메뉴 건너뛰기




Volumn 7, Issue 4, 2004, Pages 384-390

Cysteine proteases in phytopathogenic bacteria: Identification of plant targets and activation of innate immunity

Author keywords

HR; hypersensitive response; R; resistance; Rho related GTPases from plants; RIN4; ROP; RPM1 interacting protein4; small ubiquitin like modifier; SUMO; TTSS; type III secretion system; ubiquitin like protease1; ULP1

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE PROTEINASE;

EID: 3042803667     PISSN: 13695266     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pbi.2004.05.003     Document Type: Review
Times cited : (92)

References (49)
  • 1
    • 0033764483 scopus 로고    scopus 로고
    • Assembly and function of type III secretory systems
    • Cornelis G.R., Van Gijsegem F. Assembly and function of type III secretory systems. Annu Rev Microbiol. 54:2000;735-774
    • (2000) Annu Rev Microbiol , vol.54 , pp. 735-774
    • Cornelis, G.R.1    Van Gijsegem, F.2
  • 2
    • 0344256435 scopus 로고    scopus 로고
    • Genomic approaches in Xanthomonas campestris pv. vesicatoria allow fishing for virulence genes
    • Buttner D., Noel L., Thieme F., Bonas U. Genomic approaches in Xanthomonas campestris pv. vesicatoria allow fishing for virulence genes. J Biotechnol. 106:2003;203-214
    • (2003) J Biotechnol , vol.106 , pp. 203-214
    • Buttner, D.1    Noel, L.2    Thieme, F.3    Bonas, U.4
  • 5
    • 0034786931 scopus 로고    scopus 로고
    • CDNA-AFLP analysis unravels a genome-wide hrpG-regulon in the plant pathogen Xanthomonas campestris pv. vesicatoria
    • Noel L., Thieme F., Nennstiel D., Bonas U. cDNA-AFLP analysis unravels a genome-wide hrpG-regulon in the plant pathogen Xanthomonas campestris pv. vesicatoria. Mol Microbiol. 41:2001;1271-1281
    • (2001) Mol Microbiol , vol.41 , pp. 1271-1281
    • Noel, L.1    Thieme, F.2    Nennstiel, D.3    Bonas, U.4
  • 6
    • 0041335630 scopus 로고    scopus 로고
    • The complete genome sequence of the Arabidopsis and tomato pathogen Pseudomonas syringae pv. tomato DC3000
    • The recent completion of the P. syringae pv. tomato genome unveils numerous candidate type-III effectors that are potentially used during pathogenesis. The availability of this genome sequence enables researchers to perform targeted experiments to further dissect P. syringae virulence in Arabidopsis and in its natural host, tomato.
    • Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T., Gwinn M.L., Dodson R.J., Deboy R.T., Durkin A.S., Kolonay J.F., et al. The complete genome sequence of the Arabidopsis and tomato pathogen Pseudomonas syringae pv. tomato DC3000. Proc Natl Acad Sci USA. 100:2003;10181-10186 The recent completion of the P. syringae pv. tomato genome unveils numerous candidate type-III effectors that are potentially used during pathogenesis. The availability of this genome sequence enables researchers to perform targeted experiments to further dissect P. syringae virulence in Arabidopsis and in its natural host, tomato.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10181-10186
    • Buell, C.R.1    Joardar, V.2    Lindeberg, M.3    Selengut, J.4    Paulsen, I.T.5    Gwinn, M.L.6    Dodson, R.J.7    Deboy, R.T.8    Durkin, A.S.9    Kolonay, J.F.10
  • 7
    • 0029294122 scopus 로고
    • The avrRPm1 gene of Pseudomonas syringae pv. maculicola is required for virulence on Arabidopsis
    • Ritter C., Dangl J.L. The avrRPm1 gene of Pseudomonas syringae pv. maculicola is required for virulence on Arabidopsis. Mol Plant Microbe Interact. 8:1995;444-453
