메뉴 건너뛰기




Volumn 17, Issue 4, 2005, Pages 1292-1305

Molecular basis for the RIN4 negative regulation of RPS2 disease resistance

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; DISEASES; MOLECULAR DYNAMICS; PLANTS (BOTANY);

EID: 17644376794     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.104.030163     Document Type: Article
Times cited : (133)

References (40)
  • 1
    • 0141566396 scopus 로고    scopus 로고
    • Genetic and molecular evidence that the Pseudomonas syringae type III effector protein AvrRpt2 is a cysteine protease
    • Axtell, M.J., Chisholm, S.T., Dahlbeck, D., and Staskawicz, B.J. (2003). Genetic and molecular evidence that the Pseudomonas syringae type III effector protein AvrRpt2 is a cysteine protease. Mol. Microbiol. 49, 1537-1546.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1537-1546
    • Axtell, M.J.1    Chisholm, S.T.2    Dahlbeck, D.3    Staskawicz, B.J.4
  • 2
    • 0037423390 scopus 로고    scopus 로고
    • Initiation of RPS2-specified disease resistance in Arabidopsis is coupled to the AvrRpt2-directed elimination of RIN4
    • Axtell, M.J., and Staskawicz, B.J. (2003). Initiation of RPS2-specified disease resistance in Arabidopsis is coupled to the AvrRpt2-directed elimination of RIN4. Cell 112, 369-377.
    • (2003) Cell , vol.112 , pp. 369-377
    • Axtell, M.J.1    Staskawicz, B.J.2
  • 3
    • 10344257928 scopus 로고    scopus 로고
    • Arabidopsis RIN4 negatively regulates disease resistance mediated by RPS2 and RPM1 downstream or independent of the NDR1 signal modulator and is not required for the virulence functions of bacterial type III effectors AvrRpt2 or AvrRpm1
    • Belkhadir, Y., Nimchuk, Z., Hubert, D.A., Mackey, D., and Dangl, J.L. (2004a). Arabidopsis RIN4 negatively regulates disease resistance mediated by RPS2 and RPM1 downstream or independent of the NDR1 signal modulator and is not required for the virulence functions of bacterial type III effectors AvrRpt2 or AvrRpm1. Plant Cell 16, 2822-2835.
    • (2004) Plant Cell , vol.16 , pp. 2822-2835
    • Belkhadir, Y.1    Nimchuk, Z.2    Hubert, D.A.3    Mackey, D.4    Dangl, J.L.5
  • 4
    • 3042762926 scopus 로고    scopus 로고
    • Plant disease resistance protein signaling: NBS-LRR proteins and their partners
    • Belkhadir, Y., Subramaniam, R., and Dangl, J.L. (2004b). Plant disease resistance protein signaling: NBS-LRR proteins and their partners. Curr. Opin. Plant Biol. 7, 391-399.
    • (2004) Curr. Opin. Plant Biol. , vol.7 , pp. 391-399
    • Belkhadir, Y.1    Subramaniam, R.2    Dangl, J.L.3
  • 5
    • 13844316456 scopus 로고    scopus 로고
    • Molecular characterization of proteolytic cleavage sites in the Pseudomonas syringae effector AvrRpt2
    • USA
    • Chisholm, S.T., Dahlbeck, D., Krishnamurthy, N., Day, B., Sjolander, K., and Staskawicz, B.J. (2005). Molecular characterization of proteolytic cleavage sites in the Pseudomonas syringae effector AvrRpt2. Proc. Natl. Acad. Sci. USA 102, 2087-2092.
    • (2005) Proc. Natl. Acad. Sci. , vol.102 , pp. 2087-2092
    • Chisholm, S.T.1    Dahlbeck, D.2    Krishnamurthy, N.3    Day, B.4    Sjolander, K.5    Staskawicz, B.J.6
  • 6
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough, S.J., and Bent, A.F. (1998). Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16, 735-743.
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 7
    • 31344434276 scopus 로고    scopus 로고
    • A eukaryotic cyclophilin is required for the activation of a phytopathogenic bacterial effector protein
    • in press
    • Coaker, G., Falick, A., and Staskawicz, B.J. (2005). A eukaryotic cyclophilin is required for the activation of a phytopathogenic bacterial effector protein. Science, in press.
