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Zhao Zhang - One of the best experts on this subject based on the ideXlab platform.
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broad taxonomic characterization of verticillium wilt resistance genes reveals an ancient origin of the tomato ve1 Immune Receptor
Molecular Plant Pathology, 2017Co-Authors: Yin Song, Zhao Zhang, Michael F Seidl, Aljaz Majer, Jernej Jakse, Branka Javornik, Bart P H J ThommaAbstract:Plant-pathogenic microbes secrete effector molecules to establish themselves on their hosts, whereas plants use Immune Receptors to try and intercept such effectors in order to prevent pathogen colonization. The tomato cell surface-localized Receptor Ve1 confers race-specific resistance against race 1 strains of the soil-borne vascular wilt fungus Verticillium dahliae which secrete the Ave1 effector. Here, we describe the cloning and characterization of Ve1 homologues from tobacco (Nicotiana glutinosa), potato (Solanum tuberosum), wild eggplant (Solanum torvum) and hop (Humulus lupulus), and demonstrate that particular Ve1 homologues govern resistance against V. dahliae race 1 strains through the recognition of the Ave1 effector. Phylogenetic analysis shows that Ve1 homologues are widely distributed in land plants. Thus, our study suggests an ancient origin of the Ve1 Immune Receptor in the plant kingdom.
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mutational analysis of the ve1 Immune Receptor that mediates verticillium resistance in tomato
PLOS ONE, 2014Co-Authors: Zhao Zhang, Yin Song, Chunming Liu, Bart P H J ThommaAbstract:Pathogenic Verticillium species are economically important plant pathogens that cause vascular wilt diseases in hundreds of plant species. The Ve1 gene of tomato confers resistance against race 1 strains of Verticillium dahliae and V. albo-atrum. Ve1 encodes an extracellular leucine-rich repeat (eLRR) Receptor-like protein (RLP) that serves as a cell surface Receptor for recognition of the recently identified secreted Verticillium effector Ave1. To investigate recognition of Ave1 by Ve1, alanine scanning was performed on the solvent exposed β-strand/β-turn residues across the eLRR domain of Ve1. In addition, alanine scanning was also employed to functionally characterize motifs that putatively mediate protein-protein interactions and endocytosis in the transmembrane domain and the cytoplasmic tail of the Ve1 protein. Functionality of the mutant proteins was assessed by screening for the occurrence of a hypersensitive response upon co-expression with Ave1 upon Agrobacterium tumefaciens-mediated transient expression (agroinfiltration). In order to confirm the agroinfiltration results, constructs encoding Ve1 mutants were transformed into Arabidopsis and the transgenes were challenged with race 1 Verticillium. Our analyses identified several regions of the Ve1 protein that are required for functionality.
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tomato Immune Receptor ve1 recognizes effector of multiple fungal pathogens uncovered by genome and rna sequencing
Proceedings of the National Academy of Sciences of the United States of America, 2012Co-Authors: Ronnie De Jonge, Peter H Van Esse, Karunakaran Maruthachalam, Melvin D Bolton, Parthasarathy Santhanam, Mojtaba Keykha Saber, Zhao Zhang, Toshiyuki Usami, Bart Lievens, Krishna V SubbaraoAbstract:Fungal plant pathogens secrete effector molecules to establish disease on their hosts, and plants in turn use Immune Receptors to try to intercept these effectors. The tomato Immune Receptor Ve1 governs resistance to race 1 strains of the soil-borne vascular wilt fungi Verticillium dahliae and Verticillium albo-atrum, but the corresponding Verticillium effector remained unknown thus far. By high-throughput population genome sequencing, a single 50-Kb sequence stretch was identified that only occurs in race 1 strains, and subsequent transcriptome sequencing of Verticillium-infected Nicotiana benthamiana plants revealed only a single highly expressed ORF in this region, designated Ave1 (for Avirulence on Ve1 tomato). Functional analyses confirmed that Ave1 activates Ve1-mediated resistance and demonstrated that Ave1 markedly contributes to fungal virulence, not only on tomato but also on Arabidopsis. Interestingly, Ave1 is homologous to a widespread family of plant natriuretic peptides. Besides plants, homologous proteins were only found in the bacterial plant pathogen Xanthomonas axonopodis and the plant pathogenic fungi Colletotrichum higginsianum, Cercospora beticola, and Fusarium oxysporum f. sp. lycopersici. The distribution of Ave1 homologs, coincident with the presence of Ave1 within a flexible genomic region, strongly suggests that Verticillium acquired Ave1 from plants through horizontal gene transfer. Remarkably, by transient expression we show that also the Ave1 homologs from F. oxysporum and C. beticola can activate Ve1-mediated resistance. In line with this observation, Ve1 was found to mediate resistance toward F. oxysporum in tomato, showing that this Immune Receptor is involved in resistance against multiple fungal pathogens.
