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A comprehensive and informative description of the full complement of RLK and RLP genes in the Arabidopsis genome including LRR-RLKs and LRR-RLPs.
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A 24 kDa cell-wall protein NPP1 (necrosis-inducing Phytophthora protein 1) was isolated from P. parasitica and shown to induce resistance responses in parsley, including defence gene expression, phytoalexin production, HR, ethylene production and MAPK (SIPK orthologue) activation. NPP1 was also able to induce cell death in tobacco and Arabidopsis, but not in maize and barley. NPP1 induction of Arabidopsis PR1 expression was compromised in nahG plants, and ndr1 and pad4 mutants, indicating that PR1 gene-induction was salicylic acid dependent and required both NDR1- and PAD4-mediated signalling.
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Fellbrich G., Romanski A., Varet A., Blume B., Brunner F., Engelhardt S., Felix G., Kemmerling B., Krzymowska M., Nürnberger T. NPP1, a Phytophthora-associated trigger of plant defence in parsley and Arabidopsis. Plant J. 32:2002;375-390 A 24 kDa cell-wall protein NPP1 (necrosis-inducing Phytophthora protein 1) was isolated from P. parasitica and shown to induce resistance responses in parsley, including defence gene expression, phytoalexin production, HR, ethylene production and MAPK (SIPK orthologue) activation. NPP1 was also able to induce cell death in tobacco and Arabidopsis, but not in maize and barley. NPP1 induction of Arabidopsis PR1 expression was compromised in nahG plants, and ndr1 and pad4 mutants, indicating that PR1 gene-induction was salicylic acid dependent and required both NDR1- and PAD4-mediated signalling.
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The authors of this paper identify the elicitor-active, cell-wall glycoprotein GP42 from Phytophthora as a transglutaminase and shows that the previously identified, 13 amino acid, elicitor-active component of this protein lies in the conserved catalytic site.
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Brunner F., Rosahl S., Lee J., Rudd J.J., Geiler C., Kauppinen S., Rasmussen G., Sheel D., Nürnberger T. Pep-13, a plant defense-inducing pathogen-associated pattern from Phytophthora transglutaminases. EMBO J. 21:2002;6681-6688 The authors of this paper identify the elicitor-active, cell-wall glycoprotein GP42 from Phytophthora as a transglutaminase and shows that the previously identified, 13 amino acid, elicitor-active component of this protein lies in the conserved catalytic site.
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AvrPtoB is a type III effector detected by Pto in tomato, but not in Nicotiana benthamiana. Transient co-expression of AvrPtoB in N. benthamiana inhibited HR induced by Pto-AvrPto or Cf-9-Avr9 interactions. AvrPtoB also suppressed oxidative and heat-stress-induced cell death in yeast, suggesting that AvrPtoB might be a universal inhibitor of cell death.
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Abramovitch R.B., Kim Y.-J., Chen S., Dickman M.B., Matrin G.B. Pseudomonas type III effector AvrPtoB induces plant disease susceptibility by inhibition of host programmed cell death. EMBO J. 22:2003;60-69 AvrPtoB is a type III effector detected by Pto in tomato, but not in Nicotiana benthamiana. Transient co-expression of AvrPtoB in N. benthamiana inhibited HR induced by Pto-AvrPto or Cf-9-Avr9 interactions. AvrPtoB also suppressed oxidative and heat-stress-induced cell death in yeast, suggesting that AvrPtoB might be a universal inhibitor of cell death.
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Natural disulfide bond-disrupted mutants of AVR4 of the tomato pathogen Cladosporium fulvum are sensitive to proteolysis, circumvent Cf-4-mediated resistance, but retain their chitin binding ability
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Avr4, an extracellular Avr protein produced by the leaf mould fungus, Cladosporium fulvum, and detected by the tomato Cf-4 LRR-RLP protein, has chitin-binding activity thought to protect chitin in the fungal cell wall from degradation by plant chitinases. Most natural C. fulvum isolates, virulent on Cf-4 tomato, possesses Avr4 alleles with cysteine to tyrosine substitutions disrupting disulphide bonds, resulting in greater sensitivity to proteolysis in the intercellular spaces of tomato plants. However, these natural isoforms of Avr4 still retain chitin-binding activity, which appears to protect them from degradation. These results indicate selection has been imposed for Avr4 variants that avoid recognition by Cf-4, but retain chitin-binding ability, suggesting chitin protection may be an important function of Avr4.
