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Volumn 21, Issue 2, 2008, Pages 171-177

The expression of a bean PGIP in transgenic wheat confers increased resistance to the fungal pathogen Bipolaris sorokiniana

Author keywords

[No Author keywords available]

Indexed keywords

PGIP PROTEIN, PLANT; POLYGALACTURONASE; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 38349147028     PISSN: 08940282     EISSN: None     Source Type: Journal    
DOI: 10.1094/MPMI-21-2-0171     Document Type: Article
Times cited : (86)

References (36)
  • 1
    • 13844316078 scopus 로고    scopus 로고
    • Evaluation of tolerance to Pierce's disease and Botrytis in transgenic plants of Vitis vinifera L. expressing the pear PGIP gene
    • Aguero, C. B., Uratsu, S. L., Greve, C., Powell, A. T., Labavitch, J. M., Meredith, C. P., and Dandekar, A. M. 2005. Evaluation of tolerance to Pierce's disease and Botrytis in transgenic plants of Vitis vinifera L. expressing the pear PGIP gene. Mol. Plant Pathol. 6:43-51.
    • (2005) Mol. Plant Pathol , vol.6 , pp. 43-51
    • Aguero, C.B.1    Uratsu, S.L.2    Greve, C.3    Powell, A.T.4    Labavitch, J.M.5    Meredith, C.P.6    Dandekar, A.M.7
  • 2
    • 0015858165 scopus 로고
    • New method for quantitative determination of uronic acids
    • Blumenkrantz, N., and Asboe-Hansen, G. 1973. New method for quantitative determination of uronic acids. Anal. Biochem. 54:484-489.
    • (1973) Anal. Biochem , vol.54 , pp. 484-489
    • Blumenkrantz, N.1    Asboe-Hansen, G.2
  • 3
    • 0030237034 scopus 로고    scopus 로고
    • Mutagenesis of endopolygalacturonase from Fusarium moniliforme: Histidine residue 234 is critical for enzymatic and macerating activities and not for binding to polygalacturonase-inhibiting protein (PGIP)
    • Caprari, C., Mattei, B., Basile, M. L., Salvi, G., Crescenzi, V., De Lorenzo, G., and Cervone, F. 1996. Mutagenesis of endopolygalacturonase from Fusarium moniliforme: Histidine residue 234 is critical for enzymatic and macerating activities and not for binding to polygalacturonase-inhibiting protein (PGIP). Mol. Plant-Microbe Interact 9:617-624.
    • (1996) Mol. Plant-Microbe Interact , vol.9 , pp. 617-624
    • Caprari, C.1    Mattei, B.2    Basile, M.L.3    Salvi, G.4    Crescenzi, V.5    De Lorenzo, G.6    Cervone, F.7
  • 4
    • 0002467899 scopus 로고    scopus 로고
    • Perception of fungal elicitors and signal transduction
    • P. Aducci, ed. Birkhauser Verlag, Basel, Switzerland
    • Cervone, F., Castoria, R., Leckie, F., and De Lorenzo, G. 1997. Perception of fungal elicitors and signal transduction. In: Signal Transduction in plants. P. Aducci, ed. Birkhauser Verlag, Basel, Switzerland.
    • (1997) Signal Transduction in plants
    • Cervone, F.1    Castoria, R.2    Leckie, F.3    De Lorenzo, G.4
  • 5
    • 0030138945 scopus 로고    scopus 로고
    • Ubiquitin promoter-based vectors for high-level expression of selectable and/or screenable marker genes in monocotyledonous plants
    • Christensen, A. H., and Quail, P. F. 1996. Ubiquitin promoter-based vectors for high-level expression of selectable and/or screenable marker genes in monocotyledonous plants. Trans. Res. 5:213-218.
    • (1996) Trans. Res , vol.5 , pp. 213-218
    • Christensen, A.H.1    Quail, P.F.2
  • 6
    • 0030726836 scopus 로고    scopus 로고
    • Isolation and characterization of an endopolygalacturonase from Cochliobolus sativus and a cytological study of fungal penetration of barley
    • Clay, R. P., Bergmann, C. W., and Fuller, M. S. 1997. Isolation and characterization of an endopolygalacturonase from Cochliobolus sativus and a cytological study of fungal penetration of barley. Phytopathology 87:1148-1159.