Bart P H J Thomma - One of the best experts on this subject based on the ideXlab platform.
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broad taxonomic characterization of verticillium wilt resistance genes reveals an ancient origin of the tomato ve1 Immune Receptor
Molecular Plant Pathology, 2017Co-Authors: Yin Song, Zhao Zhang, Michael F Seidl, Aljaz Majer, Jernej Jakse, Branka Javornik, Bart P H J ThommaAbstract:Plant-pathogenic microbes secrete effector molecules to establish themselves on their hosts, whereas plants use Immune Receptors to try and intercept such effectors in order to prevent pathogen colonization. The tomato cell surface-localized Receptor Ve1 confers race-specific resistance against race 1 strains of the soil-borne vascular wilt fungus Verticillium dahliae which secrete the Ave1 effector. Here, we describe the cloning and characterization of Ve1 homologues from tobacco (Nicotiana glutinosa), potato (Solanum tuberosum), wild eggplant (Solanum torvum) and hop (Humulus lupulus), and demonstrate that particular Ve1 homologues govern resistance against V. dahliae race 1 strains through the recognition of the Ave1 effector. Phylogenetic analysis shows that Ve1 homologues are widely distributed in land plants. Thus, our study suggests an ancient origin of the Ve1 Immune Receptor in the plant kingdom.
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mutational analysis of the ve1 Immune Receptor that mediates verticillium resistance in tomato
PLOS ONE, 2014Co-Authors: Zhao Zhang, Yin Song, Chunming Liu, Bart P H J ThommaAbstract:Pathogenic Verticillium species are economically important plant pathogens that cause vascular wilt diseases in hundreds of plant species. The Ve1 gene of tomato confers resistance against race 1 strains of Verticillium dahliae and V. albo-atrum. Ve1 encodes an extracellular leucine-rich repeat (eLRR) Receptor-like protein (RLP) that serves as a cell surface Receptor for recognition of the recently identified secreted Verticillium effector Ave1. To investigate recognition of Ave1 by Ve1, alanine scanning was performed on the solvent exposed β-strand/β-turn residues across the eLRR domain of Ve1. In addition, alanine scanning was also employed to functionally characterize motifs that putatively mediate protein-protein interactions and endocytosis in the transmembrane domain and the cytoplasmic tail of the Ve1 protein. Functionality of the mutant proteins was assessed by screening for the occurrence of a hypersensitive response upon co-expression with Ave1 upon Agrobacterium tumefaciens-mediated transient expression (agroinfiltration). In order to confirm the agroinfiltration results, constructs encoding Ve1 mutants were transformed into Arabidopsis and the transgenes were challenged with race 1 Verticillium. Our analyses identified several regions of the Ve1 protein that are required for functionality.
Ksenia V Krasileva - One of the best experts on this subject based on the ideXlab platform.