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van den Burg H.A., Westerink N., Francoijs K.-J., Roth R., Woestenenk E., Boeren S., de Wit P.J.G.M., Joosten M.H.A.J., Vervoort J. Natural disulfide bond-disrupted mutants of AVR4 of the tomato pathogen Cladosporium fulvum are sensitive to proteolysis, circumvent Cf-4-mediated resistance, but retain their chitin binding ability. J. Biol. Chem. 278:2003;27340-27346 Avr4, an extracellular Avr protein produced by the leaf mould fungus, Cladosporium fulvum, and detected by the tomato Cf-4 LRR-RLP protein, has chitin-binding activity thought to protect chitin in the fungal cell wall from degradation by plant chitinases. Most natural C. fulvum isolates, virulent on Cf-4 tomato, possesses Avr4 alleles with cysteine to tyrosine substitutions disrupting disulphide bonds, resulting in greater sensitivity to proteolysis in the intercellular spaces of tomato plants. However, these natural isoforms of Avr4 still retain chitin-binding activity, which appears to protect them from degradation. These results indicate selection has been imposed for Avr4 variants that avoid recognition by Cf-4, but retain chitin-binding ability, suggesting chitin protection may be an important function of Avr4.
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Using virus-induced gene silencing in Nicotiana benthamiana, this paper shows that silencing of SGT1 compromised N, Rx and Pto R gene-mediated pathogen resistance, HR induced by transient expression of Rx, Pto, Cf-4 and Cf-9 R genes and their cognate Avr genes, HR induced by transient expression of the RPW8 R gene, the AvrRpt2 Avr gene or the Inf1 elicitin gene, and non-host resistance to Pseudomonas syringae pv. maculicola and Xanthomonas axonopodis pv. vesicatoria, but not X. campestris pv. campestris or cauliflower mosaic virus. The broad requirement for SGT1 in N. benthamiana suggests it may be involved in a shared signalling pathway.
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Peart J.R., Lu R., Sadanandom A., Malcuit I., Moffett P., Brice D.C., Schauser L., Jaggard D.A.W., Xiao S., Coleman M.J.et al. Ubiquitin ligase-associated protein SGT1 is required for host and nonhost disease resistance in plants. Proc. Natl. Acad. Sci. U.S.A. 99:2002;10865-10869 Using virus-induced gene silencing in Nicotiana benthamiana, this paper shows that silencing of SGT1 compromised N, Rx and Pto R gene-mediated pathogen resistance, HR induced by transient expression of Rx, Pto, Cf-4 and Cf-9 R genes and their cognate Avr genes, HR induced by transient expression of the RPW8 R gene, the AvrRpt2 Avr gene or the Inf1 elicitin gene, and non-host resistance to Pseudomonas syringae pv. maculicola and Xanthomonas axonopodis pv. vesicatoria, but not X. campestris pv. campestris or cauliflower mosaic virus. The broad requirement for SGT1 in N. benthamiana suggests it may be involved in a shared signalling pathway.
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The authors of this paper report the synergistic roles of the actin cytoskeleton and the resistance signalling protein EDS1 on non-host resistance, showing that the combination of an actin-polymerisation inhibitor and the eds1 mutation allows a wheat pathogen to complete its lifecycle on Arabidopsis, a non-host plant.
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Yun B.-W., Atkinson H.A., Gaborit C., Greenland A., Read N.D., Pallas J.A., Loake G.J. Loss of actin cytoskeletal function and EDS1 activity, in combination, severely compromises non-host resistance in Arabidopsis against wheat powdery mildew. Plant J. 34:2003;768-777 The authors of this paper report the synergistic roles of the actin cytoskeleton and the resistance signalling protein EDS1 on non-host resistance, showing that the combination of an actin-polymerisation inhibitor and the eds1 mutation allows a wheat pathogen to complete its lifecycle on Arabidopsis, a non-host plant.