    • (1997) Phytopathology , vol.87 , pp. 1148-1159
    • Clay, R.P.1    Bergmann, C.W.2    Fuller, M.S.3
  • 7
    • 0034789069 scopus 로고    scopus 로고
    • The role of polygalacturonase-inhibiting proteins (PGIPs) in defense against pathogenic fungi
    • De Lorenzo, G., D'Ovidio, R., and Cervone, F. 2001. The role of polygalacturonase-inhibiting proteins (PGIPs) in defense against pathogenic fungi. Annu. Rev. Phytopathol. 39:313-335.
    • (2001) Annu. Rev. Phytopathol , vol.39 , pp. 313-335
    • De Lorenzo, G.1    D'Ovidio, R.2    Cervone, F.3
  • 9
    • 0043192812 scopus 로고    scopus 로고
    • The crystal structure of polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat involved in plant defense
    • Di Matteo, A., Federici, L., Mattei, B., Salvi, G., Johnson, K. A., Savino, C., De Lorenzo, G., and Tsernoglou, D. 2003. The crystal structure of polygalacturonase-inhibiting protein (PGIP), a leucine-rich repeat involved in plant defense. Plant Biol. 100:10124-10128.
    • (2003) Plant Biol , vol.100 , pp. 10124-10128
    • Di Matteo, A.1    Federici, L.2    Mattei, B.3    Salvi, G.4    Johnson, K.A.5    Savino, C.6    De Lorenzo, G.7    Tsernoglou, D.8
  • 10
    • 0028057017 scopus 로고
    • Purification and molecular characterization of a soybean polygalacturonase-inhibiting protein
    • D'Ovidio, R., and Anderson, O. D. 1994 Purification and molecular characterization of a soybean polygalacturonase-inhibiting protein. Theor. Appl. Genet 88:759-763
    • (1994) Theor. Appl. Genet , vol.88 , pp. 759-763
    • D'Ovidio, R.1    Anderson, O.D.2
  • 11
    • 0002651071 scopus 로고
    • Isolation of an alpha-type gliadin gene from Triticum durum Desf. and genetic polymorphism at the Gli-2 locus
    • D'Ovidio, R., Tanzarella, O. A., and Porceddu, E. 1992. Isolation of an alpha-type gliadin gene from Triticum durum Desf. and genetic polymorphism at the Gli-2 locus. Genet. Breed. 46:41-48.
    • (1992) Genet. Breed , vol.46 , pp. 41-48
    • D'Ovidio, R.1    Tanzarella, O.A.2    Porceddu, E.3
  • 12
    • 1042289393 scopus 로고    scopus 로고
    • Polygalacturonases, polygalacturonase-inhibiting proteins and pectic oligomers in plant-pathogen interactions
    • D'Ovidio, R., Mattei, B., Roberti, S., and Bellincampi, D. 2004. Polygalacturonases, polygalacturonase-inhibiting proteins and pectic oligomers in plant-pathogen interactions. Biochim. Biophys. Acta 1696:237-244.
    • (2004) Biochim. Biophys. Acta , vol.1696 , pp. 237-244
    • D'Ovidio, R.1    Mattei, B.2    Roberti, S.3    Bellincampi, D.4
  • 13
    • 0030669654 scopus 로고    scopus 로고
    • Polygalacturonase inhibiting proteins from Allium porrum L. and their role in plant tissue against fungal endo-polygalacturonases
    • Favaron, F., Castiglioni, C., D'Ovidio, R., and Alghisi, P. 1997. Polygalacturonase inhibiting proteins from Allium porrum L. and their role in plant tissue against fungal endo-polygalacturonases. Physiol. Mol. Plant Pathol. 50:403-417.
