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Volumn 13, Issue 4, 2000, Pages 413-420

Involvement of diamine oxidase and peroxidase in insolubilization of the extracellular matrix: Implications for pea nodule initiation by Rhizobium leguminosarum

Author keywords

Extensin; Pisum sativum; Polyamine; R. leguminosarum bv. viciae; Symbiosis

Indexed keywords

AMINE OXIDASE (COPPER CONTAINING); BACTERIAL COLONIZATION; ENZYME INHIBITOR; EXTRACELLULAR MATRIX; FUNGAL GROWTH; GENETIC TRANSCRIPTION; GLYCOPROTEIN; IN SITU HYBRIDIZATION; INFECTION; MONOCLONAL ANTIBODY; NODULATION; PEROXIDASE;

EID: 0034071312     PISSN: 08940282     EISSN: None     Source Type: Journal    
DOI: 10.1094/MPMI.2000.13.4.413     Document Type: Article
Times cited : (100)

References (35)
  • 1
    • 0001836642 scopus 로고
    • Spatial and functional correlation between diamine-oxidase and peroxidase-activities and their dependence upon deetiolation and wounding in chickpea stems
    • Angelini, R., Manes, F., and Federico, R. 1990. Spatial and functional correlation between diamine-oxidase and peroxidase-activities and their dependence upon deetiolation and wounding in chickpea stems. Planta 182:89-96.
    • (1990) Planta , vol.182 , pp. 89-96
    • Angelini, R.1    Manes, F.2    Federico, R.3
  • 2
    • 0026735576 scopus 로고
    • Elicitor-induced and wound-induced oxidative cross-linking of a proline-rich plant-cell wall protein - A novel, rapid defense response
    • Bradley, D. J., Kjellbom, P., and Lamb, C. J. 1992. Elicitor-induced and wound-induced oxidative cross-linking of a proline-rich plant-cell wall protein - a novel, rapid defense response. Cell 70:21-30.
    • (1992) Cell , vol.70 , pp. 21-30
    • Bradley, D.J.1    Kjellbom, P.2    Lamb, C.J.3
  • 3
    • 34250095615 scopus 로고
    • Isolation of monoclonal antibodies reacting with peribacteroid membranes and other components of pea root nodules containing Rhizobium leguminosarum
    • Bradley, D. J., Wood, E. A., Larkins, A. P., Galfre, G., Butcher, G. W., and Brewin, N. J. 1988. Isolation of monoclonal antibodies reacting with peribacteroid membranes and other components of pea root nodules containing Rhizobium leguminosarum. Planta 173:149-160.
    • (1988) Planta , vol.173 , pp. 149-160
    • Bradley, D.J.1    Wood, E.A.2    Larkins, A.P.3    Galfre, G.4    Butcher, G.W.5    Brewin, N.J.6
  • 4
    • 0025887460 scopus 로고
    • Development of the legume root nodule
    • Brewin, N. J. 1991. Development of the legume root nodule. Annu. Rev. Cell. Biol. 7:191-226.
    • (1991) Annu. Rev. Cell. Biol. , vol.7 , pp. 191-226
    • Brewin, N.J.1
  • 5
    • 0008924870 scopus 로고    scopus 로고
    • Structure and development of infection threads
    • F. E. Pedrosa, M. Hungria, M. G. Yates, and W. E. Newton, eds. Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Brewin, N. J., Rathbun, E. A. and Wisniewski, J.-P. 2000. Structure and development of infection threads. Pages 381-382 in: Nitrogen Fixation: From Molecules to Crop Productivity. F. E. Pedrosa, M. Hungria, M. G. Yates, and W. E. Newton, eds. Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (2000) Nitrogen Fixation: From Molecules to Crop Productivity , pp. 381-382
    • Brewin, N.J.1    Rathbun, E.A.2    Wisniewski, J.-P.3
  • 6
    • 0030764809 scopus 로고    scopus 로고
    • Elicitor-induced extensin insolubilization in suspension-cultured tomato cells
    • Brownleader, M. D., McNally, P. E., Davies, G. E. A., Trevan, M., and Dey, P. M. 1997. Elicitor-induced extensin insolubilization in suspension-cultured tomato cells. Phytochemistry 46:1-9.