    • (1995) Mol Plant Microbe Interact , vol.8 , pp. 444-453
    • Ritter, C.1    Dangl, J.L.2
  • 8
    • 0344948147 scopus 로고    scopus 로고
    • Expression of a single, host-specific, bacterial pathogenicity gene in plant cells elicits division, enlargement, and cell death
    • Duan Y.P., Castaneda A., Zhao G., Erdos G., Gabriel D.W. Expression of a single, host-specific, bacterial pathogenicity gene in plant cells elicits division, enlargement, and cell death. Mol Plant Microbe Interact. 12:1999;556-560
    • (1999) Mol Plant Microbe Interact , vol.12 , pp. 556-560
    • Duan, Y.P.1    Castaneda, A.2    Zhao, G.3    Erdos, G.4    Gabriel, D.W.5
  • 9
    • 0032863184 scopus 로고    scopus 로고
    • Identification of a pathogenicity island, which contains genes for virulence and avirulence, on a large native plasmid in the bean pathogen Pseudomonas syringae pathovar phaseolicola
    • Jackson R.W., Athanassopoulos E., Tsiamis G., Mansfield J.W., Sesma A., Arnold D.L., Gibbon M.J., Murillo J., Taylor J.D., Vivian A. Identification of a pathogenicity island, which contains genes for virulence and avirulence, on a large native plasmid in the bean pathogen Pseudomonas syringae pathovar phaseolicola. Proc Natl Acad Sci USA. 96:1999;10875-10880
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10875-10880
    • Jackson, R.W.1    Athanassopoulos, E.2    Tsiamis, G.3    Mansfield, J.W.4    Sesma, A.5    Arnold, D.L.6    Gibbon, M.J.7    Murillo, J.8    Taylor, J.D.9    Vivian, A.10
  • 10
    • 0034001870 scopus 로고    scopus 로고
    • AvrPto enhances growth and necrosis caused by Pseudomonas syringae pv. tomato in tomato lines lacking either Pto or Prf
    • Chang J.H., Rathjen J.P., Bernal A.J., Staskawicz B.J., Michelmore R.W. avrPto enhances growth and necrosis caused by Pseudomonas syringae pv. tomato in tomato lines lacking either Pto or Prf. Mol Plant Microbe Interact. 13:2000;568-571
    • (2000) Mol Plant Microbe Interact , vol.13 , pp. 568-571
    • Chang, J.H.1    Rathjen, J.P.2    Bernal, A.J.3    Staskawicz, B.J.4    Michelmore, R.W.5
  • 11
    • 0033666522 scopus 로고    scopus 로고
    • The Pseudomonas syringae avrRpt2 gene product promotes pathogen virulence from inside plant cells
    • Chen Z., Kloek A.P., Boch J., Katagiri F., Kunkel B.N. The Pseudomonas syringae avrRpt2 gene product promotes pathogen virulence from inside plant cells. Mol Plant Microbe Interact. 13:2000;1312-1321
    • (2000) Mol Plant Microbe Interact , vol.13 , pp. 1312-1321
    • Chen, Z.1    Kloek, A.P.2    Boch, J.3    Katagiri, F.4    Kunkel, B.N.5
  • 12
  • 13
    • 0037413710 scopus 로고    scopus 로고
    • Pseudomonas type III effector AvrPtoB induces plant disease susceptibility by inhibition of host programmed cell death
    • The authors show that the P. syringae TTSS effector AvrPtoB functions in planta to inhibit HR triggered by the PTO and Cf9 R proteins. Furthermore, AvrPtoB also suppressed programmed cell death in yeast. This suggests that AvrPtoB induces plant susceptibility by inhibiting plant immune responses.
    • Abramovitch R.B., Kim Y.J., Chen S., Dickman M.B., Martin G.B. Pseudomonas type III effector AvrPtoB induces plant disease susceptibility by inhibition of host programmed cell death. EMBO J. 22:2003;60-69 The authors show that the P. syringae TTSS effector AvrPtoB functions in planta to inhibit HR triggered by the PTO and Cf9 R proteins. Furthermore, AvrPtoB also suppressed programmed cell death in yeast. This suggests that AvrPtoB induces plant susceptibility by inhibiting plant immune responses.
