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  Signal perception and intracellular signal transduction in plant pathogen defense

Nurnberger, T., Wirtz, W., Nennstiel, D., Hahlbrock, K., Jabs, T., Zimmermann, S., et al. (1997). Signal perception and intracellular signal transduction in plant pathogen defense. In 7th Swiss Workshop of Methodology in Receptor Research (pp. 127-136).

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-3116-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-3117-3
Genre: Conference Paper

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Nurnberger-1997-Signal perception an.pdf (Any fulltext), 318KB
 
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 Creators:
Nurnberger, T.1, Author
Wirtz, W.1, Author
Nennstiel, D.1, Author
Hahlbrock, K.1, Author
Jabs, T.1, Author
Zimmermann, S.2, Author              
Scheel, D.1, Author
Affiliations:
1External Organizations, ou_persistent22              
2Plant Signalling, Cooperative Research Groups, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753311              

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Free keywords: cultured parsley cells phytophthora-megasperma oligopeptide elicitor extracellular glycoprotein fungal infection membranes responses binding
 Abstract: Disease resistance in plant/pathogen interactions requires sensitive and specific recognition mechanisms for pathogen-derived signals in plants. Cultured parsley (Petroselinum crispum) cells respond to treatment with a crude cell wall preparation derived from the phytopathogenic fungus Phytophthora sojae with transcriptional activation of the same set of defense-related genes as are activated in parsley leaves upon infection with fungal spores. A 13 amino acid core sequence (Pep-13) of a 42 kDa fungal cell wall glycoprotein was identified which stimulates the same responses as the crude cell wall elicitor, namely macroscopic Ca2+ and H+-influxes, effluxes of K+- and Cl- ions, production of active oxygen species (oxidative burst), defense-related gene activation, and formation of antifungal phytoalexins. Using [I-125]Tyr-Pep-13 as ligand in binding assays, a single-class high-affinity binding site in parsley microsomal membranes and protoplasts could be detected. Binding was specific, saturable, and reversible. By chemical crosslinking, a 91 kDa parsley plasma membrane protein was identified to be the receptor of the peptide elicitor. Isolation of this receptor protein involved in pathogen defense in plants is under way.

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Language(s): eng - English
 Dates: 1997
 Publication Status: Published in print
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 Rev. Type: -
 Identifiers: ISI: ISI:A1997WE76200009
DOI: 10.3109/10799899709036598
URI: ://A1997WE76200009 http://informahealthcare.com/doi/pdfplus/10.3109/10799899709036598
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Title: 7th Swiss Workshop of Methodology in Receptor Research
Place of Event: MEIRINGEN, GERMANY
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Title: 7th Swiss Workshop of Methodology in Receptor Research
Source Genre: Proceedings
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Pages: - Volume / Issue: - Sequence Number: - Start / End Page: 127 - 136 Identifier: -