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Volumn 144, Issue 2, 1996, Pages 79-87

Differential induction and accumulation of β-1,3-glucanase and chitinase isoforms in the intercellular space and leaf tissues of pepper by Xanthomonas campestris pv. vesicatoria infection

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EID: 0002027662     PISSN: 09311785     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1439-0434.1996.tb01493.x     Document Type: Article
Times cited : (33)

References (34)
  • 1
    • 38249025994 scopus 로고
    • Biological function of bean pathogenesis-related (PR 3 and PR 4) proteins
    • Awade, A., M. De Tapia, L. Didierjean, G. Bukard (1989): Biological function of bean pathogenesis-related (PR 3 and PR 4) proteins. Plant Sci. 63, 121-130.
    • (1989) Plant Sci. , vol.63 , pp. 121-130
    • Awade, A.1    De Tapia, M.2    Didierjean, L.3    Bukard, G.4
  • 2
    • 0002458124 scopus 로고
    • Induction of hydrolases as a defence reaction against pathogens
    • Key, J. L. and T. Kosuge, (ed.), Alan R. Liss, New York
    • Bollet, T. (1985): Induction of hydrolases as a defence reaction against pathogens In: Key, J. L. and T. Kosuge, (ed.), Cellular and Molecular Biology of Plant Stress, pp. 247-262. Alan R. Liss, New York
    • (1985) Cellular and Molecular Biology of Plant Stress , pp. 247-262
    • Bollet, T.1
  • 3
    • 0000841902 scopus 로고
    • Extracellular localization of chitinase in cucumber
    • Boller, T., J. P. Métraux (1988). Extracellular localization of chitinase in cucumber. Physiol. Mol. Plant Pathol. 33, 11-16.
    • (1988) Physiol. Mol. Plant Pathol. , vol.33 , pp. 11-16
    • Boller, T.1    Métraux, J.P.2
  • 4
    • 0002886806 scopus 로고
    • Chitinase in bean leaves: Induction by ethylene, purification, properties, and possible function
    • Boller, T., A. Gehri, F. Mauch, U. Vògeli (1983): Chitinase in bean leaves: induction by ethylene, purification, properties, and possible function. Planta 157, 22-31.
    • (1983) Planta , vol.157 , pp. 22-31
    • Boller, T.1    Gehri, A.2    Mauch, F.3    Vògeli, U.4
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976): A rapid and sensitive method for the quantitation 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
  • 6
    • 0025718335 scopus 로고
    • Induction of Arabilopsis defence genes by virulent and avirulent Pseudomonas syringae strains and by a cloned avirulence gene
    • Dong, X., M. Mindrinos, K. R. Davis, F. M. Ausubel (1991): Induction of Arabilopsis defence genes by virulent and avirulent Pseudomonas syringae strains and by a cloned avirulence gene. Plant Cell 3, 61-72.
    • (1991) Plant Cell , vol.3 , pp. 61-72
    • Dong, X.1    Mindrinos, M.2    Davis, K.R.3    Ausubel, F.M.4
  • 7
    • 0000781834 scopus 로고
    • Analysis of the synthesis of several pathogenesis-related proteins in tobacco leaves infiltrated with water and with compatible and incompatible isolates of Pseudomonas solanacearum
    • Godiard, L., F. Ragueh, D. Froissard, J. J. Lequay, J. Grosset, Y. Chartier, Y. Meyer, Y. Marco (1990): Analysis of the synthesis of several pathogenesis-related proteins in tobacco leaves infiltrated with water and with compatible and incompatible isolates of Pseudomonas solanacearum. Mol. Plant-Microbe Interact. 3, 207-213.
    • (1990) Mol. Plant-Microbe Interact. , vol.3 , pp. 207-213
    • Godiard, L.1    Ragueh, F.2    Froissard, D.3    Lequay, J.J.4    Grosset, J.5    Chartier, Y.6    Meyer, Y.7    Marco, Y.8
  • 8
    • 0002929277 scopus 로고
    • Suppression of bean defence response by Pseudomonas syringae
    • Jokobek, J L., J. A. Smith, P. B. Lindgren (1993): Suppression of bean defence response by Pseudomonas syringae. Plant Cell 5, 57-63
    • (1993) Plant Cell , vol.5 , pp. 57-63
    • Jokobek, J.L.1    Smith, J.A.2    Lindgren, P.B.3
  • 9
    • 0001756299 scopus 로고
    • β-1.3-glucanase from soybean releases elicitor-active carbohydrates from fungus cell wall
    • Keen, N. T., M. Yoshikawa (1983): β-1.3-glucanase from soybean releases elicitor-active carbohydrates from fungus cell wall. Plant Physiol. 71, 460-465.
