MelampsoraV1, Main, Exploration, bibRecord, 000143

Crystal structures of flax rust avirulence proteins AvrL567-A and -D reveal details of the structural basis for flax disease resistance specificity.

Identifieur interne : 000143 ( Main/Exploration ); précédent : 000142; suivant : 000144

Crystal structures of flax rust avirulence proteins AvrL567-A and -D reveal details of the structural basis for flax disease resistance specificity.

Auteurs : Ching-I A. Wang [Australie] ; Gregor Guncar ; Jade K. Forwood ; Trazel Teh ; Ann-Maree Catanzariti ; Gregory J. Lawrence ; Fionna E. Loughlin ; Joel P. Mackay ; Horst Joachim Schirra ; Peter A. Anderson ; Jeffrey G. Ellis ; Peter N. Dodds ; Bostjan Kobe

Source :

The Plant cell [ 1040-4651 ] ; 2007.

RBID : pubmed:17873095

Descripteurs français

KwdFr :
- Analyse de mutations d'ADN (MeSH), Basidiomycota (composition chimique), Basidiomycota (pathogénicité), Cristallographie aux rayons X (MeSH), Données de séquences moléculaires (MeSH), Facteurs de virulence (composition chimique), Facteurs de virulence (métabolisme), Immunité innée (immunologie), Liaison aux protéines (MeSH), Lin (composition chimique), Lin (immunologie), Lin (microbiologie), Maladies des plantes (immunologie), Maladies des plantes (microbiologie), Modèles moléculaires (MeSH), Protéines végétales (composition chimique), Protéines végétales (métabolisme), Relation structure-activité (MeSH), Séquence d'acides aminés (MeSH).
MESH :
- composition chimique : Basidiomycota, Facteurs de virulence, Lin, Protéines végétales.
- immunologie : Immunité innée, Lin, Maladies des plantes.
- microbiologie : Lin, Maladies des plantes.
- métabolisme : Facteurs de virulence, Protéines végétales.
- pathogénicité : Basidiomycota.
- Analyse de mutations d'ADN, Cristallographie aux rayons X, Données de séquences moléculaires, Liaison aux protéines, Modèles moléculaires, Relation structure-activité, Séquence d'acides aminés.

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Basidiomycota (chemistry), Basidiomycota (pathogenicity), Crystallography, X-Ray (MeSH), DNA Mutational Analysis (MeSH), Flax (chemistry), Flax (immunology), Flax (microbiology), Immunity, Innate (immunology), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Plant Diseases (immunology), Plant Diseases (microbiology), Plant Proteins (chemistry), Plant Proteins (metabolism), Protein Binding (MeSH), Structure-Activity Relationship (MeSH), Virulence Factors (chemistry), Virulence Factors (metabolism).
MESH :
- chemical , chemistry : Plant Proteins, Virulence Factors.
- chemistry : Basidiomycota, Flax.
- immunology : Flax, Immunity, Innate, Plant Diseases.
- chemical , metabolism : Plant Proteins, Virulence Factors.
- microbiology : Flax, Plant Diseases.
- pathogenicity : Basidiomycota.
- Amino Acid Sequence, Crystallography, X-Ray, DNA Mutational Analysis, Models, Molecular, Molecular Sequence Data, Protein Binding, Structure-Activity Relationship.

Abstract

The gene-for-gene mechanism of plant disease resistance involves direct or indirect recognition of pathogen avirulence (Avr) proteins by plant resistance (R) proteins. Flax rust (Melampsora lini) AvrL567 avirulence proteins and the corresponding flax (Linum usitatissimum) L5, L6, and L7 resistance proteins interact directly. We determined the three-dimensional structures of two members of the AvrL567 family, AvrL567-A and AvrL567-D, at 1.4- and 2.3-A resolution, respectively. The structures of both proteins are very similar and reveal a beta-sandwich fold with no close known structural homologs. The polymorphic residues in the AvrL567 family map to the surface of the protein, and polymorphisms in residues associated with recognition differences for the R proteins lead to significant changes in surface chemical properties. Analysis of single amino acid substitutions in AvrL567 proteins confirm the role of individual residues in conferring differences in recognition and suggest that the specificity results from the cumulative effects of multiple amino acid contacts. The structures also provide insights into possible pathogen-associated functions of AvrL567 proteins, with nucleic acid binding activity demonstrated in vitro. Our studies provide some of the first structural information on avirulence proteins that bind directly to the corresponding resistance proteins, allowing an examination of the molecular basis of the interaction with the resistance proteins as a step toward designing new resistance specificities.

DOI: 10.1105/tpc.107.053611
PubMed: 17873095
PubMed Central: PMC2048696

Affiliations:

Australie

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

to stream Main, to step Corpus: 000144
to stream Main, to step Curation: 000144

Le document en format XML

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<front><div type="abstract" xml:lang="en">The gene-for-gene mechanism of plant disease resistance involves direct or indirect recognition of pathogen avirulence (Avr) proteins by plant resistance (R) proteins. Flax rust (Melampsora lini) AvrL567 avirulence proteins and the corresponding flax (Linum usitatissimum) L5, L6, and L7 resistance proteins interact directly. We determined the three-dimensional structures of two members of the AvrL567 family, AvrL567-A and AvrL567-D, at 1.4- and 2.3-A resolution, respectively. The structures of both proteins are very similar and reveal a beta-sandwich fold with no close known structural homologs. The polymorphic residues in the AvrL567 family map to the surface of the protein, and polymorphisms in residues associated with recognition differences for the R proteins lead to significant changes in surface chemical properties. Analysis of single amino acid substitutions in AvrL567 proteins confirm the role of individual residues in conferring differences in recognition and suggest that the specificity results from the cumulative effects of multiple amino acid contacts. The structures also provide insights into possible pathogen-associated functions of AvrL567 proteins, with nucleic acid binding activity demonstrated in vitro. Our studies provide some of the first structural information on avirulence proteins that bind directly to the corresponding resistance proteins, allowing an examination of the molecular basis of the interaction with the resistance proteins as a step toward designing new resistance specificities.</div>
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<Abstract><AbstractText>The gene-for-gene mechanism of plant disease resistance involves direct or indirect recognition of pathogen avirulence (Avr) proteins by plant resistance (R) proteins. Flax rust (Melampsora lini) AvrL567 avirulence proteins and the corresponding flax (Linum usitatissimum) L5, L6, and L7 resistance proteins interact directly. We determined the three-dimensional structures of two members of the AvrL567 family, AvrL567-A and AvrL567-D, at 1.4- and 2.3-A resolution, respectively. The structures of both proteins are very similar and reveal a beta-sandwich fold with no close known structural homologs. The polymorphic residues in the AvrL567 family map to the surface of the protein, and polymorphisms in residues associated with recognition differences for the R proteins lead to significant changes in surface chemical properties. Analysis of single amino acid substitutions in AvrL567 proteins confirm the role of individual residues in conferring differences in recognition and suggest that the specificity results from the cumulative effects of multiple amino acid contacts. The structures also provide insights into possible pathogen-associated functions of AvrL567 proteins, with nucleic acid binding activity demonstrated in vitro. Our studies provide some of the first structural information on avirulence proteins that bind directly to the corresponding resistance proteins, allowing an examination of the molecular basis of the interaction with the resistance proteins as a step toward designing new resistance specificities.</AbstractText>
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Crystal structures of flax rust avirulence proteins AvrL567-A and -D reveal details of the structural basis for flax disease resistance specificity.

Crystal structures of flax rust avirulence proteins AvrL567-A and -D reveal details of the structural basis for flax disease resistance specificity.

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