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•] mutants have mutations in a conserved domain of the cellulose synthase gene CESA3, leading to aberrant deposition of lignin, reduced cell expansion and enhanced resistance to powdery mildew pathogens. In cev1 and eli1-1 mutants, jasmonic acid (JA)- and ethylene-mediated defence gene expression is activated, and treatment with both JA and 1-aminocyclopropane-1-carboxylic acid (an ethylene precursor) reproduced their phenotypes in wild-type plants. These results indicate that reduced cellulose synthesis activates JA and ethylene signal transduction and leads to defence gene expression.
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•] mutants have mutations in a conserved domain of the cellulose synthase gene CESA3, leading to aberrant deposition of lignin, reduced cell expansion and enhanced resistance to powdery mildew pathogens. In cev1 and eli1-1 mutants, jasmonic acid (JA)- and ethylene-mediated defence gene expression is activated, and treatment with both JA and 1-aminocyclopropane-1- carboxylic acid (an ethylene precursor) reproduced their phenotypes in wild-type plants. These results indicate that reduced cellulose synthesis activates JA and ethylene signal transduction and leads to defence gene expression.
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The Arabidopsis pmr4 (powdery mildew resistant) mutant shows resistance to various biotrophic pathogens, including Erysiphe cichoracearum, E. oronti and Peronospora parasitica, and produces less callose in response to pathogen infection and wounding. PMR4 encodes a biosynthetic enzyme that appears to be responsible for stress-related callose deposition. Salicylic acid (SA)- and pathogen-responsive genes were upregulated in pmr4 plants, but mutations in the SA signalling pathway abolished or reduced pmr4-induced resistance.
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Nishialra M.T., Stein M., Hou B.-H., Vogel J.P., Edwards H., Somerville S.C. Loss of a callose synthase results in salicylic acid-dependent disease resistance. Science. 301:2003;969-972 The Arabidopsis pmr4 (powdery mildew resistant) mutant shows resistance to various biotrophic pathogens, including Erysiphe cichoracearum, E. oronti and Peronospora parasitica, and produces less callose in response to pathogen infection and wounding. PMR4 encodes a biosynthetic enzyme that appears to be responsible for stress-related callose deposition. Salicylic acid (SA)- and pathogen-responsive genes were upregulated in pmr4 plants, but mutations in the SA signalling pathway abolished or reduced pmr4-induced resistance.
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Che F.-S., Nakajima Y., Tanaka N., Iwano M., Yoshida T., Takayama S., Kadota I., Isogai A. Flagellin from an incompatible strain of Pseudomonas avenae induces a resistance response in cultured rice cells. J. Biol. Chem. 275:2000;32347-32356.
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Kadota, I.7
Isogai, A.8
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37
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0037406659
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2 generation accompanying hypersensitive cell death and expression of PAL, Cht-1, and PBZ1, but not of Lox in rice
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Flagellin from a non-pathogenic strain, but not a pathogenic strain, of bacteria was able to induce an HR and some pathogen-response genes in rice, but despite the inability to induce an HR, a flagellin-deficient non-pathogenic strain remained non pathogenic and retained the ability to induce pathogen-response genes. This indicates that flagellin detection contributes to pathogen recognition, but is not the only contributing factor.
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2 generation accompanying hypersensitive cell death and expression of PAL, Cht-1, and PBZ1, but not of Lox in rice. Mol. Plant Microbe Interact. 16:2003;422-428 Flagellin from a non-pathogenic strain, but not a pathogenic strain, of bacteria was able to induce an HR and some pathogen-response genes in rice, but despite the inability to induce an HR, a flagellin-deficient non-pathogenic strain remained non pathogenic and retained the ability to induce pathogen-response genes. This indicates that flagellin detection contributes to pathogen recognition, but is not the only contributing factor.
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Mol. Plant Microbe Interact
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Tanaka, N.1
Che, F.-S.2
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Isogai, A.6
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38
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0013147211
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The ΔfliD mutant of Pseudomonas syringae pv. tabaci, which secretes flagellin monomers, induces a strong hypersensitive reaction (HR) in non-host tomato cells
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This paper describes a role for detection of flagellin monomers in non-host resistance by showing that bacterial mutants unable to produce flagellin became pathogenic on tomato, whereas those producing flagellin monomers but unable to assemble flagella caused an enhanced resistance response.