    • (2003) EMBO J , vol.22 , pp. 60-69
    • Abramovitch, R.B.1    Kim, Y.J.2    Chen, S.3    Dickman, M.B.4    Martin, G.B.5
  • 14
    • 0025328112 scopus 로고
    • Widespread distribution and fitness contribution of Xanthomonas campestris avirulence gene avrBs2
    • Kearney B., Staskawicz B.J. Widespread distribution and fitness contribution of Xanthomonas campestris avirulence gene avrBs2. Nature. 346:1990;385-386
    • (1990) Nature , vol.346 , pp. 385-386
    • Kearney, B.1    Staskawicz, B.J.2
  • 15
    • 1342311961 scopus 로고    scopus 로고
    • Identification of Pseudomonas syringae type III effectors that can suppress programmed cell death in plants and yeast
    • The authors show that several P. syringae TTSS effectors suppress HR triggered by the HopPsyA effector in resistant plants. This suggests that several effectors may function in planta to suppress plant immune responses.
    • Jamir Y., Guo M., Oh H.S., Petnicki-Ocwieja T., Chen S., Tang X., Dickman M.B., Collmer A., R Alfano J. Identification of Pseudomonas syringae type III effectors that can suppress programmed cell death in plants and yeast. Plant J. 37:2004;554-565 The authors show that several P. syringae TTSS effectors suppress HR triggered by the HopPsyA effector in resistant plants. This suggests that several effectors may function in planta to suppress plant immune responses.
    • (2004) Plant J , vol.37 , pp. 554-565
    • Jamir, Y.1    Guo, M.2    Oh, H.S.3    Petnicki-Ocwieja, T.4    Chen, S.5    Tang, X.6    Dickman, M.B.7    Collmer, A.8    Alfano, J.R.9
  • 17
    • 0032422882 scopus 로고    scopus 로고
    • Plant disease-resistance proteins and the gene-for-gene concept
    • Van der Biezen E.A., Jones J.D. Plant disease-resistance proteins and the gene-for-gene concept. Trends Biochem Sci. 23:1998;454-456
    • (1998) Trends Biochem Sci , vol.23 , pp. 454-456
    • Van Der Biezen, E.A.1    Jones, J.D.2
  • 18
    • 1042278906 scopus 로고    scopus 로고
    • Plant innate immunity - Direct and indirect recognition of general and specific pathogen-associated molecules
    • A recent review that describes the events that lead to pathogen recognition and the activation of plant disease resistance.
    • Jones D.A., Takemoto D. Plant innate immunity - direct and indirect recognition of general and specific pathogen-associated molecules. Curr Opin Immunol. 16:2004;48-62 A recent review that describes the events that lead to pathogen recognition and the activation of plant disease resistance.
    • (2004) Curr Opin Immunol , vol.16 , pp. 48-62
    • Jones, D.A.1    Takemoto, D.2
  • 19
    • 0142093617 scopus 로고    scopus 로고
    • Xanthomonas type III effector XopD targets SUMO-conjugated proteins in planta
    • The authors show that the Xanthomonas XopD TTSS effector is a constitutively active cysteine protease that targets the plant SUMO pathway. XopD is translocated to plant subnuclear foci and hydrolyzes plant-specific SUMO-protein conjugates. This work reveals a novel mechanism used by Xanthomonas, and possibly other plant-associated microbes, to directly modulate plant signal transduction during infection.
    • Hotson A., Chosed R., Shu H., Orth K., Mudgett M.B. Xanthomonas type III effector XopD targets SUMO-conjugated proteins in planta. Mol Microbiol. 50:2003;377-389 The authors show that the Xanthomonas XopD TTSS effector is a constitutively active cysteine protease that targets the plant SUMO pathway. XopD is translocated to plant subnuclear foci and hydrolyzes plant-specific SUMO-protein conjugates. This work reveals a novel mechanism used by Xanthomonas, and possibly other plant-associated microbes, to directly modulate plant signal transduction during infection.