    • (1997) Phytochemistry , vol.46 , pp. 1-9
    • Brownleader, M.D.1    McNally, P.E.2    Davies, G.E.A.3    Trevan, M.4    Dey, P.M.5
  • 7
    • 0343044946 scopus 로고    scopus 로고
    • Pea seedling extracts catalyze protein amine binding and protein cross-linking. 2. Contribution of diamine oxidase to these reactions
    • Chiarello, M. D., Larre, C., Kedzior, Z. M., and Gueguen, J. 1996. Pea seedling extracts catalyze protein amine binding and protein cross-linking. 2. Contribution of diamine oxidase to these reactions. J. Agric. Food Chem. 44:3723-3726.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 3723-3726
    • Chiarello, M.D.1    Larre, C.2    Kedzior, Z.M.3    Gueguen, J.4
  • 8
    • 0029142086 scopus 로고
    • Transient induction of a peroxidase gene in Medicago truncatula precedes infection by Rhizobium meliloti
    • Cook, D., Dreyer, D., Bonnet, D., Howell, M., Nony, E., and Vanden-Bosch, K. 1995. Transient induction of a peroxidase gene in Medicago truncatula precedes infection by Rhizobium meliloti. Plant Cell 7:43-55.
    • (1995) Plant Cell , vol.7 , pp. 43-55
    • Cook, D.1    Dreyer, D.2    Bonnet, D.3    Howell, M.4    Nony, E.5    Vanden-Bosch, K.6
  • 9
    • 0031401520 scopus 로고    scopus 로고
    • Immunolocalization of PsNLEC-1, a lectin-like glycoprotein expressed in developing pea nodules
    • Dahiya, P., Kardailsky, I. V., and Brewin, N. J. 1997. Immunolocalization of PsNLEC-1, a lectin-like glycoprotein expressed in developing pea nodules. Plant Physiol. 115:1431-1442.
    • (1997) Plant Physiol. , vol.115 , pp. 1431-1442
    • Dahiya, P.1    Kardailsky, I.V.2    Brewin, N.J.3
  • 10
    • 0000477510 scopus 로고
    • Diversity of abundant mRNA sequences and patterns of protein synthesis in etiolated and greened pea seedlings
    • de Vries, S. C., Springer, J., and Wessels, J. H. G. 1982. Diversity of abundant mRNA sequences and patterns of protein synthesis in etiolated and greened pea seedlings. Planta 156:129-135.
    • (1982) Planta , vol.156 , pp. 129-135
    • De Vries, S.C.1    Springer, J.2    Wessels, J.H.G.3
  • 11
    • 0030448013 scopus 로고    scopus 로고
    • Use of green fluorescent protein to visualize the early events of symbiosis between Rhizobium meliloti and alfalfa (Medicago sativa)
    • Gage, D. J., Bobo, T., and Long, S. R. 1996. Use of green fluorescent protein to visualize the early events of symbiosis between Rhizobium meliloti and alfalfa (Medicago sativa). J. Bacteriol. 178:7159-7166.
    • (1996) J. Bacteriol. , vol.178 , pp. 7159-7166
    • Gage, D.J.1    Bobo, T.2    Long, S.R.3
  • 13
    • 0027205053 scopus 로고
    • Prokaryotic plant parasites
    • Long, S. R., and Staskawicz, B. J. 1993. Prokaryotic plant parasites. Cell 73:921-935.
    • (1993) Cell , vol.73 , pp. 921-935
    • Long, S.R.1    Staskawicz, B.J.2
  • 14
    • 0011336998 scopus 로고
    • Activity and expression of diamine oxidase in lentil seedlings under different growth-conditions
    • Maccarrone, M., Rossi, A., Avigliano, L., and Agro, A. F. 1991. Activity and expression of diamine oxidase in lentil seedlings under different growth-conditions. Plant Science 79:51-55.