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Shimizu R., Taguchi F., Marutani M., Mukaihara T., Inagaki Y., Toyoda K., Shiraishi T., Ichinose Y. The ΔfliD mutant of Pseudomonas syringae pv. tabaci, which secretes flagellin monomers, induces a strong hypersensitive reaction (HR) in non-host tomato cells. Mol. Genet Genomics. 269:2003;21-30 This paper describes a role for detection of flagellin monomers in non-host resistance by showing that bacterial mutants unable to produce flagellin became pathogenic on tomato, whereas those producing flagellin monomers but unable to assemble flagella caused an enhanced resistance response.
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Mol. Genet Genomics.
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Shimizu, R.1
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Toyoda, K.6
Shiraishi, T.7
Ichinose, Y.8
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39
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0037361893
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Post-translational modification of flagellin determines the specificity of HR induction
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This paper highlights the role of post-translational modification of otherwise sequence-identical flagellins from pathogenic and non-pathogenic bacteria, most likely by differential glycosylation, in avoiding or allowing their detection by tobacco plants.
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Taguchi F., Shimizu R., Inagaki Y., Toyoda K., Shiraishi T., Ichinose Y. Post-translational modification of flagellin determines the specificity of HR induction. Plant Cell Physiol. 44:2003;342-349 This paper highlights the role of post-translational modification of otherwise sequence-identical flagellins from pathogenic and non-pathogenic bacteria, most likely by differential glycosylation, in avoiding or allowing their detection by tobacco plants.
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Plant Cell Physiol.
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Taguchi, F.1
Shimizu, R.2
Inagaki, Y.3
Toyoda, K.4
Shiraishi, T.5
Ichinose, Y.6
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40
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Direct interaction of resistance gene and avirulence gene products confers rice blast resistance
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Jia Y., McAdams S.A., Bryan G.T., Hershey H.P., Valent B. Direct interaction of resistance gene and avirulence gene products confers rice blast resistance. EMBO J. 19:2000;4004-4014.
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Jia, Y.1
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Plant disease-resistance proteins and the gene-for-gene concept
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Van der Biezen E.A., Jones J.D.G. Plant disease-resistance proteins and the gene-for-gene concept. Trends Biochem. Sci. 23:1998;454-456.
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0037155687
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RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in Arabidopsis
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The authors identify RIN4 from a yeast two-hybrid screen using AvrB as bait and shows that RIN4 interacts with the amino terminus of RPM1 by yeast two-hybrid analysis and could be co-immunoprecipitated with RPM1, AvrB and AvrRpm1. They also show that AvrB and AvrRpm1 cause RPM1-independent phosphorylation of RIN4, and that a reduction in RIN4 expression causes reduction in RPM1 protein levels, but not vice versa.
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Mackey D., Holt B.F. III, Wiig A., Dangl J.L. RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in Arabidopsis. Cell. 108:2002;743-754 The authors identify RIN4 from a yeast two-hybrid screen using AvrB as bait and shows that RIN4 interacts with the amino terminus of RPM1 by yeast two-hybrid analysis and could be co-immunoprecipitated with RPM1, AvrB and AvrRpm1. They also show that AvrB and AvrRpm1 cause RPM1-independent phosphorylation of RIN4, and that a reduction in RIN4 expression causes reduction in RPM1 protein levels, but not vice versa.
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Cell
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Mackey, D.1
Holt III, B.F.2
Wiig, A.3
Dangl, J.L.4
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43
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0037423390
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Initiation of RPS2-specified disease resistance in Arabidopsis is coupled to the AvrRpt2-directed elimination of RIN4
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••], this paper shows that RPS2 co-immunoprecipitates with RIN4 and that AvrRpt2 causes RPS2-independent degradation of RIN4, resulting in the activation of RPS2. It also shows that RPS2 levels do not change with RPS2 or RPM1 activation and that AvrRpt2-induced degradation of RIN4 is RAR1 independent.
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••], this paper shows that RPS2 co-immunoprecipitates with RIN4 and that AvrRpt2 causes RPS2-independent degradation of RIN4, resulting in the activation of RPS2. It also shows that RPS2 levels do not change with RPS2 or RPM1 activation and that AvrRpt2-induced degradation of RIN4 is RAR1 independent.
