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Volumn 16, Issue 1, 2004, Pages 48-62

Plant innate immunity - Direct and indirect recognition of general and specific pathogen-associated molecules

Author keywords

[No Author keywords available]

Indexed keywords

F BOX PROTEIN; HEAT SHOCK PROTEIN 90; PROTEIN; PROTEIN RAR1; PROTEIN SGT1; UNCLASSIFIED DRUG;

EID: 1042278906     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.coi.2003.11.016     Document Type: Review
Times cited : (266)

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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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    • The Arabidopsis mutant cev1 links cell wall signaling to jasmonate and ethylene responses
    • •] 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.
    • •] 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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    • Loss of a callose synthase results in salicylic acid-dependent disease resistance
    • 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.
    • 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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    • Flagellin from an incompatible strain of Pseudomonas avenae induces a resistance response in cultured rice cells
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    • 2 generation accompanying hypersensitive cell death and expression of PAL, Cht-1, and PBZ1, but not of Lox in rice
    • 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.
    • 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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    • The ΔfliD mutant of Pseudomonas syringae pv. tabaci, which secretes flagellin monomers, induces a strong hypersensitive reaction (HR) in non-host tomato cells
    • 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.
    • 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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    • Post-translational modification of flagellin determines the specificity of HR induction
    • 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.
    • 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.
    • (2003) Plant Cell Physiol. , vol.44 , pp. 342-349
    • Taguchi, F.1    Shimizu, R.2    Inagaki, Y.3    Toyoda, K.4    Shiraishi, T.5    Ichinose, Y.6
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    • Direct interaction of resistance gene and avirulence gene products confers rice blast resistance
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    • Plant disease-resistance proteins and the gene-for-gene concept
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    • RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in Arabidopsis
    • 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.
    • 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.
    • (2002) Cell , vol.108 , pp. 743-754
    • Mackey, D.1    Holt III, B.F.2    Wiig, A.3    Dangl, J.L.4
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    • Initiation of RPS2-specified disease resistance in Arabidopsis is coupled to the AvrRpt2-directed elimination of RIN4
    • ••], 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.
    • ••], 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.
    • (2003) Cell , vol.112 , pp. 369-377
    • Axtell, M.J.1    Staskawicz, B.J.2
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    • Arabidopsis RIN4 is a target of the type III virulence effector AvrRpt2 and modulates RPS2-mediated resistance
    • ••], 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.
    • ••], 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.
    • (2003) Cell , vol.112 , pp. 379-389
    • Mackey, D.1    Belkhadir, Y.2    Alonso, J.M.3    Ecker, J.R.4    Dangl, J.L.5
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    • The Arabidopsis PBS1 resistance gene encodes a member of a novel protein kinase subfamily
    • 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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    • Swiderski, M.R.1    Innes, R.W.2
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    • Cleavage of Arabidopsis PBS1 by a bacterial type III effector
    • •] 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.
    • •] 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.
    • (2003) Science , vol.301 , pp. 1230-1233
    • Shao, F.1    Golstein, C.2    Ade, J.3    Stoutemyer, M.4    Dixon, J.E.5    Innes, R.W.6
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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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    • A telomeric avirulence gene determines efficacy for the rice blast resistance gene Pi-ta
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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
    • 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.
    • 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.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 2404-2409
    • 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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    • Physical interaction between RRS1-R, a protein conferring resistance to bacterial wilt, and PopP2, a type III effector targeted to the plant nucleus
    • •] 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.
    • •] 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.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 8024-8029
    • 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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    • Interaction between domains of a plant NBS-LRR protein in disease resistance-related cell death
    • 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.
    • 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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    • 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.1    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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    • 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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    • Arabidopsis RPP4 is a member of the RPP5 multigene family of TIR-NB-LRR genes and confers downy mildew resistance through multiple signalling components