    • (2003) Mol Microbiol , vol.50 , pp. 377-389
    • Hotson, A.1    Chosed, R.2    Shu, H.3    Orth, K.4    Mudgett, M.B.5
  • 20
    • 2442574862 scopus 로고    scopus 로고
    • Characterization of the Xanthomonas AvrXv4 effector, a SUMO protease translocated into plant cells
    • in press.
    • Roden J, Eardley L, Hotson A, Cao Y, Mudgett MB: Characterization of the Xanthomonas AvrXv4 effector, a SUMO protease translocated into plant cells. Mol Plant Microbe Interact 2004, in press.
    • (2004) Mol Plant Microbe Interact
    • Roden, J.1    Eardley, L.2    Hotson, A.3    Cao, Y.4    Mudgett, M.B.5
  • 21
    • 0042322616 scopus 로고    scopus 로고
    • Cleavage of Arabidopsis PBS1 by a bacterial type III effector
    • The authors revealed that the P. syringae TTSS cysteine protease AvrPphB cleaves the Arabidopsis PBS1 kinase during infection. Both PBS1 cleavage and PBS1 kinase activity are required for the activation of RPS5-mediated disease resistance. This work provides crucial insight into the molecular events that are associated with effector action and recognition in planta.
    • Shao F., Golstein C., Ade J., Stoutemyer M., Dixon J.E., Innes R.W. Cleavage of Arabidopsis PBS1 by a bacterial type III effector. Science. 301:2003;1230-1233 The authors revealed that the P. syringae TTSS cysteine protease AvrPphB cleaves the Arabidopsis PBS1 kinase during infection. Both PBS1 cleavage and PBS1 kinase activity are required for the activation of RPS5-mediated disease resistance. This work provides crucial insight into the molecular events that are associated with effector action and recognition in planta.
    • (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
  • 22
    • 0037205231 scopus 로고    scopus 로고
    • A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis
    • Shao F., Merritt P.M., Bao Z., Innes R.W., Dixon J.E. A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis. Cell. 109:2002;575-588
    • (2002) Cell , vol.109 , pp. 575-588
    • Shao, F.1    Merritt, P.M.2    Bao, Z.3    Innes, R.W.4    Dixon, J.E.5
  • 23
    • 0141566396 scopus 로고    scopus 로고
    • Genetic and molecular evidence that the Pseudomonas syringae type III effector protein AvrRpt2 is a cysteine protease
    • The authors reveal that the P. syringae TTSS effector AvrRpt2 shares structural similarity with the cysteine protease staphopain. Mutation of AvrRpt2's catalytic core abolished several AvrRpt2 phenotypes: AvrRpt2 processing in planta, RIN4 degradation, and the activation of the RPS2 resistance protein. These studies support the hypothesis that AvrRpt2 functions as a cysteine protease in planta.
    • Axtell M.J., Chisholm S.T., Dahlbeck D., Staskawicz B.J. Genetic and molecular evidence that the Pseudomonas syringae type III effector protein AvrRpt2 is a cysteine protease. Mol Microbiol. 49:2003;1537-1546 The authors reveal that the P. syringae TTSS effector AvrRpt2 shares structural similarity with the cysteine protease staphopain. Mutation of AvrRpt2's catalytic core abolished several AvrRpt2 phenotypes: AvrRpt2 processing in planta, RIN4 degradation, and the activation of the RPS2 resistance protein. These studies support the hypothesis that AvrRpt2 functions as a cysteine protease in planta.
