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Volumn 122, Issue 2, 2000, Pages 369-378

Expression and localization of nitrilase during symptom development of the clubroot disease in Arabidopsis

Author keywords

[No Author keywords available]

Indexed keywords

AUXIN; BETA GLUCURONIDASE; CLUBROOT DISEASE; ENZYME ACTIVITY; ENZYME ISOFORM; ENZYME LOCALIZATION; ENZYME SYNTHESIS; GENE OVEREXPRESSION; INOCULATION; MUTANT; NITRILASE; PATHOGENICITY; PHENOTYPE; POLYCLONAL ANTIBODY; SPOROGENESIS; TRANSGENIC PLANT; WILD RELATIVE;

EID: 0034144395     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.122.2.369     Document Type: Article
Times cited : (89)

References (38)
  • 2
    • 0028303120 scopus 로고
    • Differential regulation of an auxin-producing nitrilase gene family in Arabidopsis thaliana
    • Bartel B, Fink GR (1994) Differential regulation of an auxin-producing nitrilase gene family in Arabidopsis thaliana. Proc Natl Acad Sci USA 91: 6649-6653
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6649-6653
    • Bartel, B.1    Fink, G.R.2
  • 3
    • 0026524442 scopus 로고
    • Cloning and expression of an Arabidopsis nitrilase which can convert indole-3-acetonitrile to the plant hormone indole-3-acetic acid
    • Bartling D, Seedorf M, Mithöfer A, Weiler EW (1992) Cloning and expression of an Arabidopsis nitrilase which can convert indole-3-acetonitrile to the plant hormone indole-3-acetic acid. Eur J Biochem 205: 417-424
    • (1992) Eur J Biochem , vol.205 , pp. 417-424
    • Bartling, D.1    Seedorf, M.2    Mithöfer, A.3    Weiler, E.W.4
  • 4
    • 0028362240 scopus 로고
    • Molecular characterization of two cloned nitrilases from Arabidopsis thaliana: Key enzymes in biosynthesis of the plant hormone indole-3-acetic acid
    • Bartling D, Seedorf M, Schmidt RC, Weiler EW (1994) Molecular characterization of two cloned nitrilases from Arabidopsis thaliana: key enzymes in biosynthesis of the plant hormone indole-3-acetic acid. Proc Natl Acad Sci USA 91: 6021-6025
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6021-6025
    • Bartling, D.1    Seedorf, M.2    Schmidt, R.C.3    Weiler, E.W.4
  • 5
    • 0001362426 scopus 로고
    • Improvements in immunostaining samples embedded in methacrylate: Localisation of microtubules and other antigens throughout developing plants of diverse taxa
    • Baskin TI, Busby CH, Fowke LC, Sammut M, Gabler F (1992) Improvements in immunostaining samples embedded in methacrylate: localisation of microtubules and other antigens throughout developing plants of diverse taxa. Planta 187: 405-413
    • (1992) Planta , vol.187 , pp. 405-413
    • Baskin, T.I.1    Busby, C.H.2    Fowke, L.C.3    Sammut, M.4    Gabler, F.5
  • 6
    • 0029202475 scopus 로고
    • Infection with the obligate biotroph Plasmodiophora brassicae, the causal agent of the clubroot disease, does not affect expression of NIT1/2-related nitrilases in roots of Chinese cabbage
    • Bischoff M, Löw R, Grsic S, Rausch T, Hilgenberg W, Ludwig-Müller J (1995) Infection with the obligate biotroph Plasmodiophora brassicae, the causal agent of the clubroot disease, does not affect expression of NIT1/2-related nitrilases in roots of Chinese cabbage. J Plant Physiol 147: 341-345
    • (1995) J Plant Physiol , vol.147 , pp. 341-345