    • (1991) Plant Science , vol.79 , pp. 51-55
    • Maccarrone, M.1    Rossi, A.2    Avigliano, L.3    Agro, A.F.4
  • 15
    • 0031001232 scopus 로고    scopus 로고
    • Ozone stress modulates amine oxidase and lipoxygenase expression in lentil (Lens culinaris) seedlings
    • Maccarrone, M., Veldink, G. A., Vliegenthart, J. F. G., and Agro, A. F. 1997. Ozone stress modulates amine oxidase and lipoxygenase expression in lentil (Lens culinaris) seedlings. FEBS Lett. 408:241-244.
    • (1997) FEBS Lett. , vol.408 , pp. 241-244
    • Maccarrone, M.1    Veldink, G.A.2    Vliegenthart, J.F.G.3    Agro, A.F.4
  • 16
    • 0028535369 scopus 로고
    • Purification and characterization of pea seedling amine oxidase for crystallization studies
    • McGuirl, M. A., McCahon, C. D., McKeown, K. A., and Dooley, D. M. 1994. Purification and characterization of pea seedling amine oxidase for crystallization studies. Plant Physiol. 106:1205-1211.
    • (1994) Plant Physiol. , vol.106 , pp. 1205-1211
    • McGuirl, M.A.1    McCahon, C.D.2    McKeown, K.A.3    Dooley, D.M.4
  • 18
    • 0000868676 scopus 로고
    • Plant defense and delayed infection of alfalfa pseudonodules induced by an exopolysaccharide (Eps-I)-deficient Rhizobium meliloti mutant
    • Niehaus, K., Kapp, D., and Pühler, A. 1993. Plant defense and delayed infection of alfalfa pseudonodules induced by an exopolysaccharide (Eps-I)-deficient Rhizobium meliloti mutant. Planta 190:415-425.
    • (1993) Planta , vol.190 , pp. 415-425
    • Niehaus, K.1    Kapp, D.2    Pühler, A.3
  • 19
    • 0031685151 scopus 로고    scopus 로고
    • A Sinorhizobium meliloti lipopolysaccharide mutant induces effective nodules on the host plant Medicago sativa (alfalfa) but fails to establish a symbiosis with Medicago truncatula
    • Niehaus, K., Lagares, A., and Pühler, A. 1998. A Sinorhizobium meliloti lipopolysaccharide mutant induces effective nodules on the host plant Medicago sativa (alfalfa) but fails to establish a symbiosis with Medicago truncatula. Mol. Plant-Microbe Interact. 11:906-914.
    • (1998) Mol. Plant-Microbe Interact. , vol.11 , pp. 906-914
    • Niehaus, K.1    Lagares, A.2    Pühler, A.3
  • 20
    • 0029846567 scopus 로고    scopus 로고
    • The elicitor-induced oxidative burst in cultured chickpea cells drives the rapid insolubilization of two cell wall structural proteins
    • Otte, O., and Barz, W. 1996. The elicitor-induced oxidative burst in cultured chickpea cells drives the rapid insolubilization of two cell wall structural proteins. Planta 200:238-246.
    • (1996) Planta , vol.200 , pp. 238-246
    • Otte, O.1    Barz, W.2
  • 21
    • 0028002251 scopus 로고
    • Cytological evidence for a host defense response that reduces cell and tissue invasion in pea nodules by lipopolysaccharide-defective mutants of Rhizobium leguminosarum strain 3841
    • Perotto, S., Brewin, N. J., and Kannenberg, E. L. 1994. Cytological evidence for a host defense response that reduces cell and tissue invasion in pea nodules by lipopolysaccharide-defective mutants of Rhizobium leguminosarum strain 3841. Mol. Plant-Microbe Interact. 7:99-112.
    • (1994) Mol. Plant-Microbe Interact. , vol.7 , pp. 99-112
    • Perotto, S.1    Brewin, N.J.2    Kannenberg, E.L.3
  • 22
    • 0000597348 scopus 로고
    • Structure and growth of infection threads in the legume symbiosis with Rhizobium leguminosarum
    • Rae, A. L., Bonfantefasolo, P., and Brewin, N. J. 1992. Structure and growth of infection threads in the legume symbiosis with Rhizobium leguminosarum. Plant J. 2:385-395.