    • (1983) Plant Physiol. , vol.71 , pp. 460-465
    • Keen, N.T.1    Yoshikawa, M.2
  • 10
    • 0028103132 scopus 로고
    • Differential accumulation of β-1,3-glucanase and chitinase isoforms in pepper stems infected by compatible and incompatible isolates of Phytophthora capsici
    • Kim, Y. J., B. K Hwang (1994): Differential accumulation of β-1,3-glucanase and chitinase isoforms in pepper stems infected by compatible and incompatible isolates of Phytophthora capsici. Physiol. Molec. Plant Pathol. 45, 195-209.
    • (1994) Physiol. Molec. Plant Pathol. , vol.45 , pp. 195-209
    • Kim, Y.J.1    Hwang, B.K.2
  • 11
    • 0008076904 scopus 로고
    • Changes in protein patterns resulting from infection of rice leaves with Xanthomontas oryzae pv. orvzae
    • Kim, S. G., J. Y. Yoo (1992): Changes in protein patterns resulting from infection of rice leaves with Xanthomontas oryzae pv. orvzae. Mol. Plant-Microbe Interact. 5, 356-360.
    • (1992) Mol. Plant-Microbe Interact. , vol.5 , pp. 356-360
    • Kim, S.G.1    Yoo, J.Y.2
  • 12
    • 0003212693 scopus 로고
    • Method of obtaining fluid from the intercellular space of foliage and the fluid's merit as substrate for phytobacterial pathogens
    • Klement, Z. (1965): Method of obtaining fluid from the intercellular space of foliage and the fluid's merit as substrate for phytobacterial pathogens. Phytopathology 55, 1033-1034.
    • (1965) Phytopathology , vol.55 , pp. 1033-1034
    • Klement, Z.1
  • 13
    • 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
  • 14
    • 0007868166 scopus 로고
    • Relation of plant age to bacterial multiplication in pepper and tomato leaves inoculated with Xanthomonas campestris pv. vesicatoria
    • Lee, J. T , B. K. Hwang (1994): Relation of plant age to bacterial multiplication in pepper and tomato leaves inoculated with Xanthomonas campestris pv. vesicatoria. Korean J. Plant Pathol. 10, 18-24.
    • (1994) Korean J. Plant Pathol. , vol.10 , pp. 18-24
    • Lee, J.T.1    Hwang, B.K.2
  • 15
    • 0000598412 scopus 로고
    • Bacterial multiplications and electrophoretic patterns of soluble proteins in compatible and incompatible interactions of pepper leaves with Xanthomonas campestris pv. vesicatoria
    • Lee, Y. K., Y. J. Kim, B. K. Hwang (1994): Bacterial multiplications and electrophoretic patterns of soluble proteins in compatible and incompatible interactions of pepper leaves with Xanthomonas campestris pv. vesicatoria. Korean J. Plant Pathol. 10, 305-313.
    • (1994) Korean J. Plant Pathol. , vol.10 , pp. 305-313
    • Lee, Y.K.1    Kim, Y.J.2    Hwang, B.K.3
  • 16
    • 0014736229 scopus 로고
    • Polyacrylamide disc electrophoresis of the soluble leaf proteins from Nicotiana tabacum var. 'Samsun' and 'Samsun NN' II. Changes in protein constitution after infection with tobacco mosaic virus
    • van Loon L. C., A. van Kammen (1970): Polyacrylamide disc electrophoresis of the soluble leaf proteins from Nicotiana tabacum var. 'Samsun' and 'Samsun NN' II. Changes in protein constitution after infection with tobacco mosaic virus. Virology 40, 199-211.
    • (1970) Virology , vol.40 , pp. 199-211
    • Van Loon, L.C.1    Van Kammen, A.2
  • 17
    • 0343930469 scopus 로고
    • Identification of several pathogenesis-related protens in tomato leaves inoculated with Cladosporium fulvum (syn. Fulvia fulva) as β-1,3-glucanases and chitinases
    • Matthieu, H. A., J Joosten, J. G. M. De Wit (1989): Identification of several pathogenesis-related protens in tomato leaves inoculated with Cladosporium fulvum (syn. Fulvia fulva) as β-1,3-glucanases and chitinases. Plant Physiol. 88, 936-942.