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the nlr annotator tool enables annotation of the intracellular Immune Receptor repertoire
Plant Physiology, 2020Co-Authors: Burkhard Steuernagel, Kamil Witek, Simon G Krattinger, Ricardo H Ramirezgonzalez, Henkjan Schoonbeek, Erin Baggs, Agnieszka I Witek, Inderjit Singh Yadav, Ksenia V KrasilevaAbstract:Disease resistance genes encoding nucleotide-binding and leucine-rich repeat (NLR) intracellular Immune Receptor proteins detect pathogens by the presence of pathogen effectors. Plant genomes typically contain hundreds of NLR-encoding genes. The availability of the hexaploid wheat (Triticum aestivum) cultivar Chinese Spring reference genome allows a detailed study of its NLR complement. However, low NLR expression and high intrafamily sequence homology hinder their accurate annotation. Here, we developed NLR-Annotator, a software tool for in silico NLR identification independent of transcript support. Although developed for wheat, we demonstrate the universal applicability of NLR-Annotator across diverse plant taxa. We applied our tool to wheat and combined it with a transcript-validated subset of genes from the reference gene annotation to characterize the structure, phylogeny, and expression profile of the NLR gene family. We detected 3,400 full-length NLR loci, of which 1,560 were confirmed as expressed genes with intact open reading frames. NLRs with integrated domains mostly group in specific subclades. Members of another subclade predominantly locate in close physical proximity to NLRs carrying integrated domains, suggesting a paired helper function. Most NLRs (88%) display low basal expression (in the lower 10 percentile of transcripts). In young leaves subjected to biotic stress, we found up-regulation of 266 of the NLRs To illustrate the utility of our tool for the positional cloning of resistance genes, we estimated the number of NLR genes within the intervals of mapped rust resistance genes. Our study will support the identification of functional resistance genes in wheat to accelerate the breeding and engineering of disease-resistant varieties.
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physical and transcriptional organisation of the bread wheat intracellular Immune Receptor repertoire
bioRxiv, 2018Co-Authors: Burkhard Steuernagel, Kamil Witek, Simon G Krattinger, Ricardo H Ramirezgonzalez, Henkjan Schoonbeek, Erin Baggs, Agnieszka I Witek, Inderjit Singh Yadav, Ksenia V KrasilevaAbstract:This research was supported by the BBSRC (including BB/L011794/1, PRR-CROP BB/G024960/1, the Norwich Research Park Doctoral Training Grant BB/M011216/1, and the cross-institute strategic programmes Designing Future Wheat and Plant Health BB/P012574/1), the 2Blades Foundation, the Betty and Gordon Moore Foundation, and the Gatsby Foundation.
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Comparative analysis of plant Immune Receptor architectures uncovers host proteins likely targeted by pathogens
BMC Biology, 2016Co-Authors: Panagiotis F. Sarris, Jonathan D. G. Jones, Volkan Cevik, Gulay Dagdas, Ksenia V KrasilevaAbstract:Background Plants deploy Immune Receptors to detect pathogen-derived molecules and initiate defense responses. Intracellular plant Immune Receptors called nucleotide-binding leucine-rich repeat (NLR) proteins contain a central nucleotide-binding (NB) domain followed by a series of leucine-rich repeats (LRRs), and are key initiators of plant defense responses. However, recent studies demonstrated that NLRs with non-canonical domain architectures play an important role in plant immunity. These composite Immune Receptors are thought to arise from fusions between NLRs and additional domains that serve as “baits” for the pathogen-derived effector proteins, thus enabling pathogen recognition. Several names have been proposed to describe these proteins, including “integrated decoys” and “integrated sensors”. We adopt and argue for “integrated domains” or NLR-IDs, which describes the product of the fusion without assigning a universal mode of action. Results We have scanned available plant genome sequences for the full spectrum of NLR-IDs to evaluate the diversity of integrations of potential sensor/decoy domains across flowering plants, including 19 crop species. We manually curated wheat and brassicas and experimentally validated a subset of NLR-IDs in wild and cultivated wheat varieties. We have examined NLR fusions that occur in multiple plant families and identified that some domains show re-occurring integration across lineages. Domains fused to NLRs overlap with previously identified pathogen targets confirming that they act as baits for the pathogen. While some of the integrated domains have been previously implicated in disease resistance, others provide new targets for engineering durable resistance to plant pathogens. Conclusions We have built a robust reproducible pipeline for detecting variable domain architectures in plant Immune Receptors across species. We hypothesize that NLR-IDs that we revealed provide clues to the host proteins targeted by pathogens, and that this information can be deployed to discover new sources of disease resistance.
