Source:http://linkedlifedata.com/resource/pubmed/id/12426314
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
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| pubmed:dateCreated |
2003-1-20
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| pubmed:databankReference | |
| pubmed:abstractText |
Plants are continuously exposed to attack by potential phytopathogens. Disease prevention requires pathogen recognition and the induction of a multifaceted defense response. We are studying the non-host disease resistance response of parsley to the oomycete, Phytophthora sojae using a cell culture-based system. Receptor-mediated recognition of P. sojae may be achieved through a thirteen amino acid peptide sequence (Pep-13) present within an abundant cell wall transglutaminase. Following recognition of this elicitor molecule, parsley cells mount a defense response, which includes the generation of reactive oxygen species (ROS) and transcriptional activation of genes encoding pathogenesis-related (PR) proteins or enzymes involved in the synthesis of antimicrobial phytoalexins. Treatment of parsley cells with the NADPH oxidase inhibitor, diphenylene iodonium (DPI), blocked both Pep-13-induced phytoalexin production and the accumulation of transcripts encoding enzymes involved in their synthesis. In contrast, DPI treatment had no effect upon Pep-13-induced PR gene expression, suggesting the existence of an oxidative burst-independent mechanism for the transcriptional activation of PR genes. The use of specific antibodies enabled the identification of three parsley mitogen-activated protein kinases (MAPKs) that are activated within the signal transduction pathway(s) triggered following recognition of Pep-13. Other environmental challenges failed to activate these kinases in parsley cells, suggesting that their activation plays a key role in defense signal transduction. Moreover, by making use of a protoplast co-transfection system overexpressing wild-type and loss-of-function MAPK mutants, we show an essential role for post-translational phosphorylation and activation of MAPKs for oxidative burst-independent PR promoter activation.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Jan
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
24
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| pubmed:volume |
278
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
2256-64
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| pubmed:dateRevised |
2008-11-21
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| pubmed:meshHeading |
pubmed-meshheading:12426314-Adaptation, Physiological,
pubmed-meshheading:12426314-Amino Acid Sequence,
pubmed-meshheading:12426314-Blotting, Western,
pubmed-meshheading:12426314-Cell Line,
pubmed-meshheading:12426314-DNA, Complementary,
pubmed-meshheading:12426314-Enzyme Activation,
pubmed-meshheading:12426314-Gene Expression Regulation, Plant,
pubmed-meshheading:12426314-MAP Kinase Signaling System,
pubmed-meshheading:12426314-Molecular Sequence Data,
pubmed-meshheading:12426314-Mutagenesis, Site-Directed,
pubmed-meshheading:12426314-Petroselinum,
pubmed-meshheading:12426314-Phytophthora,
pubmed-meshheading:12426314-Plant Physiological Phenomena,
pubmed-meshheading:12426314-Plant Proteins,
pubmed-meshheading:12426314-Precipitin Tests,
pubmed-meshheading:12426314-Promoter Regions, Genetic,
pubmed-meshheading:12426314-Protoplasts,
pubmed-meshheading:12426314-Respiratory Burst,
pubmed-meshheading:12426314-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:12426314-Sequence Homology, Amino Acid,
pubmed-meshheading:12426314-Time Factors,
pubmed-meshheading:12426314-Transfection
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| pubmed:year |
2003
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| pubmed:articleTitle |
Mitogen-activated protein kinases play an essential role in oxidative burst-independent expression of pathogenesis-related genes in parsley.
|
| pubmed:affiliation |
Department of Stress and Developmental Biology, Institute of Plant Biochemistry, Weinberg 3, D-06120 Halle (Saale), Germany.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|