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Volumn 25, Issue 2, 2012, Pages 200-210

Silencing and heterologous expression of ppo-2 indicate a specific function of a single polyphenol oxidase isoform in resistance of dandelion (Taraxacum officinale) against Pseudomonas syringae pv. tomato

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; CATECHOL OXIDASE; COMPLEMENTARY DNA; ISOENZYME; PLANT EXTRACT; PLANT RNA; VEGETABLE PROTEIN;

EID: 84856160588     PISSN: 08940282     EISSN: None     Source Type: Journal    
DOI: 10.1094/MPMI-04-11-0082     Document Type: Article
Times cited : (47)

References (52)
  • 1
    • 0018899012 scopus 로고
    • Comparison of three pathogenesis-related proteins from plants of two cultivars of tobacco infected with TMV
    • Antoniw, J. F., Ritter, C. E., Pierpoint, W. S., and van Loon, L. C. 1980. Comparison of three pathogenesis-related proteins from plants of two cultivars of tobacco infected with TMV. J. Gen. Virol. 47:79-87. (Pubitemid 10105190)
    • (1980) Journal of General Virology , vol.47 , Issue.1 , pp. 79-87
    • Antoniw, J.F.1    Ritter, C.E.2    Pierpoint, W.S.3    Van Loon, L.C.4
  • 2
    • 0000097307 scopus 로고
    • Peroxidase, polyphenoloxidase, and phenols in relation to resistance against Pseudomonas syringae pv tomato in tomato plants
    • Bashan, Y., Okon, Y., and Henis, Y. 1987. Peroxidase, polyphenoloxidase, and phenols in relation to resistance against Pseudomonas syringae pv. tomato in tomato plants. Can. J. Bot. 65:366-372.
    • (1987) Can. J. Bot. , vol.65 , pp. 366-372
    • Bashan, Y.1    Okon, Y.2    Henis, Y.3
  • 3
    • 0033180574 scopus 로고    scopus 로고
    • Role of active oxygen species and NO in plant defence responses
    • DOI 10.1016/S1369-5266(99)80051-X
    • Bolwell, G. P. 1999. Role of active oxygen species and NO in plant defence responses. Curr. Opin. Plant Biol. 2:287-294. (Pubitemid 29365675)
    • (1999) Current Opinion in Plant Biology , vol.2 , Issue.4 , pp. 287-294
    • Bolwell, G.P.1
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0033997843 scopus 로고    scopus 로고
    • An improved method for the isolation of total RNA from Malva pusilla tissues infected with Colletotrichum gloeosporioides
    • DOI 10.1046/j.1439-0434.2000.00470.x
    • Chen, G. Y.-J., Jin, S., and Goodwin, P. H. 2000. An improved method for the isolation of total RNA from Malva pusilla tissues infected with Colletotrichum gloeosporioides. J. Phytopathol. 148:57-60. (Pubitemid 30112553)
    • (2000) Journal of Phytopathology , vol.148 , Issue.1 , pp. 57-60
    • Chen, G.Y.-J.1    Jin, S.2    Goodwin, P.H.3
  • 6
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough, S., 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.1    Bent, A.F.2
  • 7
    • 0035111563 scopus 로고    scopus 로고
    • Control of enzymatic browning in potato (solanum tuberosum L.) by sense and antisense RNA from tomato polyphenol oxidase
    • DOI 10.1021/jf001217f
    • Coetzer, C., Corsini, D., Love, S., Pavek, J., and Tumer, N. 2001. Control of enzymatic browning in potato (Solanum tuberosum L.) by sense and antisense RNA from tomato polyphenol oxidase. J. Agric. Food Chem. 49:652-657. (Pubitemid 32172607)
    • (2001) Journal of Agricultural and Food Chemistry , vol.49 , Issue.2 , pp. 652-657
    • Coetzer, C.1    Corsini, D.2    Love, S.3    Pavek, J.4    Turner, N.5
  • 8
    • 0000479431 scopus 로고
    • Isolation of plant DNA from fresh tissue
    • Doyle, J. J., and Doyle, J. L. 1990. Isolation of plant DNA from fresh tissue. Focus 12:13-15.