    • (1997) Physiol. Mol. Plant Pathol , vol.50 , pp. 403-417
    • Favaron, F.1    Castiglioni, C.2    D'Ovidio, R.3    Alghisi, P.4
  • 14
    • 8844285272 scopus 로고    scopus 로고
    • Relationships among endopolygalacturonase, oxalate, pH and plant polygalacturonase-inhibiting protein (PGIP) in the interaction between Sclerotinia sclerotiorum and soybean
    • Favaron F., Sella L., and D'Ovidio R. 2004. Relationships among endopolygalacturonase, oxalate, pH and plant polygalacturonase-inhibiting protein (PGIP) in the interaction between Sclerotinia sclerotiorum and soybean. Mol. Plant-Microbe Interact. 17:1402-1409.
    • (2004) Mol. Plant-Microbe Interact , vol.17 , pp. 1402-1409
    • Favaron, F.1    Sella, L.2    D'Ovidio, R.3
  • 15
    • 0347925092 scopus 로고    scopus 로고
    • Arabidopsis polygalacturonase-inhibiting proteins (PGIP) are regulated by different signal transduction pathways during fungal infection
    • Ferrari, S., Vairo, D., Ausubel, F. M., Cervone, F., and De Lorenzo, G. 2003. Arabidopsis polygalacturonase-inhibiting proteins (PGIP) are regulated by different signal transduction pathways during fungal infection. Plant Cell 15:93-106.
    • (2003) Plant Cell , vol.15 , pp. 93-106
    • Ferrari, S.1    Vairo, D.2    Ausubel, F.M.3    Cervone, F.4    De Lorenzo, G.5
  • 16
    • 0033749605 scopus 로고    scopus 로고
    • Polygalacturonases are required for rapid colonization and full virulence of Ralstonia solanacearum on tomato plants
    • Huang, Q., and Allen, C. 2000. Polygalacturonases are required for rapid colonization and full virulence of Ralstonia solanacearum on tomato plants. Physiol. Mol. Plant Pathol. 57:176-186.
    • (2000) Physiol. Mol. Plant Pathol , vol.57 , pp. 176-186
    • Huang, Q.1    Allen, C.2
  • 17
    • 0035018083 scopus 로고    scopus 로고
    • Endopolygalacturonase is essential for citrus black rot caused by Alternaria citri but not brown spot caused by Alternaria alternata
    • Isshiki, A., Akimitsu, K., Yamamoto, M., and Yamamoto, H. 2001. Endopolygalacturonase is essential for citrus black rot caused by Alternaria citri but not brown spot caused by Alternaria alternata. Mol. Plant-Microbe Interact. 14:749-757.
    • (2001) Mol. Plant-Microbe Interact , vol.14 , pp. 749-757
    • Isshiki, A.1    Akimitsu, K.2    Yamamoto, M.3    Yamamoto, H.4
  • 18
    • 77956742948 scopus 로고    scopus 로고
    • The roles of leucine rich repeats in plant defences
    • Jones, D. A., and Jones, J. D. G. 1997. The roles of leucine rich repeats in plant defences. Adv. Bot. Res. Adv. Plant Pathol. 24:90-167.
    • (1997) Adv. Bot. Res. Adv. Plant Pathol , vol.24 , pp. 90-167
    • Jones, D.A.1    Jones, J.D.G.2
  • 19
    • 33751501231 scopus 로고    scopus 로고
    • The grapevine polygalacturonase-inhibiting protein (VvPGIP1) reduces Botrytis cinerea susceptibility in transgenic tobacco and differentially inhibits fungal polygalacturonases
    • Joubert, D. A., Slaughter, A. R., Kemp, G., Becker, V. W. J., Krooshof, G. H., Bergmann, C., Benen, J., Pretorius, I. S., and Vivier, M. A. 2006. The grapevine polygalacturonase-inhibiting protein (VvPGIP1) reduces Botrytis cinerea susceptibility in transgenic tobacco and differentially inhibits fungal polygalacturonases. Transgenic Res. 15:687-702.
