RustEffectorV1, Main, Exploration, bibRecord, 000120

Intramolecular interaction influences binding of the Flax L5 and L6 resistance proteins to their AvrL567 ligands.

Identifieur interne : 000120 ( Main/Exploration ); précédent : 000119; suivant : 000121

Intramolecular interaction influences binding of the Flax L5 and L6 resistance proteins to their AvrL567 ligands.

Auteurs : Michael Ravensdale [Australie] ; Maud Bernoux ; Thomas Ve ; Bostjan Kobe ; Peter H. Thrall ; Jeffrey G. Ellis ; Peter N. Dodds

Source :

PLoS pathogens [ 1553-7374 ] ; 2012.

RBID : pubmed:23209402

Descripteurs français

KwdFr :
- Basidiomycota (génétique), Basidiomycota (métabolisme), Lin (génétique), Lin (microbiologie), Lin (métabolisme), Maladies des plantes (MeSH), Mutagenèse dirigée (MeSH), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Protéines végétales (génétique), Protéines végétales (métabolisme), Résistance à la maladie (MeSH).
MESH :
- génétique : Basidiomycota, Lin, Protéines fongiques, Protéines végétales.
- microbiologie : Lin.
- métabolisme : Basidiomycota, Lin, Protéines fongiques, Protéines végétales.
- Maladies des plantes, Mutagenèse dirigée, Résistance à la maladie.

English descriptors

KwdEn :
- Basidiomycota (genetics), Basidiomycota (metabolism), Disease Resistance (MeSH), Flax (genetics), Flax (metabolism), Flax (microbiology), Fungal Proteins (genetics), Fungal Proteins (metabolism), Mutagenesis, Site-Directed (MeSH), Plant Diseases (MeSH), Plant Proteins (genetics), Plant Proteins (metabolism).
MESH :
- chemical , genetics : Fungal Proteins, Plant Proteins.
- genetics : Basidiomycota, Flax.
- metabolism : Basidiomycota, Flax, Fungal Proteins, Plant Proteins.
- microbiology : Flax.
- Disease Resistance, Mutagenesis, Site-Directed, Plant Diseases.

Abstract

L locus resistance (R) proteins are nucleotide binding (NB-ARC) leucine-rich repeat (LRR) proteins from flax (Linum usitatissimum) that provide race-specific resistance to the causal agent of flax rust disease, Melampsora lini. L5 and L6 are two alleles of the L locus that directly recognize variants of the fungal effector AvrL567. In this study, we have investigated the molecular details of this recognition by site-directed mutagenesis of AvrL567 and construction of chimeric L proteins. Single, double and triple mutations of polymorphic residues in a variety of AvrL567 variants showed additive effects on recognition strength, suggesting that multiple contact points are involved in recognition. Domain-swap experiments between L5 and L6 show that specificity differences are determined by their corresponding LRR regions. Most positively selected amino acid sites occur in the N- and C-terminal LRR units, and polymorphisms in the first seven and last four LRR units contribute to recognition specificity of L5 and L6 respectively. This further confirms that multiple, additive contact points occur between AvrL567 variants and either L5 or L6. However, we also observed that recognition of AvrL567 is affected by co-operative polymorphisms between both adjacent and distant domains of the R protein, including the TIR, ARC and LRR domains, implying that these residues are involved in intramolecular interactions to optimize detection of the pathogen and defense signal activation. We suggest a model where Avr ligand interaction directly competes with intramolecular interactions to cause activation of the R protein.

DOI: 10.1371/journal.ppat.1003004
PubMed: 23209402
PubMed Central: PMC3510248

Affiliations:

Australie

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<term>Flax (metabolism)</term>
<term>Flax (microbiology)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Mutagenesis, Site-Directed (MeSH)</term>
<term>Plant Diseases (MeSH)</term>
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<term>Protéines fongiques (génétique)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Protéines végétales (génétique)</term>
<term>Protéines végétales (métabolisme)</term>
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<front><div type="abstract" xml:lang="en">L locus resistance (R) proteins are nucleotide binding (NB-ARC) leucine-rich repeat (LRR) proteins from flax (Linum usitatissimum) that provide race-specific resistance to the causal agent of flax rust disease, Melampsora lini. L5 and L6 are two alleles of the L locus that directly recognize variants of the fungal effector AvrL567. In this study, we have investigated the molecular details of this recognition by site-directed mutagenesis of AvrL567 and construction of chimeric L proteins. Single, double and triple mutations of polymorphic residues in a variety of AvrL567 variants showed additive effects on recognition strength, suggesting that multiple contact points are involved in recognition. Domain-swap experiments between L5 and L6 show that specificity differences are determined by their corresponding LRR regions. Most positively selected amino acid sites occur in the N- and C-terminal LRR units, and polymorphisms in the first seven and last four LRR units contribute to recognition specificity of L5 and L6 respectively. This further confirms that multiple, additive contact points occur between AvrL567 variants and either L5 or L6. However, we also observed that recognition of AvrL567 is affected by co-operative polymorphisms between both adjacent and distant domains of the R protein, including the TIR, ARC and LRR domains, implying that these residues are involved in intramolecular interactions to optimize detection of the pathogen and defense signal activation. We suggest a model where Avr ligand interaction directly competes with intramolecular interactions to cause activation of the R protein.</div>
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<Abstract><AbstractText>L locus resistance (R) proteins are nucleotide binding (NB-ARC) leucine-rich repeat (LRR) proteins from flax (Linum usitatissimum) that provide race-specific resistance to the causal agent of flax rust disease, Melampsora lini. L5 and L6 are two alleles of the L locus that directly recognize variants of the fungal effector AvrL567. In this study, we have investigated the molecular details of this recognition by site-directed mutagenesis of AvrL567 and construction of chimeric L proteins. Single, double and triple mutations of polymorphic residues in a variety of AvrL567 variants showed additive effects on recognition strength, suggesting that multiple contact points are involved in recognition. Domain-swap experiments between L5 and L6 show that specificity differences are determined by their corresponding LRR regions. Most positively selected amino acid sites occur in the N- and C-terminal LRR units, and polymorphisms in the first seven and last four LRR units contribute to recognition specificity of L5 and L6 respectively. This further confirms that multiple, additive contact points occur between AvrL567 variants and either L5 or L6. However, we also observed that recognition of AvrL567 is affected by co-operative polymorphisms between both adjacent and distant domains of the R protein, including the TIR, ARC and LRR domains, implying that these residues are involved in intramolecular interactions to optimize detection of the pathogen and defense signal activation. We suggest a model where Avr ligand interaction directly competes with intramolecular interactions to cause activation of the R protein.</AbstractText>
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Intramolecular interaction influences binding of the Flax L5 and L6 resistance proteins to their AvrL567 ligands.

Intramolecular interaction influences binding of the Flax L5 and L6 resistance proteins to their AvrL567 ligands.

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