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Cell
, vol.112
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Axtell, M.J.1
Staskawicz, B.J.2
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44
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0037423306
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Arabidopsis RIN4 is a target of the type III virulence effector AvrRpt2 and modulates RPS2-mediated resistance
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••], this paper shows that RPS2 co-immunoprecipitates with RIN4 and that AvrRpt2 causes RPS2-independent degradation of RIN4 resulting in the activation of RPS2. It also shows that overexpression of RIN4 blocks RPS2 signalling but does not affect RPM1 signalling, and that elimination of RIN4 eliminates RPM1 signalling.
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••], this paper shows that RPS2 co-immunoprecipitates with RIN4 and that AvrRpt2 causes RPS2-independent degradation of RIN4 resulting in the activation of RPS2. It also shows that overexpression of RIN4 blocks RPS2 signalling but does not affect RPM1 signalling, and that elimination of RIN4 eliminates RPM1 signalling.
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Cell
, vol.112
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Mackey, D.1
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Alonso, J.M.3
Ecker, J.R.4
Dangl, J.L.5
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45
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0034990117
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The Arabidopsis PBS1 resistance gene encodes a member of a novel protein kinase subfamily
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Swiderski M.R., Innes R.W. The Arabidopsis PBS1 resistance gene encodes a member of a novel protein kinase subfamily. Plant J. 26:2001;101-112.
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47
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0042322616
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Cleavage of Arabidopsis PBS1 by a bacterial type III effector
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•] is also responsible for the RPS5- and RAR1-independent cleavage of the protein kinase PBS1 in the activation segment of the kinase domain, leading to its kinase-activity- dependent recognition by RPS5.
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•] is also responsible for the RPS5- and RAR1-independent cleavage of the protein kinase PBS1 in the activation segment of the kinase domain, leading to its kinase-activity-dependent recognition by RPS5.
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Science
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Shao, F.1
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48
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Characterization of the Pseudomonas syringae pv. tomato AvrRpt2 protein: Demonstration of secretion and processing during bacterial pathogenesis
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Mudgett M.B., Staskawicz B.J. Characterization of the Pseudomonas syringae pv. tomato AvrRpt2 protein: demonstration of secretion and processing during bacterial pathogenesis. Mol. Microbiol. 32:1999;927-941.
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Orbach M.J., Farrall L., Sweigard J.A., Chumley F.G., Valent B. A telomeric avirulence gene determines efficacy for the rice blast resistance gene Pi-ta. Plant Cell. 12:2000;2019-2032.
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Plant Cell
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Orbach, M.J.1
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Valent, B.5
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50
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0037133245
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Resistance to Ralstonia solanacearum in Arabidopsis thaliana is conferred by the recessive RRS1-R gene, a member of a novel family of resistance genes
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This paper reports the identification of RRS1-R as a novel TIR-NBS-LRR protein containing a potential nuclear localisation signal (NLS) and a carboxy-terminal WRKY domain, which may function as a direct link to transcriptional activation of resistance effector genes. However, the functionality of either the NLS or the WRKY domain was not established. This may be an example of the principle that physical linkage of protein domains separated in other systems indicates physical interaction between the domains, however the combination of TIR-NBS-LRR and WRKY domains in RRS1 could also be a unique variation rather than a guiding principle. Resistance conferred by RRS-1R is also novel because it is shown to be dependent on NDR1, which hitherto has been associated almost exclusively with genes encoding CC-NBS-LRR proteins.
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Deslandes L., Olivier J., Theulières F., Hirsch J., Feng D.X., Bittner-Eddy P., Beynon J., Marco Y. Resistance to Ralstonia solanacearum in Arabidopsis thaliana is conferred by the recessive RRS1-R gene, a member of a novel family of resistance genes. Proc. Natl. Acad. Sci. U.S.A. 99:2002;2404-2409 This paper reports the identification of RRS1-R as a novel TIR-NBS-LRR protein containing a potential nuclear localisation signal (NLS) and a carboxy-terminal WRKY domain, which may function as a direct link to transcriptional activation of resistance effector genes. However, the functionality of either the NLS or the WRKY domain was not established. This may be an example of the principle that physical linkage of protein domains separated in other systems indicates physical interaction between the domains, however the combination of TIR-NBS-LRR and WRKY domains in RRS1 could also be a unique variation rather than a guiding principle. Resistance conferred by RRS-1R is also novel because it is shown to be dependent on NDR1, which hitherto has been associated almost exclusively with genes encoding CC-NBS-LRR proteins.
