer Membrane Proteins Fungal Proteins HIN1 protein, Nicotiana tabacum Peptide Fragments Plant Growth Regulators Plant Proteins harpin protein, Erwinia amylovora HrpZ protein, Pseudomonas syringae Mitogen-Activated Protein Kinases Salicylic Acid
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Lee J
Department of Stress and Developmental Biology, Leibniz Institute of Plant Biochemistry, Weinberg 3, D-06120 Halle/Saale, Germany.
Klessig D F
Nürnberger T
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Article Info
Journal
The Plant cell
Abbr.
Plant Cell
ISSN
1040-4651
Published
2001-05-00
Pages
1079-93
Language
English
Region
England
NLM ID
9208688
PMCID
PMC135567
Subset
IM
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