    • (2005) Science
    • Coaker, G.1    Falick, A.2    Staskawicz, B.J.3
  • 8
    • 0035859020 scopus 로고    scopus 로고
    • Plant pathogens and integrated defence responses to infection
    • Dangl, J.L., and Jones, J.D. (2001). Plant pathogens and integrated defence responses to infection. Nature 411, 826-833.
    • (2001) Nature , vol.411 , pp. 826-833
    • Dangl, J.L.1    Jones, J.D.2
  • 9
    • 0037595606 scopus 로고    scopus 로고
    • Physical interaction between RRS1-R, a protein conferring resistance to bacterial wilt, and PopP2, a type III effector targeted to the plant nucleus
    • USA
    • Deslandes, L., Olivier, J., Peeters, N., Feng, D.X., Khounlotham, M., Boucher, C., Somssich, I., Genin, S., and Marco, Y. (2003). Physical interaction between RRS1-R, a protein conferring resistance to bacterial wilt, and PopP2, a type III effector targeted to the plant nucleus. Proc. Natl. Acad. Sci. USA 100, 8024-8029.
    • (2003) Proc. Natl. Acad. Sci. , 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
  • 10
    • 0035108614 scopus 로고    scopus 로고
    • Six amino acid changes confined to the leucine-rich repeat beta-strand/beta-turn motif determine the difference between the P and P2 rust resistance specificities in flax
    • Dodds, P.N., Lawrence, G.J., and Ellis, J.G. (2001). Six amino acid changes confined to the leucine-rich repeat beta-strand/beta-turn motif determine the difference between the P and P2 rust resistance specificities in flax. Plant Cell 13, 163-178.
    • (2001) Plant Cell , vol.13 , pp. 163-178
    • Dodds, P.N.1    Lawrence, G.J.2    Ellis, J.G.3
  • 11
    • 0037359288 scopus 로고    scopus 로고
    • Transient expression of Arabidopsis thaliana ascorbate peroxidase 3 in Nicotiana benthamiana plants infected with recombinant potato virus X
    • Escobar, C., Hernandez, L.E., Jimenez, A., Creissen, G., Ruiz, M.T., and Mullineaux, P.M. (2003). Transient expression of Arabidopsis thaliana ascorbate peroxidase 3 in Nicotiana benthamiana plants infected with recombinant potato virus X. Plant Cell Rep. 21, 699-704.
    • (2003) Plant Cell Rep , vol.21 , pp. 699-704
    • Escobar, C.1    Hernandez, L.E.2    Jimenez, A.3    Creissen, G.4    Ruiz, M.T.5    Mullineaux, P.M.6
  • 12
    • 0027934792 scopus 로고
    • Extensive lipidation of a Torpedo cysteine string protein
    • Gundersen, C.B., Mastrogiacomo, A., Faull, K., and Umbach, J.A. (1994). Extensive lipidation of a Torpedo cysteine string protein. J. Biol. Chem. 269, 19197-19199.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19197-19199
    • Gundersen, C.B.1    Mastrogiacomo, A.2    Faull, K.3    Umbach, J.A.4
  • 13
    • 2542584746 scopus 로고    scopus 로고
    • Silencing of subfamily I of protein phosphatase 2A catalytic subunits results in activation of plant defense responses and localized cell death
    • He, X., Anderson, J.C., del Pozo, O., Gu, Y.Q., Tang, X., and Martin, G.B. (2004). Silencing of subfamily I of protein phosphatase 2A catalytic subunits results in activation of plant defense responses and localized cell death. Plant J. 38, 563-577.
    • (2004) Plant J , vol.38 , pp. 563-577
    • He, X.1    Anderson, J.C.2    Del Pozo, O.3    Gu, Y.Q.4    Tang, X.5    Martin, G.B.6
  • 14
    • 0242556837 scopus 로고    scopus 로고
    • Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein
    • Hubert, D.A., Tomero, P., Belkhadir, Y., Krishna, P., Takahashi, A., Shirasu, K., and Dangl, J.L. (2003). Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein. EMBO J. 22, 5679-5689.