    • (1990) Focus , vol.12 , pp. 13-15
    • Doyle, J.J.1    Doyle, J.L.2
  • 10
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites
    • Emanuelsson, O., Nielsen, H., and von Heijne, G. 1999. ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites. Protein Sci. 8:978-984. (Pubitemid 29211735)
    • (1999) Protein Science , vol.8 , Issue.5 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    Von Heijne, G.3
  • 12
    • 0010305758 scopus 로고
    • Activation of plant foliar oxidases by insect feeding reduces nutritive quality of foliage for noctuid herbivores
    • Felton, G. W., Donato, K., Del Vecchio, R. J., and Duffey, S. S. 1989. Activation of plant foliar oxidases by insect feeding reduces nutritive quality of foliage for noctuid herbivores. J. Chem. Ecol. 15:2667-2694.
    • (1989) J. Chem. Ecol. , vol.15 , pp. 2667-2694
    • Felton, G.W.1    Donato, K.2    Del Vecchio, R.J.3    Duffey, S.S.4
  • 13
    • 44049116662 scopus 로고
    • Impact of oxidized plant phenolics on the nutritional quality of dietary protein to a noctuid herbivore Spodoptera exigua
    • Felton, G. W., Donato, K. K., Broadway, R. M., and Duffey, S. S. 1992. Impact of oxidized plant phenolics on the nutritional quality of dietary protein to a noctuid herbivore, Spodoptera exigua. J. Insect Physiol. 38:277-285.
    • (1992) J. Insect Physiol. , vol.38 , pp. 277-285
    • Felton, G.W.1    Donato, K.K.2    Broadway, R.M.3    Duffey, S.S.4
  • 15
    • 0020196416 scopus 로고
    • Transcription of Cauliflower mosaic virus DNA: Detection of promoter sequences, and characterization of transcripts
    • Guilley, H., Dudley, R. K., Jonard, G., Balazs, E., and Richards, K. E. 1982. Transcription of Cauliflower mosaic virus DNA: Detection of promoter sequences, and characterization of transcripts. Cell 30:763-773.
    • (1982) Cell , vol.30 , pp. 763-773
    • Guilley, H.1    Dudley, R.K.2    Jonard, G.3    Balazs, E.4    Richards, K.E.5
  • 16
    • 0030266346 scopus 로고    scopus 로고
    • Resistance gene-dependent plant defense responses
    • DOI 10.1105/tpc.8.10.1773
    • Hammond-Kosack, K. E., and Jones, J. D. G. 1996. Resistance genedependent plant defense responses. Plant Cell 8:1773-1791. (Pubitemid 27012404)
    • (1996) Plant Cell , vol.8 , Issue.10 , pp. 1773-1791
    • Hammond-Kosack, K.E.1    Jones, J.D.G.2
  • 17
    • 0020574525 scopus 로고
    • A binary plant vector strategy based on separation of vir- and T-region of the Agrobacterium tumefaciens Ti-plasmid
    • Hoekema, A., Hirsch, P. R., Hooykaas, P. J. J., and Schilperoort, R. A. 1983. A binary plant vector strategy based on separation on vir- and T-region of the Agrobacterium tumefaciens Ti-plasmid. Nature 303:179-180. (Pubitemid 13081082)
    • (1983) Nature , vol.303 , Issue.5913 , pp. 179-180
    • Hoekema, A.1    Hirsch, P.R.2    Hooykaas, P.J.J.3    Schilperoort, R.A.4
  • 18
    • 0001569083 scopus 로고
    • New Agrobacterium helper plasmid for gene transfer to plants (EHA 105)
    • Hood, E. E., Gelvin, S. B., Melchers, S., and Hoekema, A. 1993. New Agrobacterium helper plasmid for gene transfer to plants (EHA 105). Transgenic Res. 2:208-218.
    • (1993) Transgenic Res. , vol.2 , pp. 208-218
    • Hood, E.E.1    Gelvin, S.B.2    Melchers, S.3    Hoekema, A.4
  • 19
    • 51249176890 scopus 로고
    • Assaying chimeric genes in plants: The GUS gene fusion system
    • Jefferson, R. A. 1987. Assaying chimeric genes in plants: The GUS gene fusion system. Plant Mol. Biol. Rep. 5:387-405.