    • (1992) Plant J. , vol.2 , pp. 385-395
    • Rae, A.L.1    Bonfantefasolo, P.2    Brewin, N.J.3
  • 23
    • 0000669584 scopus 로고
    • Expression of extracellular glycoproteins in the uninfected cells of developing pea nodule tissue
    • Rae, A. L., Perotto, S., Knox, J. P., Kannenberg, E. L., and Brewin, N. J. 1991. Expression of extracellular glycoproteins in the uninfected cells of developing pea nodule tissue. Mol. Plant-Microbe Interact. 4:563-570.
    • (1991) Mol. Plant-Microbe Interact. , vol.4 , pp. 563-570
    • Rae, A.L.1    Perotto, S.2    Knox, J.P.3    Kannenberg, E.L.4    Brewin, N.J.5
  • 24
    • 0040964382 scopus 로고    scopus 로고
    • Hydrogen peroxide accumulation in Medicago truncatula roots colonized by the arbuscular mycorrhiza-forming fungus Glomus intraradices
    • Salzer, P., Corbiere, H., and Boller, T. 1999. Hydrogen peroxide accumulation in Medicago truncatula roots colonized by the arbuscular mycorrhiza-forming fungus Glomus intraradices. Planta 208:319-325.
    • (1999) Planta , vol.208 , pp. 319-325
    • Salzer, P.1    Corbiere, H.2    Boller, T.3
  • 25
    • 0027345627 scopus 로고
    • pSym nod gene influence on elicitation of peroxidase activity from white clover and pea roots by rhizobia and their cell-free supernatants
    • Salzwedel, J. L. and Dazzo, F. B. 1993. pSym nod gene influence on elicitation of peroxidase activity from white clover and pea roots by rhizobia and their cell-free supernatants. Mol. Plant-Microbe Interact. 6:127-134.
    • (1993) Mol. Plant-Microbe Interact. , vol.6 , pp. 127-134
    • Salzwedel, J.L.1    Dazzo, F.B.2
  • 26
    • 0028038501 scopus 로고
    • Localization of cell wall proteins in relation to the developmental anatomy of the carrot root apex
    • Smallwood, M., Beven, A., Donovan, N., Neill, S. J., Peart, J., Roberts, K., and Knox, J. P. 1994. Localization of cell wall proteins in relation to the developmental anatomy of the carrot root apex. Plant J. 5:237-246.
    • (1994) Plant J. , vol.5 , pp. 237-246
    • Smallwood, M.1    Beven, A.2    Donovan, N.3    Neill, S.J.4    Peart, J.5    Roberts, K.6    Knox, J.P.7
  • 27
    • 0024148185 scopus 로고
    • The di- and polyamine oxidase of plants
    • V. Zappia and A. E. Pegg, eds. Plenum Press, New York
    • Smith, T. A., and Barker, J. H. A. 1988. The di- and polyamine oxidase of plants. Pages 573-587 in: Progress in Polyamine Research. V. Zappia and A. E. Pegg, eds. Plenum Press, New York.
    • (1988) Progress in Polyamine Research , pp. 573-587
    • Smith, T.A.1    Barker, J.H.A.2
  • 28
    • 0029040435 scopus 로고
    • Cloning and molecular analysis of the pea seedling copper amine oxidase
    • Tipping, A. J., and McPherson, M. J. 1995. Cloning and molecular analysis of the pea seedling copper amine oxidase. J. Biol. Chem. 270:16939-16946.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16939-16946
    • Tipping, A.J.1    McPherson, M.J.2
  • 29
    • 0028308177 scopus 로고
    • Cell-wall degradation during infection thread formation by the root-nodule bacterium Rhizobium-leguminosarum is a 2-step process
    • van Spronsen, P. C., Bakhuizen, R., van Brussel, A. A. N., and Kijne, J. W. 1994. Cell-wall degradation during infection thread formation by the root-nodule bacterium Rhizobium-leguminosarum is a 2-step process. Eur. J. Cell Biol. 64:88-94.