    • (2003) EMBO J , vol.22 , pp. 5679-5689
    • Hubert, D.A.1    Tomero, P.2    Belkhadir, Y.3    Krishna, P.4    Takahashi, A.5    Shirasu, K.6    Dangl, J.L.7
  • 15
    • 0034254266 scopus 로고    scopus 로고
    • Direct interaction of resistance gene and avirulence gene products confers rice blast resistance
    • Jia, Y., McAdams, S.A., Bryan, G.T., Hershey, H.P., and Valent, B. (2000). Direct interaction of resistance gene and avirulence gene products confers rice blast resistance. EMBO J. 19, 4004-4014.
    • (2000) EMBO J , vol.19 , pp. 4004-4014
    • Jia, Y.1    McAdams, S.A.2    Bryan, G.T.3    Hershey, H.P.4    Valent, B.5
  • 16
    • 0036696447 scopus 로고    scopus 로고
    • NPK1, an MEKK1-like mitogen-activated protein kinase kinase kinase, regulates innate immunity and development in plants
    • Jin, H., Axtell, M.J., Dahlbeck, D., Ekwenna, O., Zhang, S., Staskawicz, B., and Baker, B. (2002). NPK1, an MEKK1-like mitogen-activated protein kinase kinase kinase, regulates innate immunity and development in plants. Dev. Cell 3, 291-297.
    • (2002) Dev. Cell , vol.3 , pp. 291-297
    • Jin, H.1    Axtell, M.J.2    Dahlbeck, D.3    Ekwenna, O.4    Zhang, S.5    Staskawicz, B.6    Baker, B.7
  • 17
    • 1042278906 scopus 로고    scopus 로고
    • Plant innate immunity-Direct and indirect recognition of general and specific pathogen-associated molecules
    • Jones, D.A., and Takemoto, D. (2004). Plant innate immunity-Direct and indirect recognition of general and specific pathogen-associated molecules. Curr. Opin. Immunol. 16, 48-62.
    • (2004) Curr. Opin. Immunol. , vol.16 , pp. 48-62
    • Jones, D.A.1    Takemoto, D.2
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0030800671 scopus 로고    scopus 로고
    • Characterization of the palmitoylation domain of SNAP-25
    • Lane, S.R., and Liu, Y. (1997). Characterization of the palmitoylation domain of SNAP-25. J. Neurochem. 69, 1864-1869.
    • (1997) J. Neurochem. , vol.69 , pp. 1864-1869
    • Lane, S.R.1    Liu, Y.2
  • 20
    • 21044458960 scopus 로고    scopus 로고
    • Molecular genetic evidence for the role of SGT1 in the intramolecular complementation of Bs2 protein activity in Nicotiana benthamiana
    • Leister, R.T., Dahlbeck, D., Day, B., Li, Y., Chesnokova, O., and Staskawicz, B.J. (2005). Molecular genetic evidence for the role of SGT1 in the intramolecular complementation of Bs2 protein activity in Nicotiana benthamiana. Plant Cell 17, 1268-1278.
    • (2005) Plant Cell , vol.17 , pp. 1268-1278
    • Leister, R.T.1    Dahlbeck, D.2    Day, B.3    Li, Y.4    Chesnokova, O.5    Staskawicz, B.J.6
  • 21
    • 0347087451 scopus 로고    scopus 로고
    • Molecular chaperone Hsp90 associates with resistance protein N and its signaling proteins SGT1 and Rar1 to modulate an innate immune response in plants
    • Liu, Y., Burch-Smith, T., Schiff, M., Feng, S., and Dinesh-Kumar, S.P. (2004). Molecular chaperone Hsp90 associates with resistance protein N and its signaling proteins SGT1 and Rar1 to modulate an innate immune response in plants. J. Biol. Chem. 279, 2101-2108.