    • (2003) Mol Microbiol , vol.49 , pp. 1537-1546
    • Axtell, M.J.1    Chisholm, S.T.2    Dahlbeck, D.3    Staskawicz, B.J.4
  • 25
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell-cycle progression in yeast
    • Li S.J., Hochstrasser M. A new protease required for cell-cycle progression in yeast. Nature. 398:1999;246-251
    • (1999) Nature , vol.398 , pp. 246-251
    • Li, S.J.1    Hochstrasser, M.2
  • 26
    • 0034523266 scopus 로고    scopus 로고
    • SUMO-nonclassical ubiquitin
    • Melchoir F. SUMO-nonclassical ubiquitin. Annu Rev Cell Dev Biol. 16:2000;591-626
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 591-626
    • Melchoir, F.1
  • 27
    • 0037470238 scopus 로고    scopus 로고
    • The small ubiquitin-like modifier (SUMO) protein modification system in Arabidopsis. Accumulation of SUMO1 and -2 conjugates is increased by stress
    • The work described in this paper reveals that the SUMO pathway operates in plants. The SUMO pathway in Arabidopsis is more complex than that in any other system characterized to date. The authors show that a diverse array of sumoylated proteins exist in planta, and that some are SUMO-isoform specific. Moreover, they show that sumoylation is induced by heat, peroxide, ethanol, and canavanine.
    • Kurepa J., Walker J.M., Smalle J., Gosink M.M., Davis S.J., Durham T.L., Sung D.Y., Vierstra R.D. The small ubiquitin-like modifier (SUMO) protein modification system in Arabidopsis. Accumulation of SUMO1 and -2 conjugates is increased by stress. J Biol Chem. 278:2003;6862-6872 The work described in this paper reveals that the SUMO pathway operates in plants. The SUMO pathway in Arabidopsis is more complex than that in any other system characterized to date. The authors show that a diverse array of sumoylated proteins exist in planta, and that some are SUMO-isoform specific. Moreover, they show that sumoylation is induced by heat, peroxide, ethanol, and canavanine.
    • (2003) J Biol Chem , vol.278 , pp. 6862-6872
    • Kurepa, J.1    Walker, J.M.2    Smalle, J.3    Gosink, M.M.4    Davis, S.J.5    Durham, T.L.6    Sung, D.Y.7    Vierstra, R.D.8
  • 28
    • 0037295721 scopus 로고    scopus 로고
    • Modification with SUMO. A role in transcriptional regulation
    • A recent review that describes the role of SUMO in transcriptional repression.
    • Verger A., Perdomo J., Crossley M. Modification with SUMO. A role in transcriptional regulation. EMBO Rep. 4:2003;137-142 A recent review that describes the role of SUMO in transcriptional repression.
    • (2003) EMBO Rep , vol.4 , pp. 137-142
    • Verger, A.1    Perdomo, J.2    Crossley, M.3
  • 29
    • 0033199037 scopus 로고    scopus 로고
    • Isolation of a novel SUMO protein from tomato that suppresses EIX-induced cell death
    • Hanania U., Furman-Matarasso N., Ron M., Avni A. Isolation of a novel SUMO protein from tomato that suppresses EIX-induced cell death. Plant J. 19:1999;533-541
    • (1999) Plant J , vol.19 , pp. 533-541
    • Hanania, U.1    Furman-Matarasso, N.2    Ron, M.3    Avni, A.4
  • 30
    • 0037781038 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier modulates abscisic acid signaling in Arabidopsis
    • The authors reveal a link between SUMO and hormone signaling. Growth inhibition mediated by abscisic acid (ABA) is attenuated in transgenic plants that overexpress AtSUMO1/2, and the induction of ABA- and stress-responsive genes is amplified in these transgenics.
    • Lois L.M., Lima C.D., Chua N.H. Small ubiquitin-like modifier modulates abscisic acid signaling in Arabidopsis. Plant Cell. 15:2003;1347-1359 The authors reveal a link between SUMO and hormone signaling. Growth inhibition mediated by abscisic acid (ABA) is attenuated in transgenic plants that overexpress AtSUMO1/2, and the induction of ABA- and stress-responsive genes is amplified in these transgenics.