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comparative analysis of plant Immune Receptor architectures uncovers host proteins likely targeted by pathogens
BMC Biology, 2016Co-Authors: Jonathan D. G. Jones, Panagiotis F. Sarris, Volkan Cevik, Gulay Dagdas, Ksenia V KrasilevaAbstract:Plants deploy Immune Receptors to detect pathogen-derived molecules and initiate defense responses. Intracellular plant Immune Receptors called nucleotide-binding leucine-rich repeat (NLR) proteins contain a central nucleotide-binding (NB) domain followed by a series of leucine-rich repeats (LRRs), and are key initiators of plant defense responses. However, recent studies demonstrated that NLRs with non-canonical domain architectures play an important role in plant immunity. These composite Immune Receptors are thought to arise from fusions between NLRs and additional domains that serve as “baits” for the pathogen-derived effector proteins, thus enabling pathogen recognition. Several names have been proposed to describe these proteins, including “integrated decoys” and “integrated sensors”. We adopt and argue for “integrated domains” or NLR-IDs, which describes the product of the fusion without assigning a universal mode of action. We have scanned available plant genome sequences for the full spectrum of NLR-IDs to evaluate the diversity of integrations of potential sensor/decoy domains across flowering plants, including 19 crop species. We manually curated wheat and brassicas and experimentally validated a subset of NLR-IDs in wild and cultivated wheat varieties. We have examined NLR fusions that occur in multiple plant families and identified that some domains show re-occurring integration across lineages. Domains fused to NLRs overlap with previously identified pathogen targets confirming that they act as baits for the pathogen. While some of the integrated domains have been previously implicated in disease resistance, others provide new targets for engineering durable resistance to plant pathogens. We have built a robust reproducible pipeline for detecting variable domain architectures in plant Immune Receptors across species. We hypothesize that NLR-IDs that we revealed provide clues to the host proteins targeted by pathogens, and that this information can be deployed to discover new sources of disease resistance.
Yin Song - One of the best experts on this subject based on the ideXlab platform.
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broad taxonomic characterization of verticillium wilt resistance genes reveals an ancient origin of the tomato ve1 Immune Receptor
Molecular Plant Pathology, 2017Co-Authors: Yin Song, Zhao Zhang, Michael F Seidl, Aljaz Majer, Jernej Jakse, Branka Javornik, Bart P H J ThommaAbstract:Plant-pathogenic microbes secrete effector molecules to establish themselves on their hosts, whereas plants use Immune Receptors to try and intercept such effectors in order to prevent pathogen colonization. The tomato cell surface-localized Receptor Ve1 confers race-specific resistance against race 1 strains of the soil-borne vascular wilt fungus Verticillium dahliae which secrete the Ave1 effector. Here, we describe the cloning and characterization of Ve1 homologues from tobacco (Nicotiana glutinosa), potato (Solanum tuberosum), wild eggplant (Solanum torvum) and hop (Humulus lupulus), and demonstrate that particular Ve1 homologues govern resistance against V. dahliae race 1 strains through the recognition of the Ave1 effector. Phylogenetic analysis shows that Ve1 homologues are widely distributed in land plants. Thus, our study suggests an ancient origin of the Ve1 Immune Receptor in the plant kingdom.
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mutational analysis of the ve1 Immune Receptor that mediates verticillium resistance in tomato
PLOS ONE, 2014Co-Authors: Zhao Zhang, Yin Song, Chunming Liu, Bart P H J ThommaAbstract:Pathogenic Verticillium species are economically important plant pathogens that cause vascular wilt diseases in hundreds of plant species. The Ve1 gene of tomato confers resistance against race 1 strains of Verticillium dahliae and V. albo-atrum. Ve1 encodes an extracellular leucine-rich repeat (eLRR) Receptor-like protein (RLP) that serves as a cell surface Receptor for recognition of the recently identified secreted Verticillium effector Ave1. To investigate recognition of Ave1 by Ve1, alanine scanning was performed on the solvent exposed β-strand/β-turn residues across the eLRR domain of Ve1. In addition, alanine scanning was also employed to functionally characterize motifs that putatively mediate protein-protein interactions and endocytosis in the transmembrane domain and the cytoplasmic tail of the Ve1 protein. Functionality of the mutant proteins was assessed by screening for the occurrence of a hypersensitive response upon co-expression with Ave1 upon Agrobacterium tumefaciens-mediated transient expression (agroinfiltration). In order to confirm the agroinfiltration results, constructs encoding Ve1 mutants were transformed into Arabidopsis and the transgenes were challenged with race 1 Verticillium. Our analyses identified several regions of the Ve1 protein that are required for functionality.
Panagiotis F. Sarris - One of the best experts on this subject based on the ideXlab platform.