    • (1989) Plant Physiol. , vol.88 , pp. 936-942
    • Matthieu, H.A.1    Joosten, J.2    De Wit, J.G.M.3
  • 18
    • 0001008022 scopus 로고
    • Functional implication of the sub-cellular localization of ethylene-induced chitinase and β-1,3-glucanase in bean leaves
    • Mauch, F., L. A. Staehelin (1989). Functional implication of the sub-cellular localization of ethylene-induced chitinase and β-1,3-glucanase in bean leaves. Plant Cell 1, 447-457.
    • (1989) Plant Cell , vol.1 , pp. 447-457
    • Mauch, F.1    Staehelin, L.A.2
  • 19
    • 0001324867 scopus 로고
    • Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combinations of chitinase and β-1,3-glucanase
    • Mauch, F., B., Mauch-Mani, T. Boller (1988): Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combinations of chitinase and β-1,3-glucanase. Plant Physiol. 88, 936-942
    • (1988) Plant Physiol. , vol.88 , pp. 936-942
    • Mauch, F.1    Mauch-Mani, B.2    Boller, T.3
  • 20
    • 0001042436 scopus 로고
    • Tween media for semi-selective isolation of Xanthomonas campestris pv. vesicatoria from soil and plant material
    • McGuire, R. G., J. B. Jones, M. Sasser (1986): Tween media for semi-selective isolation of Xanthomonas campestris pv. vesicatoria from soil and plant material. Plant Dis 70, 887-891.
    • (1986) Plant Dis , vol.70 , pp. 887-891
    • McGuire, R.G.1    Jones, J.B.2    Sasser, M.3
  • 22
    • 0017610344 scopus 로고
    • A rapid and sensitive assay for chitinase using tritiated chitin
    • Molano, J . A. Duran, E. Cabib (1977): A rapid and sensitive assay for chitinase using tritiated chitin Anal. Biochem. 83, 648-656.
    • (1977) Anal. Biochem. , vol.83 , pp. 648-656
    • Molano, J.1    Duran, A.2    Cabib, E.3
  • 23
    • 0000674033 scopus 로고
    • A photometric adaptation of the Somogyi method for the determination of glucose
    • Nelson, N. (1944): A photometric adaptation of the Somogyi method for the determination of glucose. J. Biol. Chem. 153, 375-380.
    • (1944) J. Biol. Chem. , vol.153 , pp. 375-380
    • Nelson, N.1
  • 24
    • 0028139605 scopus 로고
    • Comparison of bacterial growth and activity of glucanase and chitinase in pepper leaf and flower tissue infected with Xanthomonas campestris pv. vesicatoria
    • O'Garro, L. W., E. Charlemange (1994): Comparison of bacterial growth and activity of glucanase and chitinase in pepper leaf and flower tissue infected with Xanthomonas campestris pv. vesicatoria. Physiol Molec. Plant Pathol. 45, 181-188.
    • (1994) Physiol Molec. Plant Pathol. , vol.45 , pp. 181-188
    • O'Garro, L.W.1    Charlemange, E.2
  • 25
    • 0024746614 scopus 로고
    • Direct detection of β-1,3-glucanase isozymes on polyacrylamide electrophoresis and isoelectrofocusing
    • Pan, S. Q., X. E. Ye, J. Kuć (1989): Direct detection of β-1,3-glucanase isozymes on polyacrylamide electrophoresis and isoelectrofocusing. Anal. Biochem. 182, 136-140.
    • (1989) Anal. Biochem. , vol.182 , pp. 136-140
    • Pan, S.Q.1    Ye, X.E.2    Kuć, J.3
  • 26
    • 0000859095 scopus 로고
    • A technique for detection of chitinase. β-1,3-glucanase, and protein patterns after a single separation using polyacrylamide gel electrophoresis or isoelectrofocusing
    • Pan, S. Q., X. E. Ye. J. Kuć (1991): A technique for detection of chitinase. β-1,3-glucanase, and protein patterns after a single separation using polyacrylamide gel electrophoresis or isoelectrofocusing. Phytopathology 81, 970-974.
