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

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 variant...

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Autores principales:	Michael Ravensdale, Maud Bernoux, Thomas Ve, Bostjan Kobe, Peter H Thrall, Jeffrey G Ellis, Peter N Dodds
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/0417695e85464e7aa43a95ae3835388b
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spelling	oai:doaj.org-article:0417695e85464e7aa43a95ae3835388b2021-11-18T06:06:20ZIntramolecular interaction influences binding of the Flax L5 and L6 resistance proteins to their AvrL567 ligands.1553-73661553-737410.1371/journal.ppat.1003004https://doaj.org/article/0417695e85464e7aa43a95ae3835388b2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23209402/pdf/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374L 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.Michael RavensdaleMaud BernouxThomas VeBostjan KobePeter H ThrallJeffrey G EllisPeter N DoddsPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 8, Iss 11, p e1003004 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Michael Ravensdale Maud Bernoux Thomas Ve Bostjan Kobe Peter H Thrall Jeffrey G Ellis Peter N Dodds Intramolecular interaction influences binding of the Flax L5 and L6 resistance proteins to their AvrL567 ligands.
description	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.
format	article
author	Michael Ravensdale Maud Bernoux Thomas Ve Bostjan Kobe Peter H Thrall Jeffrey G Ellis Peter N Dodds
author_facet	Michael Ravensdale Maud Bernoux Thomas Ve Bostjan Kobe Peter H Thrall Jeffrey G Ellis Peter N Dodds
author_sort	Michael Ravensdale
title	Intramolecular interaction influences binding of the Flax L5 and L6 resistance proteins to their AvrL567 ligands.
title_short	Intramolecular interaction influences binding of the Flax L5 and L6 resistance proteins to their AvrL567 ligands.
title_full	Intramolecular interaction influences binding of the Flax L5 and L6 resistance proteins to their AvrL567 ligands.
title_fullStr	Intramolecular interaction influences binding of the Flax L5 and L6 resistance proteins to their AvrL567 ligands.
title_full_unstemmed	Intramolecular interaction influences binding of the Flax L5 and L6 resistance proteins to their AvrL567 ligands.
title_sort	intramolecular interaction influences binding of the flax l5 and l6 resistance proteins to their avrl567 ligands.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/0417695e85464e7aa43a95ae3835388b
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Intramolecular interaction influences binding of the Flax L5 and L6 resistance proteins to their AvrL567 ligands.

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