    • (1987) Plant Mol. Biol. Rep. , vol.5 , pp. 387-405
    • Jefferson, R.A.1
  • 21
    • 0030113929 scopus 로고    scopus 로고
    • Calcium-mediated apoptosis in a plant hypersensitive disease resistance response
    • Levine, A., Pennell, R. I., Alvarez, M. E., Palmer, R., and Lamb, C. 1996. Calcium-mediated apoptosis in a plant hypersensitive disease resistance response. Curr. Biol. 6:427-437. (Pubitemid 126656290)
    • (1996) Current Biology , vol.6 , Issue.4 , pp. 427-437
    • Levine, A.1    Pennell, R.I.2    Alvarez, M.E.3    Palmer, R.4    Lamb, C.5
  • 22
    • 0036939059 scopus 로고    scopus 로고
    • Overexpression of polyphenol oxidase in transgenic tomato plants results in enhanced bacterial disease resistance
    • DOI 10.1007/s00425-002-0750-4
    • Li, L., and Steffens, J. C. 2002. Overexpression of polyphenol oxidase in transgenic tomato plants results in enhanced bacterial disease resistance. Planta 215:239-247. (Pubitemid 36064973)
    • (2002) Planta , vol.215 , Issue.2 , pp. 239-247
    • Li, L.1    Steffens, J.C.2
  • 23
    • 0035710746 scopus 로고    scopus 로고
    • -ΔΔCT method
    • DOI 10.1006/meth.2001.1262
    • Livak, K. J., and Schmittgen, T. D. 2001. Analysis of relative gene expression data using real-time quantitative PCR and the 2[-delta delta(CT)] method. Methods 25:402-408. (Pubitemid 34164012)
    • (2001) Methods , vol.25 , Issue.4 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 24
    • 46149132278 scopus 로고
    • Polyphenol oxidase in plant-recent progress
    • Mayer, A. M. 1987. Polyphenol oxidase in plant-recent progress. Phytochemistry 26:11-20.
    • (1987) Phytochemistry , vol.26 , pp. 11-20
    • Mayer, A.M.1
  • 25
    • 33749517866 scopus 로고    scopus 로고
    • Polyphenol oxidases in plants and fungi: Going places? A review
    • DOI 10.1016/j.phytochem.2006.08.006, PII S0031942206004560
    • Mayer, A. M. 2006. Polyphenol oxidases in plants and fungi: Going places? A review. Phytochemistry 67:2318-2331. (Pubitemid 44527933)
    • (2006) Phytochemistry , vol.67 , Issue.21 , pp. 2318-2331
    • Mayer, A.M.1
  • 26
    • 49249153466 scopus 로고
    • Polyphenol oxidases in plants
    • Mayer, A. M., and Harel, E. 1979. Polyphenol oxidases in plants. Phytochemistry 31:193-215.
    • (1979) Phytochemistry , vol.31 , pp. 193-215
    • Mayer, A.M.1    Harel, E.2
  • 28
    • 0035259944 scopus 로고    scopus 로고
    • A transgenic apple callus showing reduced polyphenol oxidase activity and lower browning potential
    • DOI 10.1271/bbb.65.383
    • Murata, M., Nishimura, M., Murai, N., Haruta, M., Homma, S., and Itoh, Y. 2001. A transgenic apple callus showing reduced polyphenol oxidase activity and low browning potential. Biosci. Biotechnol. Biochem. 65:383-388. (Pubitemid 33626250)
    • (2001) Bioscience, Biotechnology and Biochemistry , vol.65 , Issue.2 , pp. 383-388
    • Murata, M.1    Nishimura, M.2    Murai, N.3    Haruta, M.4    Homma, S.5    Itoh, Y.6
  • 29
    • 33744960267 scopus 로고    scopus 로고
    • Induction and accumulation of polyphenol oxidase activities as implicated in development of resistance against pearl millet downy mildew disease
    • DOI 10.1071/FP06003
    • Niranjan Raj, S., Sarosh, B. R., and Shetty, H. S., 2006. Induction and accumulation of polyphenol oxidase activities as implicated in development of resistance against pearl millet downy mildew disease. Funct. Plant Biol. 33:563-571. (Pubitemid 43854201)
    • (2006) Functional Plant Biology , vol.33 , Issue.6 , pp. 563-571
    • Niranjan Raj, S.1    Sarosh, B.R.2    Shetty, H.S.3
  • 30
    • 33846227093 scopus 로고    scopus 로고
    • Flavonoid oxidation in plants: from biochemical properties to physiological functions
    • DOI 10.1016/j.tplants.2006.11.006, PII S1360138506003141
    • Pourcel, L., Routaboul, J.-M., Cheynier, V., Lepiniec, L., Debeaujon, I., 2007. Flavonoid oxidation in plants: From biochemical properties to physiological functions. Trends Plant Sci. 12:29-36. (Pubitemid 46096808)
    • (2007) Trends in Plant Science , vol.12 , Issue.1 , pp. 29-36
    • Pourcel, L.1    Routaboul, J.-M.2    Cheynier, V.3    Lepiniec, L.4    Debeaujon, I.5
  • 31
    • 0345279970 scopus 로고    scopus 로고
    • Evidence for three different specific saponin-detoxifying activities in Botrytis cinerea and cloning and functional analysis of a gene coding for a putative avenacinase
    • DOI 10.1023/A:1008796006051
    • Quidde, T., Büttner, P., and Tudzynski, P. 1999. Evidence for 3 different specific saponin-detoxyfying activities in Botrytis cinerea and cloning and functional analysis of a gene coding for a putative avenacinase. Eur. J. Plant Pathol. 105:273-283. (Pubitemid 29324166)
    • (1999) European Journal of Plant Pathology , vol.105 , Issue.3 , pp. 273-283
    • Quidde, T.1    Buttner, P.2    Tudzynski, P.3
  • 32
    • 0001722618 scopus 로고
    • The origin of Taraxacum agamospecies
    • Richards, A. J. 1973. The origin of Taraxacum agamospecies. Bot. J. Linn. Soc. 66:189-211.
