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Silencing of acidic pathogenesis-related PR-1 genes increases extracellular beta-(1->3)-glucanase activity at the onset of tobacco defence reactions.

Identifieur interne : 001C22 ( Main/Exploration ); précédent : 001C21; suivant : 001C23

Silencing of acidic pathogenesis-related PR-1 genes increases extracellular beta-(1->3)-glucanase activity at the onset of tobacco defence reactions.

Auteurs : Marie-Pierre Rivière [France] ; Antoine Marais ; Michel Ponchet ; William Willats ; Eric Galiana

Source :

RBID : pubmed:18390849

Descripteurs français

English descriptors

Abstract

The class 1 pathogenesis-related (PR) proteins are thought to be involved in plant defence responses, but their molecular functions are unknown. The function of PR-1 was investigated in tobacco by generating stable PR-1a-silenced lines in which other acidic PR-1 genes (PR-1b and PR-1c) were silenced. Plants lacking extracellular PR-1s were more susceptible than wild-type plants to the oomycete Phytophthora parasitica but displayed unaffected systemic acquired resistance and developmental resistance to this pathogen. Treatment with salicylic acid up-regulates the PR-1g gene, encoding a basic protein of the PR-1 family, in PR-1-deficient tobacco, indicating that PR-1 expression may repress that of PR-1g. This shows that acidic PR-1s are dispensable for expression of salicylic acid-dependent acquired resistances against P. parasitica and may reveal a functional overlap in tobacco defence or a functional redundancy in the PR-1 gene family. The data also show that there is a specific increase in apoplastic beta-(1-->3)-glucanase activity and a decrease in beta-(1-->3)-glucan deposition in PR-1-silenced lines following activation of defence reactions. Complementation of the silencing by apoplastic treatment with a recombinant PR-1a protein largely restores the wild-type beta-(1-->3)-glucanase activity and callose phenotype. Taken together with the immunolocalization of PR-1a to sites of beta-(1-->3)-glucan deposition in wild-type plants, these results are indicative of a function for PR-1a in regulation of enzymatic activity of extracellular beta-(1-->3)-glucanases.

DOI: 10.1093/jxb/ern044
PubMed: 18390849


Affiliations:


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Le document en format XML

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<term>Fungal Proteins (MeSH)</term>
<term>Gene Expression Regulation, Plant (drug effects)</term>
<term>Gene Silencing (drug effects)</term>
<term>Genetic Complementation Test (MeSH)</term>
<term>Glucan 1,3-beta-Glucosidase (analysis)</term>
<term>Glucan 1,3-beta-Glucosidase (antagonists & inhibitors)</term>
<term>Glucan 1,3-beta-Glucosidase (metabolism)</term>
<term>Glucans (metabolism)</term>
<term>Immunity, Innate (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Phytophthora (MeSH)</term>
<term>Plant Diseases (genetics)</term>
<term>Plant Proteins (analysis)</term>
<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (metabolism)</term>
<term>Plants, Genetically Modified (MeSH)</term>
<term>Protein Isoforms (genetics)</term>
<term>Protein Isoforms (metabolism)</term>
<term>RNA Interference (drug effects)</term>
<term>Recombinant Proteins (analysis)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>Salicylic Acid (pharmacology)</term>
<term>Tobacco (enzymology)</term>
<term>Tobacco (genetics)</term>
<term>Tobacco (immunology)</term>
<term>Tobacco (parasitology)</term>
<term>Up-Regulation (drug effects)</term>
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<term>Acide salicylique (pharmacologie)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Extinction de l'expression des gènes (effets des médicaments et des substances chimiques)</term>
<term>Glucan 1,3-beta-glucosidase (analyse)</term>
<term>Glucan 1,3-beta-glucosidase (antagonistes et inhibiteurs)</term>
<term>Glucan 1,3-beta-glucosidase (métabolisme)</term>
<term>Glucanes (métabolisme)</term>
<term>Immunité innée (MeSH)</term>
<term>Interférence par ARN (effets des médicaments et des substances chimiques)</term>
<term>Isoformes de protéines (génétique)</term>
<term>Isoformes de protéines (métabolisme)</term>
<term>Maladies des plantes (génétique)</term>
<term>Phytophthora (MeSH)</term>
<term>Protéines d'algue (pharmacologie)</term>
<term>Protéines fongiques (MeSH)</term>
<term>Protéines recombinantes (analyse)</term>
<term>Protéines recombinantes (génétique)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Protéines végétales (analyse)</term>
<term>Protéines végétales (génétique)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Régulation de l'expression des gènes végétaux (effets des médicaments et des substances chimiques)</term>
<term>Régulation positive (effets des médicaments et des substances chimiques)</term>
<term>Tabac (enzymologie)</term>
<term>Tabac (génétique)</term>
<term>Tabac (immunologie)</term>
<term>Tabac (parasitologie)</term>
<term>Test de complémentation (MeSH)</term>
<term>Végétaux génétiquement modifiés (MeSH)</term>
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<term>Plant Proteins</term>
<term>Recombinant Proteins</term>
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<term>Protein Isoforms</term>
<term>Recombinant Proteins</term>
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<term>Glucan 1,3-beta-glucosidase</term>
<term>Protéines recombinantes</term>
<term>Protéines végétales</term>
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<term>Glucan 1,3-beta-glucosidase</term>
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<term>RNA Interference</term>
<term>Up-Regulation</term>
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<term>Extinction de l'expression des gènes</term>
<term>Interférence par ARN</term>
<term>Régulation de l'expression des gènes végétaux</term>
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<term>Tabac</term>
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<term>Tobacco</term>
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<term>Maladies des plantes</term>
<term>Protéines recombinantes</term>
<term>Protéines végétales</term>
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<term>Tabac</term>
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<term>Tobacco</term>
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<term>Protéines recombinantes</term>
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<div type="abstract" xml:lang="en">The class 1 pathogenesis-related (PR) proteins are thought to be involved in plant defence responses, but their molecular functions are unknown. The function of PR-1 was investigated in tobacco by generating stable PR-1a-silenced lines in which other acidic PR-1 genes (PR-1b and PR-1c) were silenced. Plants lacking extracellular PR-1s were more susceptible than wild-type plants to the oomycete Phytophthora parasitica but displayed unaffected systemic acquired resistance and developmental resistance to this pathogen. Treatment with salicylic acid up-regulates the PR-1g gene, encoding a basic protein of the PR-1 family, in PR-1-deficient tobacco, indicating that PR-1 expression may repress that of PR-1g. This shows that acidic PR-1s are dispensable for expression of salicylic acid-dependent acquired resistances against P. parasitica and may reveal a functional overlap in tobacco defence or a functional redundancy in the PR-1 gene family. The data also show that there is a specific increase in apoplastic beta-(1-->3)-glucanase activity and a decrease in beta-(1-->3)-glucan deposition in PR-1-silenced lines following activation of defence reactions. Complementation of the silencing by apoplastic treatment with a recombinant PR-1a protein largely restores the wild-type beta-(1-->3)-glucanase activity and callose phenotype. Taken together with the immunolocalization of PR-1a to sites of beta-(1-->3)-glucan deposition in wild-type plants, these results are indicative of a function for PR-1a in regulation of enzymatic activity of extracellular beta-(1-->3)-glucanases.</div>
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<AbstractText>The class 1 pathogenesis-related (PR) proteins are thought to be involved in plant defence responses, but their molecular functions are unknown. The function of PR-1 was investigated in tobacco by generating stable PR-1a-silenced lines in which other acidic PR-1 genes (PR-1b and PR-1c) were silenced. Plants lacking extracellular PR-1s were more susceptible than wild-type plants to the oomycete Phytophthora parasitica but displayed unaffected systemic acquired resistance and developmental resistance to this pathogen. Treatment with salicylic acid up-regulates the PR-1g gene, encoding a basic protein of the PR-1 family, in PR-1-deficient tobacco, indicating that PR-1 expression may repress that of PR-1g. This shows that acidic PR-1s are dispensable for expression of salicylic acid-dependent acquired resistances against P. parasitica and may reveal a functional overlap in tobacco defence or a functional redundancy in the PR-1 gene family. The data also show that there is a specific increase in apoplastic beta-(1-->3)-glucanase activity and a decrease in beta-(1-->3)-glucan deposition in PR-1-silenced lines following activation of defence reactions. Complementation of the silencing by apoplastic treatment with a recombinant PR-1a protein largely restores the wild-type beta-(1-->3)-glucanase activity and callose phenotype. Taken together with the immunolocalization of PR-1a to sites of beta-(1-->3)-glucan deposition in wild-type plants, these results are indicative of a function for PR-1a in regulation of enzymatic activity of extracellular beta-(1-->3)-glucanases.</AbstractText>
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