Harpin induces mitogen-activated protein kinase activity during defence responses in Arabidopsis thaliana suspension cultures

Elicitation of Arabidopsis thaliana (L.) Heynh. suspension cultures with the bacterial protein harpin (from Pseudomonas syringae pv. syringae) induced the activation of two kinases of 39 and 44 kDa, as demonstrated by in-gel kinase assays using myelin basic protein (MBP) as a substrate. Both these k...

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Veröffentlicht in:Planta 1999-11, Vol.210 (1), p.97-103
Hauptverfasser: Desikan, R, Clarke, A, Atherfold, P, Hancock, J.T, Neill, S.J
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creator Desikan, R
Clarke, A
Atherfold, P
Hancock, J.T
Neill, S.J
description Elicitation of Arabidopsis thaliana (L.) Heynh. suspension cultures with the bacterial protein harpin (from Pseudomonas syringae pv. syringae) induced the activation of two kinases of 39 and 44 kDa, as demonstrated by in-gel kinase assays using myelin basic protein (MBP) as a substrate. Both these kinases appeared to be tyrosine-phosphorylated upon activation, as demonstrated by treatment with tyrosine phosphatase and immunoprecipitation using an anti-phosphotyrosine monoclonal antibody. An inhibitor of mammalian mitogen-activated protein kinase (MAPK) activation, PD98059, inhibited harpin-induced MBPK activation, but did not inhibit the activity of these kinases. PD98059 also inhibited harpin-induced programmed cell death and defence gene expression, suggesting the involvement of harpin-induced MAPKs in defence responses in Arabidopsis thaliana.
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Heynh. suspension cultures with the bacterial protein harpin (from Pseudomonas syringae pv. syringae) induced the activation of two kinases of 39 and 44 kDa, as demonstrated by in-gel kinase assays using myelin basic protein (MBP) as a substrate. Both these kinases appeared to be tyrosine-phosphorylated upon activation, as demonstrated by treatment with tyrosine phosphatase and immunoprecipitation using an anti-phosphotyrosine monoclonal antibody. An inhibitor of mammalian mitogen-activated protein kinase (MAPK) activation, PD98059, inhibited harpin-induced MBPK activation, but did not inhibit the activity of these kinases. PD98059 also inhibited harpin-induced programmed cell death and defence gene expression, suggesting the involvement of harpin-induced MAPKs in defence responses in Arabidopsis thaliana.</description><identifier>ISSN: 0032-0935</identifier><identifier>EISSN: 1432-2048</identifier><identifier>DOI: 10.1007/s004250050658</identifier><identifier>PMID: 10592037</identifier><identifier>CODEN: PLANAB</identifier><language>eng</language><publisher>Berlin: Springer-Verlag</publisher><subject>Animal and plant ecology ; Animal, plant and microbial ecology ; Antibodies ; Apoptosis ; Apoptosis - drug effects ; Arabidopsis - cytology ; Arabidopsis - enzymology ; Arabidopsis thaliana ; Autoecology ; Bacterial Outer Membrane Proteins - pharmacology ; bacterial proteins ; Biological and medical sciences ; cell suspension culture ; Cells, Cultured ; defense mechanisms ; Enzyme Activation ; enzyme activity ; Enzyme Induction ; enzyme inhibitors ; Enzyme Inhibitors - pharmacology ; Fundamental and applied biological sciences. Psychology ; Gels ; Gene expression ; Generalities. Disease free stocks ; Hypersensitive response ; immunochemistry ; Mitogen-Activated Protein Kinases - antagonists &amp; inhibitors ; Mitogen-Activated Protein Kinases - biosynthesis ; Mitogen-Activated Protein Kinases - metabolism ; mitogens ; molecular weight ; Phosphatases ; Phosphorylation ; Phytopathology. Animal pests. 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Heynh. suspension cultures with the bacterial protein harpin (from Pseudomonas syringae pv. syringae) induced the activation of two kinases of 39 and 44 kDa, as demonstrated by in-gel kinase assays using myelin basic protein (MBP) as a substrate. Both these kinases appeared to be tyrosine-phosphorylated upon activation, as demonstrated by treatment with tyrosine phosphatase and immunoprecipitation using an anti-phosphotyrosine monoclonal antibody. An inhibitor of mammalian mitogen-activated protein kinase (MAPK) activation, PD98059, inhibited harpin-induced MBPK activation, but did not inhibit the activity of these kinases. 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Psychology</subject><subject>Gels</subject><subject>Gene expression</subject><subject>Generalities. Disease free stocks</subject><subject>Hypersensitive response</subject><subject>immunochemistry</subject><subject>Mitogen-Activated Protein Kinases - antagonists &amp; inhibitors</subject><subject>Mitogen-Activated Protein Kinases - biosynthesis</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>mitogens</subject><subject>molecular weight</subject><subject>Phosphatases</subject><subject>Phosphorylation</subject><subject>Phytopathology. Animal pests. 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subjects Animal and plant ecology
Animal, plant and microbial ecology
Antibodies
Apoptosis
Apoptosis - drug effects
Arabidopsis - cytology
Arabidopsis - enzymology
Arabidopsis thaliana
Autoecology
Bacterial Outer Membrane Proteins - pharmacology
bacterial proteins
Biological and medical sciences
cell suspension culture
Cells, Cultured
defense mechanisms
Enzyme Activation
enzyme activity
Enzyme Induction
enzyme inhibitors
Enzyme Inhibitors - pharmacology
Fundamental and applied biological sciences. Psychology
Gels
Gene expression
Generalities. Disease free stocks
Hypersensitive response
immunochemistry
Mitogen-Activated Protein Kinases - antagonists & inhibitors
Mitogen-Activated Protein Kinases - biosynthesis
Mitogen-Activated Protein Kinases - metabolism
mitogens
molecular weight
Phosphatases
Phosphorylation
Phytopathology. Animal pests. Plant and forest protection
Plant cells
plant proteins
Plants
Plants and fungi
Pseudomonas syringae pv. syringae
RNA
substrates
tyrosine
Tyrosine - metabolism
title Harpin induces mitogen-activated protein kinase activity during defence responses in Arabidopsis thaliana suspension cultures
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