    • (1994) Eur. J. Cell Biol. , vol.64 , pp. 88-94
    • Van Spronsen, P.C.1    Bakhuizen, R.2    Van Brussel, A.A.N.3    Kijne, J.W.4
  • 30
    • 0000868941 scopus 로고
    • Common components of the infection thread matrix and the intercellular space identified by immunocytochemical analysis of pea nodules and uninfected roots
    • VandenBosch, K. A., Bradley, D. J., Knox, J. P., Perotto, S., Butcher, G. W., and Brewin, N. J. 1989. Common components of the infection thread matrix and the intercellular space identified by immunocytochemical analysis of pea nodules and uninfected roots. EMBO J. 8: 335-341.
    • (1989) EMBO J. , vol.8 , pp. 335-341
    • VandenBosch, K.A.1    Bradley, D.J.2    Knox, J.P.3    Perotto, S.4    Butcher, G.W.5    Brewin, N.J.6
  • 31
    • 0001042970 scopus 로고
    • Abortion of infection during the Rhizobium meliloti-alfalfa symbiotic interaction is accompanied by a hypersensitive reaction
    • Vasse, J., Debilly, F., and Truchet, G. 1993. Abortion of infection during the Rhizobium meliloti-alfalfa symbiotic interaction is accompanied by a hypersensitive reaction. Plant J. 4:555-566.
    • (1993) Plant J. , vol.4 , pp. 555-566
    • Vasse, J.1    Debilly, F.2    Truchet, G.3
  • 32
    • 0033103289 scopus 로고    scopus 로고
    • Isolation of lipoxygenase cDNA clones from pea nodule mRNA
    • Wisniewski, J. P., Gardner, C. D., and Brewin, N. J. 1999. Isolation of lipoxygenase cDNA clones from pea nodule mRNA. Plant Mol. Biol. 39:775-783.
    • (1999) Plant Mol. Biol. , vol.39 , pp. 775-783
    • Wisniewski, J.P.1    Gardner, C.D.2    Brewin, N.J.3
  • 33
    • 0029360730 scopus 로고
    • Specificity in the immobilization of cell-wall proteins in response to different elicitor molecules in suspension-cultured cells of French bean (Phaseolus vulgaris L.)
    • Wojtaszek, P., Trethowan, J., and Bolwell, G. P. 1995. Specificity in the immobilization of cell-wall proteins in response to different elicitor molecules in suspension-cultured cells of French bean (Phaseolus vulgaris L.). Plant Mol. Biol. 28:1075-1087.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 1075-1087
    • Wojtaszek, P.1    Trethowan, J.2    Bolwell, G.P.3
  • 34
    • 0030979046 scopus 로고    scopus 로고
    • Reconstitution in vitro of the components and conditions required for the oxidative cross-linking of extracellular proteins in French bean (Phaseolus vulgaris L.)
    • Wojtaszek, P., Trethowan, J., and Bolwell, G. P. 1997. Reconstitution in vitro of the components and conditions required for the oxidative cross-linking of extracellular proteins in French bean (Phaseolus vulgaris L.). FEBS Lett. 405:95-98.
    • (1997) FEBS Lett. , vol.405 , pp. 95-98
    • Wojtaszek, P.1    Trethowan, J.2    Bolwell, G.P.3
  • 35
    • 0024725592 scopus 로고
    • Genetic derepression of a developmentally regulated lipopolysaccharide antigen from Rhizobium leguminosarum 3841
    • Wood, E. A., Butcher, G. W., Brewin, N. J., and Kannenberg, E. L. 1989. Genetic derepression of a developmentally regulated lipopolysaccharide antigen from Rhizobium leguminosarum 3841. J. Bacteriol. 171: 4549-4555.
    • (1989) J. Bacteriol. , vol.171 , pp. 4549-4555
    • Wood, E.A.1    Butcher, G.W.2    Brewin, N.J.3    Kannenberg, E.L.4


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