High affinity binding of a fungal oligopeptide elicitor to parsley plasma membranes triggers multiple defense responses.
Identifieur interne : 002C21 ( Main/Exploration ); précédent : 002C20; suivant : 002C22High affinity binding of a fungal oligopeptide elicitor to parsley plasma membranes triggers multiple defense responses.
Auteurs : T. Nürnberger [Allemagne] ; D. Nennstiel ; T. Jabs ; W R Sacks ; K. Hahlbrock ; D. ScheelSource :
- Cell [ 0092-8674 ] ; 1994.
Descripteurs français
- KwdFr :
- Cellules cultivées (MeSH), Données de séquences moléculaires (MeSH), Extraits de plantes (biosynthèse), Glycoprotéines (métabolisme), Ions (MeSH), Liaison aux protéines (MeSH), Légumes (microbiologie), Légumes (physiologie), Membrane cellulaire (métabolisme), Microsomes (métabolisme), Modèles biologiques (MeSH), Oligopeptides (pharmacologie), Phytophthora (composition chimique), Protoplastes (métabolisme), Relation structure-activité (MeSH), Sesquiterpènes (MeSH), Sites de fixation (MeSH), Stimulation du métabolisme oxydatif (MeSH), Séquence d'acides aminés (MeSH), Terpènes (MeSH), Transcription génétique (MeSH), Transduction du signal (MeSH).
- MESH :
- biosynthèse : Extraits de plantes.
- composition chimique : Phytophthora.
- microbiologie : Légumes.
- métabolisme : Glycoprotéines, Membrane cellulaire, Microsomes, Protoplastes.
- pharmacologie : Oligopeptides.
- physiologie : Légumes.
- Cellules cultivées, Données de séquences moléculaires, Ions, Liaison aux protéines, Modèles biologiques, Relation structure-activité, Sesquiterpènes, Sites de fixation, Stimulation du métabolisme oxydatif, Séquence d'acides aminés, Terpènes, Transcription génétique, Transduction du signal.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Binding Sites (MeSH), Cell Membrane (metabolism), Cells, Cultured (MeSH), Glycoproteins (metabolism), Ions (MeSH), Microsomes (metabolism), Models, Biological (MeSH), Molecular Sequence Data (MeSH), Oligopeptides (pharmacology), Phytophthora (chemistry), Plant Extracts (biosynthesis), Protein Binding (MeSH), Protoplasts (metabolism), Respiratory Burst (MeSH), Sesquiterpenes (MeSH), Signal Transduction (MeSH), Structure-Activity Relationship (MeSH), Terpenes (MeSH), Transcription, Genetic (MeSH), Vegetables (microbiology), Vegetables (physiology).
- MESH :
- chemical , biosynthesis : Plant Extracts.
- chemical , metabolism : Glycoproteins.
- chemistry : Phytophthora.
- metabolism : Cell Membrane, Microsomes, Protoplasts.
- microbiology : Vegetables.
- chemical , pharmacology : Oligopeptides.
- physiology : Vegetables.
- Amino Acid Sequence, Binding Sites, Cells, Cultured, Ions, Models, Biological, Molecular Sequence Data, Protein Binding, Respiratory Burst, Sesquiterpenes, Signal Transduction, Structure-Activity Relationship, Terpenes, Transcription, Genetic.
Abstract
An oligopeptide of 13 amino acids (Pep-13) identified within a 42 kDa glycoprotein elicitor from P. mega-sperma was shown to be necessary and sufficient to stimulate a complex defense response in parsley cells comprising H+/Ca2+ influxes, K+/Cl- effluxes, an oxidative burst, defense-related gene activation, and phytoalexin formation. Binding of radiolabeled Pep-13 to parsley microsomes and protoplasts was specific, reversible, and saturable. Identical structural features of Pep-13 were found to be responsible for specific binding and initiation of all plant responses analyzed. The high affinity binding site recognizing the peptide ligand (KD = 2.4 nM) may therefore represent a novel class of receptors in plants, and the rapidly induced ion fluxes may constitute elements of the signal transduction cascade triggering pathogen defense in plants.
DOI: 10.1016/0092-8674(94)90423-5
PubMed: 8062387
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<term>Cells, Cultured (MeSH)</term>
<term>Glycoproteins (metabolism)</term>
<term>Ions (MeSH)</term>
<term>Microsomes (metabolism)</term>
<term>Models, Biological (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
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<term>Phytophthora (chemistry)</term>
<term>Plant Extracts (biosynthesis)</term>
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<term>Sesquiterpenes (MeSH)</term>
<term>Signal Transduction (MeSH)</term>
<term>Structure-Activity Relationship (MeSH)</term>
<term>Terpenes (MeSH)</term>
<term>Transcription, Genetic (MeSH)</term>
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<term>Vegetables (physiology)</term>
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<term>Glycoprotéines (métabolisme)</term>
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<term>Liaison aux protéines (MeSH)</term>
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<term>Légumes (physiologie)</term>
<term>Membrane cellulaire (métabolisme)</term>
<term>Microsomes (métabolisme)</term>
<term>Modèles biologiques (MeSH)</term>
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<term>Phytophthora (composition chimique)</term>
<term>Protoplastes (métabolisme)</term>
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<term>Terpènes (MeSH)</term>
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<term>Membrane cellulaire</term>
<term>Microsomes</term>
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<term>Terpenes</term>
<term>Transcription, Genetic</term>
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<term>Données de séquences moléculaires</term>
<term>Ions</term>
<term>Liaison aux protéines</term>
<term>Modèles biologiques</term>
<term>Relation structure-activité</term>
<term>Sesquiterpènes</term>
<term>Sites de fixation</term>
<term>Stimulation du métabolisme oxydatif</term>
<term>Séquence d'acides aminés</term>
<term>Terpènes</term>
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<front><div type="abstract" xml:lang="en">An oligopeptide of 13 amino acids (Pep-13) identified within a 42 kDa glycoprotein elicitor from P. mega-sperma was shown to be necessary and sufficient to stimulate a complex defense response in parsley cells comprising H+/Ca2+ influxes, K+/Cl- effluxes, an oxidative burst, defense-related gene activation, and phytoalexin formation. Binding of radiolabeled Pep-13 to parsley microsomes and protoplasts was specific, reversible, and saturable. Identical structural features of Pep-13 were found to be responsible for specific binding and initiation of all plant responses analyzed. The high affinity binding site recognizing the peptide ligand (KD = 2.4 nM) may therefore represent a novel class of receptors in plants, and the rapidly induced ion fluxes may constitute elements of the signal transduction cascade triggering pathogen defense in plants.</div>
</front>
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<Abstract><AbstractText>An oligopeptide of 13 amino acids (Pep-13) identified within a 42 kDa glycoprotein elicitor from P. mega-sperma was shown to be necessary and sufficient to stimulate a complex defense response in parsley cells comprising H+/Ca2+ influxes, K+/Cl- effluxes, an oxidative burst, defense-related gene activation, and phytoalexin formation. Binding of radiolabeled Pep-13 to parsley microsomes and protoplasts was specific, reversible, and saturable. Identical structural features of Pep-13 were found to be responsible for specific binding and initiation of all plant responses analyzed. The high affinity binding site recognizing the peptide ligand (KD = 2.4 nM) may therefore represent a novel class of receptors in plants, and the rapidly induced ion fluxes may constitute elements of the signal transduction cascade triggering pathogen defense in plants.</AbstractText>
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