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The Nuclear Immune Receptor RPS4 Is Required for RRS1SLH1-Dependent Constitutive Defense Activation in
2016Co-Authors: Arabidopsis Thaliana, Panagiotis F. Sarris, Ghanasyam Rallapalli, Simon J Williams, Kee Hoon Sohn, Joo Yong Woo, Toby E. Newman, Kyung Hee Paek, Bostjan Kobe, Jonathan D. G. JonesAbstract:Plant nucleotide-binding leucine-rich repeat (NB-LRR) disease resistance (R) proteins recognize specific ‘‘avirulent’ ’ pathogen effectors and activate Immune responses. NB-LRR proteins structurally and functionally resemble mammalian Nod-like Receptors (NLRs). How NB-LRR and NLR proteins activate defense is poorly understood. The divergently transcribed Arabidopsis R genes, RPS4 (resistance to Pseudomonas syringae 4) and RRS1 (resistance to Ralstonia solanacearum 1), function together to confer recognition of Pseudomonas AvrRps4 and Ralstonia PopP2. RRS1 is the only known recessive NB-LRR R gene and encodes a WRKY DNA binding domain, prompting suggestions that it acts downstream of RPS4 for transcriptional activation of defense genes. We define here the early RRS1-dependent transcriptional changes upon delivery of PopP2 via Pseudomonas type III secretion. The Arabidopsis slh1 (sensitive to low humidity 1) mutant encodes an RRS1 allele (RRS1SLH1) with a single amino acid (leucine) insertion in the WRKY DNA-binding domain. Its poor growth due to constitutive defense activation is rescued at higher temperature. Transcription profiling data indicate that RRS1SLH1-mediated defense activation overlaps substantially with AvrRps4- and PopP2-regulated responses. To better understand the genetic basis of RPS4/RRS1-dependent immunity, we performed a genetic screen to identify suppressor of slh1 immunity (sushi) mutants. We show that many sushi mutants carry mutations in RPS4, suggesting that RPS4 acts downstream or in a complex with RRS1. Interestingly, several mutations were identified in a domain C-terminal to the RPS4 LRR domain. Usin
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Comparative analysis of plant Immune Receptor architectures uncovers host proteins likely targeted by pathogens
BMC Biology, 2016Co-Authors: Panagiotis F. Sarris, Jonathan D. G. Jones, Volkan Cevik, Gulay Dagdas, Ksenia V KrasilevaAbstract:Background Plants deploy Immune Receptors to detect pathogen-derived molecules and initiate defense responses. Intracellular plant Immune Receptors called nucleotide-binding leucine-rich repeat (NLR) proteins contain a central nucleotide-binding (NB) domain followed by a series of leucine-rich repeats (LRRs), and are key initiators of plant defense responses. However, recent studies demonstrated that NLRs with non-canonical domain architectures play an important role in plant immunity. These composite Immune Receptors are thought to arise from fusions between NLRs and additional domains that serve as “baits” for the pathogen-derived effector proteins, thus enabling pathogen recognition. Several names have been proposed to describe these proteins, including “integrated decoys” and “integrated sensors”. We adopt and argue for “integrated domains” or NLR-IDs, which describes the product of the fusion without assigning a universal mode of action. Results We have scanned available plant genome sequences for the full spectrum of NLR-IDs to evaluate the diversity of integrations of potential sensor/decoy domains across flowering plants, including 19 crop species. We manually curated wheat and brassicas and experimentally validated a subset of NLR-IDs in wild and cultivated wheat varieties. We have examined NLR fusions that occur in multiple plant families and identified that some domains show re-occurring integration across lineages. Domains fused to NLRs overlap with previously identified pathogen targets confirming that they act as baits for the pathogen. While some of the integrated domains have been previously implicated in disease resistance, others provide new targets for engineering durable resistance to plant pathogens. Conclusions We have built a robust reproducible pipeline for detecting variable domain architectures in plant Immune Receptors across species. We hypothesize that NLR-IDs that we revealed provide clues to the host proteins targeted by pathogens, and that this information can be deployed to discover new sources of disease resistance.