    • 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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    • Recognition specificity and RAR1/SGT1 dependence in barley Mla disease resistance genes to the powdery mildew fungus
    • 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.
    • 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.
    • (2003) Plant Cell , vol.15 , pp. 732-744
    • Shen, Q.-H.1    Zhou, F.2    Bieri, S.3    Haizel, T.4    Shirasu, K.5    Schulze-Lefert, P.6
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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
    • 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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    • Banerjee, D.1    Zhang, X.2    Bent, A.F.3
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    • The RAR1 interactor SGT1, an essential component of R gene-triggered disease resistance
    • 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.
    • 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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    • Azevedo, C.1    Sadanandom, A.2    Kitagawa, K.3    Freialdenhoven, A.4    Shirasu, K.5    Schulze-Lefert, P.6
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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.1    Schiff, M.2    Marathe, R.3    Dinesh-Kumar, S.P.4
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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
    • 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.
    • (2002) Plant Cell , vol.14 , pp. 1005-1015
    • Tornero, P.1    Merritt, P.2    Sadanandom, A.3    Shirasu, K.4    Innes, R.W.5    Dangl, J.L.6
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    • Role of ubiquitination in the regulation of plant defence against pathogens
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    • Resistance gene signaling in plants -complex similarities to animal innate immunity
    • Holt B.F. III, Hubert D.A., Dangl J.L. Resistance gene signaling in plants -complex similarities to animal innate immunity. Curr. Opin. Immunol. 15:2003;20-25.
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    • Complex formation, promiscuity and multi-functionality: Protein interactions in disease-resistance pathways
    • A stimulating review that postulates a chaperone function for RAR1 and SGT1, and introduces HSP90 as a new player in resistance signalling. It also reports unpublished data indicating interactions between HSP90 and both RAR1 and SGT1 in yeast two-hybrid analyses.
    • Shirasu K., Schulze-Lefert P. Complex formation, promiscuity and multi-functionality: protein interactions in disease-resistance pathways. Trends Plant Sci. 8:2003;252-258 A stimulating review that postulates a chaperone function for RAR1 and SGT1, and introduces HSP90 as a new player in resistance signalling. It also reports unpublished data indicating interactions between HSP90 and both RAR1 and SGT1 in yeast two-hybrid analyses.
    • (2003) Trends Plant Sci. , vol.8 , pp. 252-258
    • Shirasu, K.1    Schulze-Lefert, P.2
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    • Role of SCF ubiquitin-ligase and the COP9 signalosome in the N gene-mediated resistance response to tobacco mosaic virus
    • These authors report the isolation of Nicotiana benthamiana SGT1 and HSP90 as RAR1-interacting proteins in a yeast two-hybrid screen, and show that SKP1 interacts with SGT1 in a yeast two-hybrid analysis. Interactions between SGT1 and both RAR1 and SKP1 were confirmed by in vitro binding assays. Immunoprecipitation experiments show that RAR1 and SGT1 co-immunoprecipitate with one another, with SCF-E3 components SKP1 and CUL1, and with CSN component CSN4. Virus-induced gene silencing of SGT1, SKP1 and CSN components CSN3 and CSN8 compromised N gene-mediated resistance to TMV in N. benthamiana, suggesting both SCF-E3 and CSN complexes are required for N protein function. These data suggest that RAR1, SGT1, SCFE3 and CSN may form a single complex in N. benthamiana.
    • Liu Y., Schiff M., Serino G., Deng X.-W., Dinesh-Kumar S.P. Role of SCF ubiquitin-ligase and the COP9 signalosome in the N gene-mediated resistance response to tobacco mosaic virus. Plant Cell. 14:2002;1483-1496 These authors report the isolation of Nicotiana benthamiana SGT1 and HSP90 as RAR1-interacting proteins in a yeast two-hybrid screen, and show that SKP1 interacts with SGT1 in a yeast two-hybrid analysis. Interactions between SGT1 and both RAR1 and SKP1 were confirmed by in vitro binding assays. Immunoprecipitation experiments show that RAR1 and SGT1 co-immunoprecipitate with one another, with SCF-E3 components SKP1 and CUL1, and with CSN component CSN4. Virus-induced gene silencing of SGT1, SKP1 and CSN components CSN3 and CSN8 compromised N gene-mediated resistance to TMV in N. benthamiana, suggesting both SCF-E3 and CSN complexes are required for N protein function. These data suggest that RAR1, SGT1, SCFE3 and CSN may form a single complex in N. benthamiana.
    • (2002) Plant Cell , vol.14 , pp. 1483-1496
    • Liu, Y.1    Schiff, M.2    Serino, G.3    Deng, X.-W.4    Dinesh-Kumar, S.P.5
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    • The Arabidopsis thaliana RPM1 disease resistance gene product is a peripheral plasma membrane protein that is degraded coincident with the hypersensitive response
    • Boyes D.C., Nam J., Dangl J.L. The Arabidopsis thaliana RPM1 disease resistance gene product is a peripheral plasma membrane protein that is degraded coincident with the hypersensitive response. Proc. Natl. Acad. Sci. U.S.A. 95:1998;15849-15854.
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    • Sgt1p contributes to cyclic AMP pathway activity and physically interacts with the adenylyl cyclase Cyr1p/Cdc35p in budding yeast
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    • Schizosaccharomyces pombe Git7p, a member of the Saccharomyces cerevisiae Sgtlp family, is required for glucose and cyclic AMP signaling, cell wall integrity, and septation
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.