    • (2006) Transgenic Res , vol.15 , pp. 687-702
    • Joubert, D.A.1    Slaughter, A.R.2    Kemp, G.3    Becker, V.W.J.4    Krooshof, G.H.5    Bergmann, C.6    Benen, J.7    Pretorius, I.S.8    Vivier, M.A.9
  • 22
    • 0033522402 scopus 로고    scopus 로고
    • The specificity of polygalacturonase-inhibiting protein (PGIP): A single amino acid substitution in the solvent-exposed β-strand/β-turn region of the leucine-rich repeats (LRRs) confers a new recognition capability
    • Leckie, F., Mattei, B., Capodicasa, C., Hemmings, A., Nuss, L., Aracri, B., De Lorenzo, G., and Cervone, F. 1999. The specificity of polygalacturonase-inhibiting protein (PGIP): A single amino acid substitution in the solvent-exposed β-strand/β-turn region of the leucine-rich repeats (LRRs) confers a new recognition capability. EMBO (Eur. Mol. Biol. Organ.) J. 18:2352-2363.
    • (1999) EMBO (Eur. Mol. Biol. Organ.) J , vol.18 , pp. 2352-2363
    • Leckie, F.1    Mattei, B.2    Capodicasa, C.3    Hemmings, A.4    Nuss, L.5    Aracri, B.6    De Lorenzo, G.7    Cervone, F.8
  • 23
    • 31744435195 scopus 로고    scopus 로고
    • Polygalacturonase-inhibiting protein 2 of Phaseolus vulgaris inhibits BcPG1, a polygalacturonase of Botrytis cinerea important for pathogenicity, and protects transgenic plants from infection
    • Manfredini, C., Sicilia, F., Ferrari, S., Pontiggia, D., Salvi, G., Caprai, C., Lorito, M., and De Lorenzo, G. 2006. Polygalacturonase-inhibiting protein 2 of Phaseolus vulgaris inhibits BcPG1, a polygalacturonase of Botrytis cinerea important for pathogenicity, and protects transgenic plants from infection. Physiol. Mol. Plant Pathol. 67:108-115.
    • (2006) Physiol. Mol. Plant Pathol , vol.67 , pp. 108-115
    • Manfredini, C.1    Sicilia, F.2    Ferrari, S.3    Pontiggia, D.4    Salvi, G.5    Caprai, C.6    Lorito, M.7    De Lorenzo, G.8
  • 24
    • 0000854587 scopus 로고
    • A copper reagent for the determination of hexuronic acids and certain ketohexoses
    • Milner, Y., and Avigad, G. 1967. A copper reagent for the determination of hexuronic acids and certain ketohexoses. Carbohydr. Res. 4:359-361.
    • (1967) Carbohydr. Res , vol.4 , pp. 359-361
    • Milner, Y.1    Avigad, G.2
  • 25
    • 0036343103 scopus 로고    scopus 로고
    • Polygalacturonase is a pathogenicity factor in Claviceps purpurea/rye interaction
    • Oeser, B., Heidrich, P. M., Muller, U., Tudzynski, P., and Tenberge, K. B. 2002. Polygalacturonase is a pathogenicity factor in Claviceps purpurea/rye interaction. Fungal Genet. Biol. 36:176-186.
    • (2002) Fungal Genet. Biol , vol.36 , pp. 176-186
    • Oeser, B.1    Heidrich, P.M.2    Muller, U.3    Tudzynski, P.4    Tenberge, K.B.5
  • 26
    • 0036984378 scopus 로고    scopus 로고
    • Engineering deoxynivalenol metabolism in wheat through expression of a fungal trichothecene acetyltransferase gene
    • Okubara, P. A., Blechl, A. E., McCormick, S. P., Alexander, N. J., Dill-Macky, R., and Hohn, T. M. 2002. Engineering deoxynivalenol metabolism in wheat through expression of a fungal trichothecene acetyltransferase gene. Theor. Appl. Genet. 106:74-83.
    • (2002) Theor. Appl. Genet , vol.106 , pp. 74-83
    • Okubara, P.A.1    Blechl, A.E.2    McCormick, S.P.3    Alexander, N.J.4    Dill-Macky, R.5    Hohn, T.M.6
  • 28
    • 0022344608 scopus 로고
    • An activity stain for the rapid characterization of pectic enzymes in isoelectric focusing and sodium dodecyl sulfate polyacrylamide gels
    • Ried, J. L., and Collmer, A. 1985. An activity stain for the rapid characterization of pectic enzymes in isoelectric focusing and sodium dodecyl sulfate polyacrylamide gels. Appl. Environ. Microbiol. 50:615-622.