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(2002)
Proc. Natl. Acad. Sci. U.S.A.
, vol.99
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Deslandes, L.1
Olivier, J.2
Theulières, F.3
Hirsch, J.4
Feng, D.X.5
Bittner-Eddy, P.6
Beynon, J.7
Marco, Y.8
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51
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0037595606
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Physical interaction between RRS1-R, a protein conferring resistance to bacterial wilt, and PopP2, a type III effector targeted to the plant nucleus
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•] as PopP2, a type III effector protein of the YopJ/AvrRxv protein family. Direct interaction between PopP2 and both RRS1-R and RRS1-S (which does not confer resistance) is shown using a yeast split-ubiquitin two-hybrid system. Tagging with fluorescent proteins revealed that PopP2 carries a functional nuclear localisation signal (NLS) and forms a nuclear localised complex with both RRS1-R and RRS1-S, suggesting that delivery of the WRKY domain to the nucleus where it might act as a transcriptional activator is not, by itself, sufficient for resistance. Neither fluorescent-protein-tagged RRS-1R nor RRS1-S could be detected alone, but could be detected in a cytosolic complex with a derivative of PopP2 lacking a NLS, suggesting that the potential NLS in RRS1 may not be functional.
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•] as PopP2, a type III effector protein of the YopJ/AvrRxv protein family. Direct interaction between PopP2 and both RRS1-R and RRS1-S (which does not confer resistance) is shown using a yeast split-ubiquitin two-hybrid system. Tagging with fluorescent proteins revealed that PopP2 carries a functional nuclear localisation signal (NLS) and forms a nuclear localised complex with both RRS1-R and RRS1-S, suggesting that delivery of the WRKY domain to the nucleus where it might act as a transcriptional activator is not, by itself, sufficient for resistance. Neither fluorescent-protein-tagged RRS-1R nor RRS1-S could be detected alone, but could be detected in a cytosolic complex with a derivative of PopP2 lacking a NLS, suggesting that the potential NLS in RRS1 may not be functional.
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(2003)
Proc. Natl. Acad. Sci. U.S.A.
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Deslandes, L.1
Olivier, J.2
Peeters, N.3
Feng, D.X.4
Khounlotham, M.5
Boucher, C.6
Somssich, I.7
Genin, S.8
Marco, Y.9
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54
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Interaction between domains of a plant NBS-LRR protein in disease resistance-related cell death
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This paper reports the physical interaction and functional complementation of separated domains of the Rx CC-NBS-LRR protein transiently expressed in N. benthamiana. It also describes the clever use of virus-induced gene silencing of SGT1 to allow immunoprecipitation of epitope-tagged Rx protein domains following co-expression of the cognate Avr protein, which would otherwise trigger destructive resistance responses. The data obtained suggest intramolecular interaction of the CC and LRR domains with different subregions of the NBS domain (or differential control of intramolecular interaction by the ATP-binding subregion) and that the cognate Avr protein disrupts these interactions leading to Rx activation.
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Moffett P., Farnham G., Peart J., Baulcombe D.C. Interaction between domains of a plant NBS-LRR protein in disease resistance-related cell death. EMBO J. 21:2002;4511-4519 This paper reports the physical interaction and functional complementation of separated domains of the Rx CC-NBS-LRR protein transiently expressed in N. benthamiana. It also describes the clever use of virus-induced gene silencing of SGT1 to allow immunoprecipitation of epitope-tagged Rx protein domains following co-expression of the cognate Avr protein, which would otherwise trigger destructive resistance responses. The data obtained suggest intramolecular interaction of the CC and LRR domains with different subregions of the NBS domain (or differential control of intramolecular interaction by the ATP-binding subregion) and that the cognate Avr protein disrupts these interactions leading to Rx activation.
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EMBO J.
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Moffett, P.1
Farnham, G.2
Peart, J.3
Baulcombe, D.C.4
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Leucine-rich repeat-mediated intramolecular interactions in nematode recognition and cell death signaling by the tomato resistance protein Mi
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Hwang C.F., Williamson V.M. Leucine-rich repeat-mediated intramolecular interactions in nematode recognition and cell death signaling by the tomato resistance protein Mi. Plant J. 34:2003;585-593.