    • Bischoff, M.1    Löw, R.2    Grsic, S.3    Rausch, T.4    Hilgenberg, W.5    Ludwig-Müller, J.6
  • 8
    • 0001319210 scopus 로고
    • The role of indole glucosinolates in the clubroot disease of the Cruciferae
    • Butcher DN, El-Tigani S, Ingram DS (1974) The role of indole glucosinolates in the clubroot disease of the Cruciferae. Physiol Plant Pathol 4: 127-141
    • (1974) Physiol Plant Pathol , vol.4 , pp. 127-141
    • Butcher, D.N.1    El-Tigani, S.2    Ingram, D.S.3
  • 9
    • 84880780932 scopus 로고
    • A rapid and simple procedure for purification of indole-3-acetic acid prior to GC-SIM-MS analysis
    • Chen K-H, Miller AN, Patterson GW, Cohen JD (1988) A rapid and simple procedure for purification of indole-3-acetic acid prior to GC-SIM-MS analysis. Plant Physiol 86: 822-825
    • (1988) Plant Physiol , vol.86 , pp. 822-825
    • Chen, K.-H.1    Miller, A.N.2    Patterson, G.W.3    Cohen, J.D.4
  • 10
    • 0002004249 scopus 로고
    • The occurrence of free and bound cytokinins in plasmodia of Plasmodiophora brassicae isolated from tissue cultures of clubroots
    • Dekhuijzen HM (1981) The occurrence of free and bound cytokinins in plasmodia of Plasmodiophora brassicae isolated from tissue cultures of clubroots. Plant Cell Rep 1: 18-20
    • (1981) Plant Cell Rep , vol.1 , pp. 18-20
    • Dekhuijzen, H.M.1
  • 13
    • 0031787565 scopus 로고    scopus 로고
    • Physiological analysis of transgenic Arabidopsis thaliana plants expressing one nitrilase isoform in sense or antisense direction
    • Grsic S, Sauerteig S, Neuhaus K, Albrecht M, Rossiter J, Ludwig-Müller J (1998) Physiological analysis of transgenic Arabidopsis thaliana plants expressing one nitrilase isoform in sense or antisense direction. J Plant Physiol 153: 446-456
    • (1998) J Plant Physiol , vol.153 , pp. 446-456
    • Grsic, S.1    Sauerteig, S.2    Neuhaus, K.3    Albrecht, M.4    Rossiter, J.5    Ludwig-Müller, J.6
  • 14
    • 84987013734 scopus 로고
    • Localization of newly synthesized indole-3-methylglucosinolate (=glucobrassicin) in vacuoles from horseradish (Armoracia rusticana)
    • Helmlinger J, Rausch T, Hilgenberg W (1983) Localization of newly synthesized indole-3-methylglucosinolate (=glucobrassicin) in vacuoles from horseradish (Armoracia rusticana). Physiol Plant 58: 302-310
    • (1983) Physiol Plant , vol.58 , pp. 302-310
    • Helmlinger, J.1    Rausch, T.2    Hilgenberg, W.3
  • 15
    • 0030191773 scopus 로고    scopus 로고
    • Quantification of free plus conjugated indoleacetic acid in Arabidopsis requires correction for nonenzymatic conversion of indolic nitriles
    • Ilic' N, Normanly J, Cohen JD (1996) Quantification of free plus conjugated indoleacetic acid in Arabidopsis requires correction for nonenzymatic conversion of indolic nitriles. Plant Physiol 111: 781-788
    • (1996) Plant Physiol , vol.111 , pp. 781-788
    • Ilic', N.1    Normanly, J.2    Cohen, J.D.3
  • 16
    • 0000173681 scopus 로고
    • The life history of Plasmodiophora brassicae Woron
    • Ingram DS, Tommerup IC (1972) The life history of Plasmodiophora brassicae Woron. Proc R Soc Lond B 180: 103-112
    • (1972) Proc R Soc Lond B , vol.180 , pp. 103-112
    • Ingram, D.S.1    Tommerup, I.C.2
  • 17
    • 51249176890 scopus 로고