    • (2004) J. Biol. Chem. , vol.279 , pp. 2101-2108
    • Liu, Y.1    Burch-Smith, T.2    Schiff, M.3    Feng, S.4    Dinesh-Kumar, S.P.5
  • 22
    • 0037423306 scopus 로고    scopus 로고
    • Arabidopsis RIN4 is a target of the type III virulence effector AvrRpt2 and modulates RPS2-mediated resistance
    • Mackey, D., Belkhadir, Y., Alonso, J.M., Ecker, J.R., and Dangl, J.L. (2003). Arabidopsis RIN4 is a target of the type III virulence effector AvrRpt2 and modulates RPS2-mediated resistance. Cell 112, 379-389.
    • (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
  • 23
    • 0037155687 scopus 로고    scopus 로고
    • RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in Arabidopsis
    • Mackey, D., Holt, B.F., Wiig, A., and Dangl, J.L. (2002). RIN4 interacts with Pseudomonas syringae type III effector molecules and is required for RPM1-mediated resistance in Arabidopsis. Cell 108, 743-754.
    • (2002) Cell , vol.108 , pp. 743-754
    • Mackey, D.1    Holt, B.F.2    Wiig, A.3    Dangl, J.L.4
  • 24
    • 0037009437 scopus 로고    scopus 로고
    • Interaction between domains of a plant NBS-LRR protein in disease resistance-related cell death
    • Moffett, P., Farnham, G., Peart, J., and Baulcombe, D.C. (2002). Interaction between domains of a plant NBS-LRR protein in disease resistance-related cell death. EMBO J. 21, 4511-4519.
    • (2002) EMBO J. , vol.21 , pp. 4511-4519
    • Moffett, P.1    Farnham, G.2    Peart, J.3    Baulcombe, D.C.4
  • 25
    • 0033018269 scopus 로고    scopus 로고
    • Characterization of the Pseudomonas syringae pv. tomato AvrRpt2 protein: Demonstration of secretion and processing during bacterial pathogenesis
    • Mudgett, M.B., and Staskawicz, B.J. (1999). Characterization of the Pseudomonas syringae pv. tomato AvrRpt2 protein: Demonstration of secretion and processing during bacterial pathogenesis. Mol. Microbiol. 32, 927-941.
    • (1999) Mol. Microbiol. , vol.32 , pp. 927-941
    • Mudgett, M.B.1    Staskawicz, B.J.2
  • 26
    • 0029158550 scopus 로고
    • Strength and tissue specificity of chimeric promoters derived from the octopine and mannopine synthase genes
    • Ni, M., Cui, D., Einstein, J., Narasimhulu, S., Vergara, C.E., and Gelvin, S.B. (1995). Strength and tissue specificity of chimeric promoters derived from the octopine and mannopine synthase genes. Plant J. 7, 661-676.
    • (1995) Plant J. , vol.7 , pp. 661-676
    • Ni, M.1    Cui, D.2    Einstein, J.3    Narasimhulu, S.4    Vergara, C.E.5    Gelvin, S.B.6
  • 27
    • 7444255626 scopus 로고    scopus 로고
    • Membrane targeting of lipid modified signal transduction proteins
    • Resh, M.D. (2004). Membrane targeting of lipid modified signal transduction proteins. Subcell. Biochem. 37, 217-232.
    • (2004) Subcell. Biochem. , vol.37 , pp. 217-232
    • Resh, M.D.1
  • 29
    • 0038607608 scopus 로고    scopus 로고
    • Complex formation, promiscuity and multi-functionality: Protein interactions in disease-resistance pathways
    • Shirasu, K., and Schulze-Lefert, P. (2003). Complex formation, promiscuity and multi-functionality: Protein interactions in disease-resistance pathways. Trends Plant Sci. 8, 252-258.
    • (2003) Trends Plant Sci. , vol.8 , pp. 252-258
    • Shirasu, K.1    Schulze-Lefert, P.2
  • 30
    • 3543099503 scopus 로고    scopus 로고
    • Palmitoylation of intracellular signaling proteins: Regulation and function
    • Smotrys, J.E., and Linder, M.E. (2004). Palmitoylation of intracellular signaling proteins: Regulation and function. Annu. Rev. Biochem. 73, 559-587.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 559-587
    • Smotrys, J.E.1    Linder, M.E.2
  • 31
    • 0035933536 scopus 로고    scopus 로고
    • Common and contrasting themes of plant and animal diseases
    • Staskawicz, B.J., Mudgett, M.B., Dangl, J.L., and Galan, J.E. (2001). Common and contrasting themes of plant and animal diseases. Science 292, 2285-2289.