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Williamson, V.M.2
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Regions outside of the leucine-rich repeats of flax rust resistance proteins play a role in specificity determination
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Luck J.E., Lawrence G.J., Dodds P.N., Shepherd K.W., Ellis J.G. Regions outside of the leucine-rich repeats of flax rust resistance proteins play a role in specificity determination. Plant Cell. 12:2000;1367-1377.
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Plant Cell
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Luck, J.E.1
Lawrence, G.J.2
Dodds, P.N.3
Shepherd, K.W.4
Ellis, J.G.5
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57
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0032170811
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A mutation within the leucine-rich repeat domain of the Arabidopsis disease resistance gene RPS5 partially suppresses multiple bacterial and downy mildew resistance genes
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Warren R.F., Henk A., Mowery P., Holub E., Innes R.W. A mutation within the leucine-rich repeat domain of the Arabidopsis disease resistance gene RPS5 partially suppresses multiple bacterial and downy mildew resistance genes. Plant Cell. 10:1998;1439-1452.
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Plant Cell
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Warren, R.F.1
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Mowery, P.3
Holub, E.4
Innes, R.W.5
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58
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0036008975
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Arabidopsis RPP4 is a member of the RPP5 multigene family of TIR-NB-LRR genes and confers downy mildew resistance through multiple signalling components
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van der Biezen E.A., Freddie C.T., Kahn K., Parker J.E., Jones J.D.G. Arabidopsis RPP4 is a member of the RPP5 multigene family of TIR-NB-LRR genes and confers downy mildew resistance through multiple signalling components. Plant J. 29:2002;439-451.
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Plant J.
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Van Der Biezen, E.A.1
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Jones, J.D.G.5
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59
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0242669338
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Recognition specificity and RAR1/SGT1 dependence in barley Mla disease resistance genes to the powdery mildew fungus
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RAR1 and SGT1 dependence of MLA6 can be separated from recognition specificity by domain swaps with MLA1, which does not depend on RAR1 and SGT1, resulting in a RAR1- and SGT1-independent version of MLA6. However, the reciprocal swap, rather than creating a RAR1- and SGT1-dependent version of MLA1, produced a non-functional R protein. RAR1 and SGT1 dependence was found to be determined by LRRs 2-7 of MLA6, which could indicate a region of physical interaction, but could also indicate an unstable region requiring greater assistance in folding, given that RAR1, SGT1 and HSP90 may form a chaperone complex.
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Shen Q.-H., Zhou F., Bieri S., Haizel T., Shirasu K., Schulze-Lefert P. Recognition specificity and RAR1/SGT1 dependence in barley Mla disease resistance genes to the powdery mildew fungus. Plant Cell. 15:2003;732-744 RAR1 and SGT1 dependence of MLA6 can be separated from recognition specificity by domain swaps with MLA1, which does not depend on RAR1 and SGT1, resulting in a RAR1- and SGT1-independent version of MLA6. However, the reciprocal swap, rather than creating a RAR1- and SGT1-dependent version of MLA1, produced a non-functional R protein. RAR1 and SGT1 dependence was found to be determined by LRRs 2-7 of MLA6, which could indicate a region of physical interaction, but could also indicate an unstable region requiring greater assistance in folding, given that RAR1, SGT1 and HSP90 may form a chaperone complex.
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(2003)
Plant Cell
, vol.15
, pp. 732-744
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Shen, Q.-H.1
Zhou, F.2
Bieri, S.3
Haizel, T.4
Shirasu, K.5
Schulze-Lefert, P.6
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60
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The leucine-rich repeat domain can determine effective interaction between RPS2 and other host factors in Arabidopsis RPS2-mediated disease resistance
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Banerjee D., Zhang X., Bent A.F. The leucine-rich repeat domain can determine effective interaction between RPS2 and other host factors in Arabidopsis RPS2-mediated disease resistance. Genetics. 158:2001;439-450.
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Genetics
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Banerjee, D.1
Zhang, X.2
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Regulatory role of SGT1 in early R gene-mediated plant defenses
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Austin M.J., Muskett P., Kahn K., Feys B.J., Jones J.D.G., Parker J.E. Regulatory role of SGT1 in early R gene-mediated plant defenses. Science. 295:2002;2077-2080.