    • (2003) Plant Cell , vol.15 , pp. 1347-1359
    • Lois, L.M.1    Lima, C.D.2    Chua, N.H.3
  • 31
    • 0142028822 scopus 로고    scopus 로고
    • A nuclear protease required for flowering-time regulation in Arabidopsis reduces the abundance of SMALL UBIQUITIN-RELATED MODIFIER conjugates
    • The work described in this paper reveals a link between SUMO and the regulation of flowering. EARLY IN SHORT DAYS (ESD4) encodes a nuclear protein that has SUMO protease activity. esd4 mutants flower early and contain less free SUMO but more SUMO-protein conjugates than wildtype plants. Thus, the authors speculate that ESD4 functions to recycle SUMO from SUMO-protein conjugates.
    • Murtas G., Reeves P.H., Fu Y.F., Bancroft I., Dean C., Coupland G. A nuclear protease required for flowering-time regulation in Arabidopsis reduces the abundance of SMALL UBIQUITIN-RELATED MODIFIER conjugates. Plant Cell. 15:2003;2308-2319 The work described in this paper reveals a link between SUMO and the regulation of flowering. EARLY IN SHORT DAYS (ESD4) encodes a nuclear protein that has SUMO protease activity. esd4 mutants flower early and contain less free SUMO but more SUMO-protein conjugates than wildtype plants. Thus, the authors speculate that ESD4 functions to recycle SUMO from SUMO-protein conjugates.
    • (2003) Plant Cell , vol.15 , pp. 2308-2319
    • Murtas, G.1    Reeves, P.H.2    Fu, Y.F.3    Bancroft, I.4    Dean, C.5    Coupland, G.6
  • 32
    • 0036175537 scopus 로고    scopus 로고
    • Two novel type III-secreted proteins of Xanthomonas campestris pv. vesicatoria are encoded within the hrp pathogenicity island
    • Noel L., Thieme F., Nennstiel D., Bonas U. Two novel type III-secreted proteins of Xanthomonas campestris pv. vesicatoria are encoded within the hrp pathogenicity island. J Bacteriol. 184:2002;1340-1348
    • (2002) J Bacteriol , vol.184 , pp. 1340-1348
    • Noel, L.1    Thieme, F.2    Nennstiel, D.3    Bonas, U.4
  • 33
    • 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
    • The authors report that the Arabidopsis RRS1-R resistance protein physically interacts with the Ralstonia solanacearum TTSS effector PopP2. When PopP2 is expressed in plant cells, cytoplasmic RRS1-R moves to the plant nucleus. This study hints at the molecular events leading to RRS1-R activation.
    • Deslandes L., Olivier J., Peeters N., Feng D.X., Khounlotham M., Boucher C., Somssich I., Genin S., Marco Y. 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. 100:2003;8024-8029 The authors report that the Arabidopsis RRS1-R resistance protein physically interacts with the Ralstonia solanacearum TTSS effector PopP2. When PopP2 is expressed in plant cells, cytoplasmic RRS1-R moves to the plant nucleus. This study hints at the molecular events leading to RRS1-R activation.
    • (2003) Proc Natl Acad Sci USA , 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
  • 34
    • 0037133245 scopus 로고    scopus 로고
    • Resistance to Ralstonia solanacearum in Arabidopsis thaliana is conferred by the recessive RRS1-R gene, a member of a novel family of resistance genes
    • Deslandes L., Olivier J., Theulieres 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 USA. 99:2002;2404-2409
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2404-2409
    • Deslandes, L.1    Olivier, J.2    Theulieres, F.3    Hirsch, J.4    Feng, D.X.5    Bittner-Eddy, P.6    Beynon, J.7    Marco, Y.8
  • 35
    • 0347719364 scopus 로고    scopus 로고
    • The crystal structure of Pseudomonas avirulence protein AvrPphB: A papain-like fold with a distinct substrate-binding site
    • The exciting release of the crystal structure of AvrPphB confirms that this TTSS effector belongs to the papain superfamily of cysteine proteases. In addition, the AvrPphB structure advances our understanding of substrate specificity and pathogen recognition at the structural level.