    • (1991) Phytopathology , vol.81 , pp. 970-974
    • Pan, S.Q.1    Ye, X.E.2    Kuć, J.3
  • 27
    • 21344497174 scopus 로고
    • Plant chitinases and their roles in resistance to fungal diseases
    • Punja, Z. K., Y. Y. Zhang (1993): Plant chitinases and their roles in resistance to fungal diseases. J. Nematology 25, 526-540.
    • (1993) J. Nematology , vol.25 , pp. 526-540
    • Punja, Z.K.1    Zhang, Y.Y.2
  • 28
    • 36949089946 scopus 로고
    • Disk electrophoresis of basic proteins and peptides on polyacrylamide gels
    • Reisfield, R. A., U. J. Lewis, D. E. Williams (1962). Disk electrophoresis of basic proteins and peptides on polyacrylamide gels. Nature 195, 281-283.
    • (1962) Nature , vol.195 , pp. 281-283
    • Reisfield, R.A.1    Lewis, U.J.2    Williams, D.E.3
  • 29
    • 77049251255 scopus 로고
    • A modified colorimetric method for the estimation of N-acetylamino sugars
    • Reissig J. L., J. L. Strominger, L. F. Leloir (1955): A modified colorimetric method for the estimation of N-acetylamino sugars. J. Biol. Chem. 217, 959-967.
    • (1955) J. Biol. Chem. , vol.217 , pp. 959-967
    • Reissig, J.L.1    Strominger, J.L.2    Leloir, L.F.3
  • 30
    • 84986948445 scopus 로고
    • Changes in gene activity during expression of the hypersensitive response in Phaseolus vulgaris cv. Red Mexican to an avirulent race 1 isolate of Pseudomonas syringae pv phaseolicola
    • Slusarenko, A. J., A. Longland (1986). Changes in gene activity during expression of the hypersensitive response in Phaseolus vulgaris cv. Red Mexican to an avirulent race 1 isolate of Pseudomonas syringae pv phaseolicola. Physiol. Mol. Plant Path. 29, 79-94.
    • (1986) Physiol. Mol. Plant Path. , vol.29 , pp. 79-94
    • Slusarenko, A.J.1    Longland, A.2
  • 31
    • 2842546199 scopus 로고
    • Multiplication of Xanthomonas campestris pv. vesicatoria and lesion development in resistant and susceptible pepper
    • Stall, R. E., A. A. Cook (1966): Multiplication of Xanthomonas campestris pv. vesicatoria and lesion development in resistant and susceptible pepper. Phytopathology 56, 1152-1154.
    • (1966) Phytopathology , vol.56 , pp. 1152-1154
    • Stall, R.E.1    Cook, A.A.2
  • 32
    • 2842601705 scopus 로고
    • Inhibition of Xanthomonas vesicatoria in extracts from hypersensitive and susceptible pepper leaves
    • Stall, R. E., A A. Cook (1968): Inhibition of Xanthomonas vesicatoria in extracts from hypersensitive and susceptible pepper leaves. Phytopathology 58, 1584-1587.
    • (1968) Phytopathology , vol.58 , pp. 1584-1587
    • Stall, R.E.1    Cook, A.A.2
  • 33
    • 0000715993 scopus 로고
    • Induction of hydrolytic enzymes in Brassica campestris in response to pathovars of Xanthomonas campestris
    • Strauch, J. C., J. M. Dow, D. E. Miligan, R. Parra, M. J. Daniels (1990): Induction of hydrolytic enzymes in Brassica campestris in response to pathovars of Xanthomonas campestris. Plant Physiol. 93, 238-243.
    • (1990) Plant Physiol. , vol.93 , pp. 238-243
    • Strauch, J.C.1    Dow, J.M.2    Miligan, D.E.3    Parra, R.4    Daniels, M.J.5
  • 34
    • 0002892696 scopus 로고
    • β-Glucan and β-glucan hydrolase in plant pathogenesis with special reference to wilt-inducing toxins from Phytophthora species
    • Sandford P. (ed.), Fungal Polysaccharide American Chemical Society, Washington
    • Woodward, J. R., P. J. Keane, B. A. Stone (1980): β-Glucan and β-glucan hydrolase in plant pathogenesis with special reference to wilt-inducing toxins from Phytophthora species. In: Sandford P. (ed.), Fungal Polysaccharide. pp. 113-141 ACS Symposium Series 126. American Chemical Society, Washington.
    • (1980) Symposium Series 126
    • Woodward, J.R.1    Keane, P.J.2    Stone, B.A.3


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