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Science
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Austin, M.J.1
Muskett, P.2
Kahn, K.3
Feys, B.J.4
Jones, J.D.G.5
Parker, J.E.6
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62
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0037086007
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The RAR1 interactor SGT1, an essential component of R gene-triggered disease resistance
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These authors report the isolation of barley SGT1 as a RAR1 interacting protein in a yeast two-hybrid screen. They also use gene silencing and pathogen infection to demonstrate that MLA6 requires SGT1, but MLA1 does not, in line with their RAR1 requirements. Immunoprecipitation experiments show that RAR1 and SGT1 co-immunoprecipitate with one another and that SGT1 co-immunoprecipitates with SCF-E3 components SKP1 and CUL1, but RAR1 does not, whereas both co-immunoprecipitate with CSN components CSN4 and CSN5. These data suggest that there may be at least two different kinds of SGT1 complex in barley.
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Azevedo C., Sadanandom A., Kitagawa K., Freialdenhoven A., Shirasu K., Schulze-Lefert P. The RAR1 interactor SGT1, an essential component of R gene-triggered disease resistance. Science. 295:2002;2073-2076 These authors report the isolation of barley SGT1 as a RAR1 interacting protein in a yeast two-hybrid screen. They also use gene silencing and pathogen infection to demonstrate that MLA6 requires SGT1, but MLA1 does not, in line with their RAR1 requirements. Immunoprecipitation experiments show that RAR1 and SGT1 co-immunoprecipitate with one another and that SGT1 co-immunoprecipitates with SCF-E3 components SKP1 and CUL1, but RAR1 does not, whereas both co-immunoprecipitate with CSN components CSN4 and CSN5. These data suggest that there may be at least two different kinds of SGT1 complex in barley.
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(2002)
Science
, vol.295
, pp. 2073-2076
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Azevedo, C.1
Sadanandom, A.2
Kitagawa, K.3
Freialdenhoven, A.4
Shirasu, K.5
Schulze-Lefert, P.6
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63
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0036015061
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Tobacco Rar1, EDS1 and NPR1/NIM1 like genes are required for N-mediated resistance to tobacco mosaic virus
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Liu Y., Schiff M., Marathe R., Dinesh-Kumar S.P. Tobacco Rar1, EDS1 and NPR1/NIM1 like genes are required for N-mediated resistance to tobacco mosaic virus. Plant J. 30:2002;415-429.
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Liu, Y.1
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0036016432
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Arabidopsis RAR1 exerts rate-limiting control of R gene-mediated defenses against multiple pathogens
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Muskett P.R., Kahn K., Austin M.J., Moisan L.J., Sadanandom A., Shirasu K., Jones J.D.G., Parker J.E. Arabidopsis RAR1 exerts rate-limiting control of R gene-mediated defenses against multiple pathogens. Plant Cell. 14:2002;979-992.
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Plant Cell
, vol.14
, pp. 979-992
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Muskett, P.R.1
Kahn, K.2
Austin, M.J.3
Moisan, L.J.4
Sadanandom, A.5
Shirasu, K.6
Jones, J.D.G.7
Parker, J.E.8
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65
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0036016433
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Arabidopsis SGT1b is required for defense signaling conferred by several downy mildew resistance genes
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Tör M., Gordon P., Cuzick A., Eulgem T., Sinapidou E., Mert-Türk F., Can C., Dangl J.L., Holub E.B. Arabidopsis SGT1b is required for defense signaling conferred by several downy mildew resistance genes. Plant Cell. 14:2002;993-1003.
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(2002)
Plant Cell
, vol.14
, pp. 993-1003
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Tör, M.1
Gordon, P.2
Cuzick, A.3
Eulgem, T.4
Sinapidou, E.5
Mert-Türk, F.6
Can, C.7
Dangl, J.L.8
Holub, E.B.9
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66
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0036016434
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RAR1 and NDR1 contribute quantitatively to disease resistance in Arabidopsis, and their relative contributions are dependent on the R gene assayed
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Tornero P., Merritt P., Sadanandom A., Shirasu K., Innes R.W., Dangl J.L. RAR1 and NDR1 contribute quantitatively to disease resistance in Arabidopsis, and their relative contributions are dependent on the R gene assayed. Plant Cell. 14:2002;1005-1015.
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Plant Cell
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Tornero, P.1
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