    • (1985) Appl. Environ. Microbiol , vol.50 , pp. 615-622
    • Ried, J.L.1    Collmer, A.2
  • 29
    • 0035800186 scopus 로고    scopus 로고
    • Pectins: Structure, biosynthesis, and oligogalacturonide-related signaling
    • Ridley, B. L., O'Neill, M. A., and Mohnen, D. 2001. Pectins: Structure, biosynthesis, and oligogalacturonide-related signaling. Phytochemistry 57:929-967.
    • (2001) Phytochemistry , vol.57 , pp. 929-967
    • Ridley, B.L.1    O'Neill, M.A.2    Mohnen, D.3
  • 30
    • 0026000437 scopus 로고
    • Polygalacturonase is a virulence factor in Agrobacterium tumefaciens biovar 3
    • Rodriguez-Palenzuela, P., Burr, J., and Collmer, A. 1991. Polygalacturonase is a virulence factor in Agrobacterium tumefaciens biovar 3. J. Bacteriol. 173:6547-6552.
    • (1991) J. Bacteriol , vol.173 , pp. 6547-6552
    • Rodriguez-Palenzuela, P.1    Burr, J.2    Collmer, A.3
  • 31
    • 0001470646 scopus 로고
    • A Polygalacturnase-Inhibiting Protein in the flowers of Phaseolus vulgaris L
    • Salvi, G., Giarrizzo, F., De Lorenzo, G., and Cervone, F. 1990. A Polygalacturnase-Inhibiting Protein in the flowers of Phaseolus vulgaris L. J. Plant Physiol. 136:513-518.
    • (1990) J. Plant Physiol , vol.136 , pp. 513-518
    • Salvi, G.1    Giarrizzo, F.2    De Lorenzo, G.3    Cervone, F.4
  • 33
    • 33745659241 scopus 로고    scopus 로고
    • Polygalacturonase- inhibiting protein interacts with pectin through a binding site formed by four clustered residues of arginine and lysine
    • Spadoni, S., Zabotina, O., Di Matteo, A., Mikkelsen, J. D., Cervone, F., De Lorenzo, G., Mattei, B., and Bellincampi, D. 2006. Polygalacturonase- inhibiting protein interacts with pectin through a binding site formed by four clustered residues of arginine and lysine. Plant Physiol. 141:557-564.
    • (2006) Plant Physiol , vol.141 , pp. 557-564
    • Spadoni, S.1    Zabotina, O.2    Di Matteo, A.3    Mikkelsen, J.D.4    Cervone, F.5    De Lorenzo, G.6    Mattei, B.7    Bellincampi, D.8
  • 34
    • 51249171888 scopus 로고
    • A rapid and inexpensive method for isolation of total DNA from dehydrated plant tissue
    • Tai, T. H., and Tanksley, S. D. 1991. A rapid and inexpensive method for isolation of total DNA from dehydrated plant tissue. Plant Mol. Biol. Rep. 8:297-303.
    • (1991) Plant Mol. Biol. Rep , vol.8 , pp. 297-303
    • Tai, T.H.1    Tanksley, S.D.2
  • 35
    • 0000741223 scopus 로고
    • An improved diffusion assay for quantifying the polygalacturonase content of Erwinia culture filtrates
    • Taylor, R. J., and Secor, G. A. 1988. An improved diffusion assay for quantifying the polygalacturonase content of Erwinia culture filtrates. Phytopathology 78:1101-1103.
    • (1988) Phytopathology , vol.78 , pp. 1101-1103
    • Taylor, R.J.1    Secor, G.A.2
  • 36
    • 0032190199 scopus 로고    scopus 로고
    • The endopolygalacturonase gene Bcpg1 is required for full virulence of Botrytis cinerea
    • ten Have, A., Mulder, W., Visser, J., van Kaan, J. A. L. 1998. The endopolygalacturonase gene Bcpg1 is required for full virulence of Botrytis cinerea. Mol. Plant-Microbe Interact. 11:1009-1016.
    • (1998) Mol. Plant-Microbe Interact , vol.11 , pp. 1009-1016
    • ten Have, A.1    Mulder, W.2    Visser, J.3    van Kaan, J.A.L.4


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