    • (1973) Bot. J. Linn. Soc. , vol.66 , pp. 189-211
    • Richards, A.J.1
  • 33
    • 0000201402 scopus 로고
    • Activation of a bean chitinase promoter in transgenic tobacco plants by phytopathogenic fungi
    • Roby, D., Broglie, K., Cressman, R., Biddle, P., Chet, I., and Broglie, R. 1990. Activation of a bean chitinase promoter in transgenic tobacco plants by phytopathogenic fungi. Plant Cell 2:999-1007. (Pubitemid 120015452)
    • (1990) Plant Cell , vol.2 , Issue.10 , pp. 999-1007
    • Roby, D.1    Brogue, K.2    Cressman, R.3    Biddle, P.4    Chet, I.5    Broglie, R.6
  • 36
    • 16544395540 scopus 로고    scopus 로고
    • Cloning and characterization of red clover polyphenol oxidase cDNAs and expressing of active protein in Escherichia coli and transgenic alfalfa
    • Sullivan, M. L., Hatfield, R. D., Thoma, S. L., and Samac, D. A. 2004. Cloning and characterization of red clover polyphenol oxidase cDNAs and expressing of active protein in Escherichia coli and transgenic alfalfa. Plant Physiol. 136:3234-3244.
    • (2004) Plant Physiol. , vol.136 , pp. 3234-3244
    • Sullivan, M.L.1    Hatfield, R.D.2    Thoma, S.L.3    Samac, D.A.4
  • 38
    • 11144325647 scopus 로고    scopus 로고
    • Antisense downregulation of polyphenol oxidase results in enhanced disease susceptibility
    • DOI 10.1007/s00425-004-1330-6
    • Thipyapong, P., Hunt, M. D., and Steffens, J.C. 2004a. Antisense downregulation of polyphenol oxidase results in enhanced disease susceptibility. Planta 220:105-117. (Pubitemid 40033005)
    • (2004) Planta , vol.220 , Issue.1 , pp. 105-117
    • Thipyapong, P.1    Hunt, M.D.2    Steffens, J.C.3
  • 39
    • 3543054123 scopus 로고    scopus 로고
    • Suppression of polyphenol oxidases increases stress tolerance in tomato
    • DOI 10.1016/j.plantsci.2004.04.008, PII S0168945204001621
    • Thipyapong, P., Melkonian, J., Wolfe, D. W., and Steffens, J. C. 2004b. Suppression of polyphenol oxidases increases stress tolerance in tomato. Plant Sci. 167:693-703. (Pubitemid 39017392)
    • (2004) Plant Science , vol.167 , Issue.4 , pp. 693-703
    • Thipyapong, P.1    Melkonian, J.2    Wolfe, D.W.3    Steffens, J.C.4
  • 40
    • 34548433005 scopus 로고    scopus 로고
    • Functional analysis of polyphenol oxidase by antisense/sense technology
    • Thipyapong, P., Stout, M. J., and Attajarusit, J. 2007. Functional analysis of polyphenol oxidase by antisense/sense technology. Molecules 12:1569-1595.