    • Zhu M., Shao F., Innes R.W., Dixon J.E., Xu Z. The crystal structure of Pseudomonas avirulence protein AvrPphB: a papain-like fold with a distinct substrate-binding site. Proc Natl Acad Sci USA. 101:2004;302-307 The exciting release of the crystal structure of AvrPphB confirms that this TTSS effector belongs to the papain superfamily of cysteine proteases. In addition, the AvrPphB structure advances our understanding of substrate specificity and pathogen recognition at the structural level.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 302-307
    • Zhu, M.1    Shao, F.2    Innes, R.W.3    Dixon, J.E.4    Xu, Z.5
  • 36
    • 0031105461 scopus 로고    scopus 로고
    • Expression of avrPphB, an avirulence gene from Pseudomonas syringae pv. phaseolicola, and the delivery of signals causing the hypersensitive reaction in bean
    • Puri N., Jenner C., Bennett M., Stewart R., Mansfield J., Lyons N., Taylor J. Expression of avrPphB, an avirulence gene from Pseudomonas syringae pv. phaseolicola, and the delivery of signals causing the hypersensitive reaction in bean. Mol Plant Microbe Interact. 10:1997;247-256
    • (1997) Mol Plant Microbe Interact , vol.10 , pp. 247-256
    • Puri, N.1    Jenner, C.2    Bennett, M.3    Stewart, R.4    Mansfield, J.5    Lyons, N.6    Taylor, J.7
  • 37
    • 0034640111 scopus 로고    scopus 로고
    • Eukaryotic fatty acylation drives plasma membrane targeting and enhances function of several type III effector proteins from Pseudomonas syringae
    • Nimchuk Z., Marois E., Kjemtrup S., Leister R.T., Katagiri F., Dangl J.L. Eukaryotic fatty acylation drives plasma membrane targeting and enhances function of several type III effector proteins from Pseudomonas syringae. Cell. 101:2000;353-363
    • (2000) Cell , vol.101 , pp. 353-363
    • Nimchuk, Z.1    Marois, E.2    Kjemtrup, S.3    Leister, R.T.4    Katagiri, F.5    Dangl, J.L.6
  • 38
    • 0029328293 scopus 로고
    • A disease resistance gene in Arabidopsis with specificity for the avrPph3 gene of Pseudomonas syringae pv. phaseolicola
    • Simonich M.T., Innes R.W. A disease resistance gene in Arabidopsis with specificity for the avrPph3 gene of Pseudomonas syringae pv. phaseolicola. Mol Plant Microbe Interact. 8:1995;637-640
    • (1995) Mol Plant Microbe Interact , vol.8 , pp. 637-640
    • Simonich, M.T.1    Innes, R.W.2
  • 39
    • 0034990117 scopus 로고    scopus 로고
    • The Arabidopsis PBS1 resistance gene encodes a member of a novel protein kinase subfamily
    • Swiderski M., Innes R.W. The Arabidopsis PBS1 resistance gene encodes a member of a novel protein kinase subfamily. Plant J. 26:2001;101-112
    • (2001) Plant J , vol.26 , pp. 101-112
    • Swiderski, M.1    Innes, R.W.2
  • 40
    • 0038198644 scopus 로고    scopus 로고
    • Small GTPase 'Rop': Molecular switch for plant defense responses
    • A recent review that discusses the function of Rho-related GTPases in plant defense.
    • Agrawal G.K., Iwahashi H., Rakwal R. Small GTPase 'Rop': molecular switch for plant defense responses. FEBS Lett. 546:2003;173-180 A recent review that discusses the function of Rho-related GTPases in plant defense.
    • (2003) FEBS Lett , vol.546 , pp. 173-180
    • Agrawal, G.K.1    Iwahashi, H.2    Rakwal, R.3
  • 42
    • 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., 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
    • (1999) Mol Microbiol , vol.32 , pp. 927-941
    • Mudgett, M.B.1    Staskawicz, B.J.2
  • 43
    • 0037423306 scopus 로고    scopus 로고
    • Arabidopsis RIN4 is a target of the type III virulence effector AvrRpt2 and modulates RPS2-mediated resistance
    • ••] are back-to-back papers showing that the P. syringae TTSS effector AvrRpt2 targets Arabidopsis RIN4, inducing its disappearance and the activation of RPS2 resistance. RIN4 physically interacts with RPS2, providing a mechanism for RPS2 activation. Interestingly, RIN4 overexpression attenuates AvrRpt2-induced phenotypes, whereas RIN4 elimination constitutively activates RPS2, resulting in seedling lethality. Thus, RPS2 indirectly perceives AvrRpt2 action by monitoring the steady-state of RIN4.