    • (2001) Science , vol.292 , pp. 2285-2289
    • Staskawicz, B.J.1    Mudgett, M.B.2    Dangl, J.L.3    Galan, J.E.4
  • 33
    • 0141705339 scopus 로고    scopus 로고
    • HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis
    • USA
    • Takahashi, A., Casais, C., Ichimura, K., and Shirasu, K. (2003). HSP90 interacts with RAR1 and SGT1 and is essential for RPS2-mediated disease resistance in Arabidopsis. Proc. Natl. Acad. Sci. USA 100, 11777-11782.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 11777-11782
    • Takahashi, A.1    Casais, C.2    Ichimura, K.3    Shirasu, K.4
  • 34
    • 0034489715 scopus 로고    scopus 로고
    • Mutational analysis of the Arabidopsis nucleotide binding site-leucine-rich repeat resistance gene RPS2
    • Tao, Y., Yuan, F., Leister, R.T., Ausubel, F.M., and Katagiri, F. (2000). Mutational analysis of the Arabidopsis nucleotide binding site-leucine-rich repeat resistance gene RPS2. Plant Cell 12, 2541-2554.
    • (2000) Plant Cell , vol.12 , pp. 2541-2554
    • Tao, Y.1    Yuan, F.2    Leister, R.T.3    Ausubel, F.M.4    Katagiri, F.5
  • 35
    • 0036009775 scopus 로고    scopus 로고
    • Large-scale structure-function analysis of the Arabidopsis RPM1 disease resistance protein
    • Tornero, P., Chao, R.A., Luthin, W.N., Goff, S.A., and Dangl, J.L. (2002). Large-scale structure-function analysis of the Arabidopsis RPM1 disease resistance protein. Plant Cell 14, 435-450.
    • (2002) Plant Cell , vol.14 , pp. 435-450
    • Tornero, P.1    Chao, R.A.2    Luthin, W.N.3    Goff, S.A.4    Dangl, J.L.5
  • 36
    • 0032422882 scopus 로고    scopus 로고
    • Plant disease resistance proteins and the "gene-for-gene" concept
    • Van der Biezen, E.A., and Jones, J.D.G. (1998). Plant disease resistance proteins and the "gene-for-gene" concept. Trends Biochem. Sci. 23, 454-456.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 454-456
    • Van Der Biezen, E.A.1    Jones, J.D.G.2
  • 37
  • 38
    • 0029999325 scopus 로고    scopus 로고
    • Hypermutagenic PCR involving all four transitions and a sizeable proportion of transversions
    • Vartanian, J.P., Henry, M., and Wain-Hobson, S. (1996). Hypermutagenic PCR involving all four transitions and a sizeable proportion of transversions. Nucleic Acids Res. 24, 2627-2631.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2627-2631
    • Vartanian, J.P.1    Henry, M.2    Wain-Hobson, S.3
  • 39
    • 6444233160 scopus 로고    scopus 로고
    • Expression of RPS4 in tobacco induces an AvrRps4-independent HR that requires EDS1, SGT1 and HSP90
    • Zhang, Y., Dorey, S., Swiderski, M., and Jones, J.D.G. (2004). Expression of RPS4 in tobacco induces an AvrRps4-independent HR that requires EDS1, SGT1 and HSP90. Plant J. 40, 213-224.
    • (2004) Plant J. , vol.40 , pp. 213-224
    • Zhang, Y.1    Dorey, S.2    Swiderski, M.3    Jones, J.D.G.4
  • 40
    • 0034304056 scopus 로고    scopus 로고
    • Technical advance: An estrogen receptor-based transactivator XVE mediates highly inducible gene expression in transgenic plants
    • Zuo, J., Niu, Q.W., and Chua, N.H. (2000). Technical advance: An estrogen receptor-based transactivator XVE mediates highly inducible gene expression in transgenic plants. Plant J. 24, 265-273.
    • (2000) Plant J. , vol.24 , pp. 265-273
    • Zuo, J.1    Niu, Q.W.2    Chua, N.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.