    • (2007) Molecules , vol.12 , pp. 1569-1595
    • Thipyapong, P.1    Stout, M.J.2    Attajarusit, J.3
  • 42
    • 1642322999 scopus 로고    scopus 로고
    • Formation of unreduced megaspores (diplospoy) in apomictic dandelions (Taraxacum officinale, s.l.) is controlled by a sex-specific dominant locus
    • DOI 10.1534/genetics.166.1.483
    • van Dijk, P. J., and Bakx-Schotman, J. M. T. 2004. Formation of unreduced megaspores (diplospoy) in apomictic dandelions (Taraxacum officinale, s.l.) is controlled by a sex-specific dominant locus. Genetics 166:483-492. (Pubitemid 38364733)
    • (2004) Genetics , vol.166 , Issue.1 , pp. 483-492
    • Van Dijk, P.J.1    Bakx-Schotman, J.M.T.2
  • 44
    • 33748941620 scopus 로고    scopus 로고
    • Significance of inducible defense-related proteins in infected plants
    • DOI 10.1146/annurev.phyto.44.070505.143425
    • van Loon, L. C., Rep, M., and Pieterse, C. M. 2006. Significance of inducible defense-related proteins in infected plants. Annu. Rev. Phytopathol. 44:135-162. (Pubitemid 44435701)
    • (2006) Annual Review of Phytopathology , vol.44 , pp. 135-162
    • Van Loon, L.C.1    Rep, M.2    Pieterse, C.M.J.3
  • 45
    • 0000975516 scopus 로고
    • Polyphenol oxidase: The chloroplast oxidase with no established function
    • Vaughn, K. C., Lax, A. R., and Duke, S. O. 1988. Polyphenol oxidase: The chloroplast oxidase with no established function. Phys. Plant 72:659-665.
    • (1988) Phys. Plant , vol.72 , pp. 659-665
    • Vaughn, K.C.1    Lax, A.R.2    Duke, S.O.3
  • 47
    • 0031900371 scopus 로고    scopus 로고
    • Diphenol oxidases, enzyme-catalysed browning and plant disease resistance
    • Walker, J. R. L., and Ferrar, P. H. 1998. Diphenol oxidases, enzyme-catalysed browning and plant disease resistance. Biotechnol. Genet. Eng. Rev. 15:457-498. (Pubitemid 28185152)
    • (1998) Biotechnology and Genetic Engineering Reviews , vol.15 , pp. 457-498
    • Walker, J.R.L.1    Ferrar, P.H.2
  • 48
    • 7044238819 scopus 로고    scopus 로고
    • Polyphenol oxidase overexpression in transgenic Populus enhances resistance to herbivory by forest tent caterpillar (Malacosoma disstria)
    • DOI 10.1007/s00425-004-1327-1
    • Wang, J., and Constabel, C. P. 2004. Polyphenol oxidase overexpression in transgenic Populus enhances resistance to herbivory by forest tent caterpillar (Malacosoma disstria). Planta 220:87-96. (Pubitemid 40033003)
    • (2004) Planta , vol.220 , Issue.1 , pp. 87-96
    • Wang, J.1    Constabel, C.P.2
  • 49
    • 0030152985 scopus 로고    scopus 로고
    • Flavonoids, cinnamic acids and coumarins from the different tissues and medicinal preparations of Taraxacum officinale
    • Williams, C. A., Goldstone, F., Greenham, J. 1996. Flavonoids, cinnamic acids and coumarins from the different tissues and medicinal preparations of Taraxacum officinale. Phytochemisry 42:121-127.
    • (1996) Phytochemisry , vol.42 , pp. 121-127
    • Williams, C.A.1    Goldstone, F.2    Greenham, J.3
  • 50
    • 71549130403 scopus 로고    scopus 로고
    • Cloning, microbial expression and structure-activity relationship of polyphenol oxidases from Camellia sinensis
    • Wu, Y.-L., Pan, L.-P., Yu, S.-L., Li, H.-H. 2010. Cloning, microbial expression and structure-activity relationship of polyphenol oxidases from Camellia sinensis. J. Biotechnol. 145:66-72.
    • (2010) J. Biotechnol. , vol.145 , pp. 66-72
    • Wu, Y.-L.1    Pan, L.-P.2    Yu, S.-L.3    Li, H.-H.4
  • 51
    • 0042415543 scopus 로고    scopus 로고
    • Physicochemical properties and function of plant polyphenol oxidase: A review
    • Yoruk, R., and Marshall, M. R. 2003. Physicochemical properties and function of plant polyphenol oxidase: A review. J. Food Biochem. 27:361-422. (Pubitemid 38034245)
    • (2003) Journal of Food Biochemistry , vol.27 , Issue.5 , pp. 361-422
    • Yoruk, R.1    Marshall, M.R.2


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