    • ••] are back-to-back papers showing that the P. syringae TTSS effector AvrRpt2 targets Arabidopsis RIN4, inducing its disappearance and the activation of RPS2 resistance. RIN4 physically interacts with RPS2, providing a mechanism for RPS2 activation. Interestingly, RIN4 overexpression attenuates AvrRpt2-induced phenotypes, whereas RIN4 elimination constitutively activates RPS2, resulting in seedling lethality. Thus, RPS2 indirectly perceives AvrRpt2 action by monitoring the steady-state of RIN4.
    • (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
  • 44
    • 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., 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
    • (2002) Cell , vol.108 , pp. 743-754
    • MacKey, D.1    Holt, B.F.2    Wiig, A.3    Dangl, J.L.4
  • 45
    • 0037423390 scopus 로고    scopus 로고
    • Initiation of RPS2-specified disease resistance in Arabidopsis is coupled to the AvrRpt2-directed elimination of RIN4
    • ••].
    • ••].
    • (2003) Cell , vol.112 , pp. 369-377
    • Axtell, M.J.1    Staskawicz, B.J.2
  • 46
    • 0344530453 scopus 로고    scopus 로고
    • Cleavage of the Pseudomonas syringae type III effector AvrRpt2 requires a host factor(s) common among eukaryotes and is important for AvrRpt2 localization in the host cell
    • The processing of the P. syringae TTSS effector AvrRpt2 in planta requires a host factor. The authors present evidence that this factor is a peptide that is present in several eukaryotes.
    • Jin P., Wood M.D., Wu Y., Xie Z., Katagiri F. Cleavage of the Pseudomonas syringae type III effector AvrRpt2 requires a host factor(s) common among eukaryotes and is important for AvrRpt2 localization in the host cell. Plant Physiol. 133:2003;1072-1082 The processing of the P. syringae TTSS effector AvrRpt2 in planta requires a host factor. The authors present evidence that this factor is a peptide that is present in several eukaryotes.
    • (2003) Plant Physiol , vol.133 , pp. 1072-1082
    • Jin, P.1    Wood, M.D.2    Wu, Y.3    Xie, Z.4    Katagiri, F.5
  • 47
    • 0032430187 scopus 로고    scopus 로고
    • The Arabidopsis thaliana RPM1 disease resistance gene product in 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 in a peripheral plasma membrane protein that is degraded coincident with the hypersensitive response. Proc Natl Acad Sci USA. 95:1998;15849-15854
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15849-15854
    • Boyes, D.C.1    Nam, J.2    Dangl, J.L.3
  • 48
    • 0030046186 scopus 로고    scopus 로고
    • Interference between two specific pathogen recognition events mediated by distinct plant disease resistance genes
    • Ritter C., Dangl J.L. Interference between two specific pathogen recognition events mediated by distinct plant disease resistance genes. Plant Cell. 8:1996;251-257
    • (1996) Plant Cell , vol.8 , pp. 251-257
    • Ritter, C.1    Dangl, J.L.2
  • 49
    • 0030088109 scopus 로고    scopus 로고
    • Isolation of Arabidopsis genes that differentiate between resistance responses mediated by the RPS2 and RPM1 disease resistance genes
    • Reuber T.L., Ausubel F.M. Isolation of Arabidopsis genes that differentiate between resistance responses mediated by the RPS2 and RPM1 disease resistance genes. Plant Cell. 8:1996;241-249
    • (1996) Plant Cell , vol.8 , pp. 241-249
    • Reuber, T.L.1    Ausubel, F.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.