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comparative analysis of plant Immune Receptor architectures uncovers host proteins likely targeted by pathogens
BMC Biology, 2016Co-Authors: Jonathan D. G. Jones, Panagiotis F. Sarris, Volkan Cevik, Gulay Dagdas, Ksenia V KrasilevaAbstract:Plants deploy Immune Receptors to detect pathogen-derived molecules and initiate defense responses. Intracellular plant Immune Receptors called nucleotide-binding leucine-rich repeat (NLR) proteins contain a central nucleotide-binding (NB) domain followed by a series of leucine-rich repeats (LRRs), and are key initiators of plant defense responses. However, recent studies demonstrated that NLRs with non-canonical domain architectures play an important role in plant immunity. These composite Immune Receptors are thought to arise from fusions between NLRs and additional domains that serve as “baits” for the pathogen-derived effector proteins, thus enabling pathogen recognition. Several names have been proposed to describe these proteins, including “integrated decoys” and “integrated sensors”. We adopt and argue for “integrated domains” or NLR-IDs, which describes the product of the fusion without assigning a universal mode of action. We have scanned available plant genome sequences for the full spectrum of NLR-IDs to evaluate the diversity of integrations of potential sensor/decoy domains across flowering plants, including 19 crop species. We manually curated wheat and brassicas and experimentally validated a subset of NLR-IDs in wild and cultivated wheat varieties. We have examined NLR fusions that occur in multiple plant families and identified that some domains show re-occurring integration across lineages. Domains fused to NLRs overlap with previously identified pathogen targets confirming that they act as baits for the pathogen. While some of the integrated domains have been previously implicated in disease resistance, others provide new targets for engineering durable resistance to plant pathogens. We have built a robust reproducible pipeline for detecting variable domain architectures in plant Immune Receptors across species. We hypothesize that NLR-IDs that we revealed provide clues to the host proteins targeted by pathogens, and that this information can be deployed to discover new sources of disease resistance.
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A Plant Immune Receptor Detects Pathogen Effectors that Target WRKY Transcription Factors
Cell, 2015Co-Authors: Panagiotis F. Sarris, Zane Duxbury, Yan Ma, Cécile Segonzac, Jan Sklenar, Paul Derbyshire, Volkan Cevik, Ghanasyam Rallapalli, Simon B. SaucetAbstract:Defense against pathogens in multicellular eukaryotes depends on intracellular Immune Receptors, yet surveillance by these Receptors is poorly understood. Several plant nucleotide-binding, leucine-rich repeat (NB-LRR) Immune Receptors carry fusions with other protein domains. The Arabidopsis RRS1-R NB-LRR protein carries a C-terminal WRKY DNA binding domain and forms a Receptor complex with RPS4, another NB-LRR protein. This complex detects the bacterial effectors AvrRps4 or PopP2 and then activates defense. Both bacterial proteins interact with the RRS1 WRKY domain, and PopP2 acetylates lysines to block DNA binding. PopP2 and AvrRps4 interact with other WRKY domain-containing proteins, suggesting these effectors interfere with WRKY transcription factor-dependent defense, and RPS4/RRS1 has integrated a "decoy" domain that enables detection of effectors that target WRKY proteins. We propose that NB-LRR Receptor pairs, one member of which carries an additional protein domain, enable perception of pathogen effectors whose function is to target that domain.
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structural basis for assembly and function of a heterodimeric plant Immune Receptor
Science, 2014Co-Authors: Simon J Williams, Panagiotis F. Sarris, Cécile Segonzac, Simon B. Saucet, Kee Hoon Sohn, Li Wan, Maud Bernoux, Daniel J EricssonAbstract:Cytoplasmic plant Immune Receptors recognize specific pathogen effector proteins and initiate effector-triggered immunity. In Arabidopsis, the Immune Receptors RPS4 and RRS1 are both required to activate defense to three different pathogens. We show that RPS4 and RRS1 physically associate. Crystal structures of the N-terminal Toll–interleukin-1 Receptor/resistance (TIR) domains of RPS4 and RRS1, individually and as a heterodimeric complex (respectively at 2.05, 1.75, and 2.65 angstrom resolution), reveal a conserved TIR/TIR interaction interface. We show that TIR domain heterodimerization is required to form a functional RRS1/RPS4 effector recognition complex. The RPS4 TIR domain activates effector-independent defense, which is inhibited by the RRS1 TIR domain through the heterodimerization interface. Thus, RPS4 and RRS1 function as a Receptor complex in which the two components play distinct roles in recognition and signaling.