    • Assaying chimeric genes in plants: The GUS gene fusion system
    • Jefferson RA (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
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (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
  • 19
    • 0023654956 scopus 로고
    • Improved method for the isolation of RNA from plant tissues
    • Logemann J, Schell J, Willmitzer L (1987) Improved method for the isolation of RNA from plant tissues. Anal Biochem 163: 16-20
    • (1987) Anal Biochem , vol.163 , pp. 16-20
    • Logemann, J.1    Schell, J.2    Willmitzer, L.3
  • 20
    • 0028248861 scopus 로고
    • Sensitive nonradioactive northern blots using alkaline transfer of total RNA and PCR-amplified biotinylated probes
    • Löw R, Rausch T (1994) Sensitive nonradioactive northern blots using alkaline transfer of total RNA and PCR-amplified biotinylated probes. Biotechniques 17: 1026-1030
    • (1994) Biotechniques , vol.17 , pp. 1026-1030
    • Löw, R.1    Rausch, T.2
  • 21
    • 0344267635 scopus 로고    scopus 로고
    • Plasmodiophora brassicae, the causal agent of clubroot disease: A review on molecular and biochemical events in pathogenesis
    • Ludwig-Müller J (1999) Plasmodiophora brassicae, the causal agent of clubroot disease: a review on molecular and biochemical events in pathogenesis. Z Pflanzenkr Pflanzenschutz 106: 109-127
    • (1999) Z Pflanzenkr Pflanzenschutz , vol.106 , pp. 109-127
    • Ludwig-Müller, J.1
  • 22
    • 0027145242 scopus 로고
    • Concentrations of indole-3-acetic acid in plants of tolerant and susceptible varieties of Chinese cabbage infected with Plasmodiophora brassicae Woron
    • Ludwig-Müller J, Bendel U, Thermann P, Ruppel M, Epstein E, Hilgenberg W (1993) Concentrations of indole-3-acetic acid in plants of tolerant and susceptible varieties of Chinese cabbage infected with Plasmodiophora brassicae Woron. New Phytol 125: 763-769
    • (1993) New Phytol , vol.125 , pp. 763-769
    • Ludwig-Müller, J.1    Bendel, U.2    Thermann, P.3    Ruppel, M.4    Epstein, E.5    Hilgenberg, W.6
  • 23
    • 0030515936 scopus 로고    scopus 로고
    • Auxin-conjugate hydrolysis in Chinese cabbage: Characterization of an amidohydrolase and its role during the clubroot disease
    • Ludwig-Müller J, Epstein E, Hilgenberg W (1996) Auxin-conjugate hydrolysis in Chinese cabbage: characterization of an amidohydrolase and its role during the clubroot disease. Physiol Plant 97: 627-634
    • (1996) Physiol Plant , vol.97 , pp. 627-634
    • Ludwig-Müller, J.1    Epstein, E.2    Hilgenberg, W.3
  • 24
    • 84989674547 scopus 로고
    • A plasma membrane-bound enzyme oxidizes L-tryptophan to indole-3-acetaldoxime
    • Ludwig-Müller J, Hilgenberg W (1988) A plasma membrane-bound enzyme oxidizes L-tryptophan to indole-3-acetaldoxime. Physiol Plant 74: 240-250
    • (1988) Physiol Plant , vol.74 , pp. 240-250
    • Ludwig-Müller, J.1    Hilgenberg, W.2
  • 25
    • 84989674583 scopus 로고
    • Conversion of indole-3-acetaldoxime to indole-3-acetonitrile by plasma membranes from Chinese cabbage
    • Ludwig-Müller J, Hilgenberg W (1990) Conversion of indole-3-acetaldoxime to indole-3-acetonitrile by plasma membranes from Chinese cabbage. Physiol Plant 79: 311-318
    • (1990) Physiol Plant , vol.79 , pp. 311-318
    • Ludwig-Müller, J.1    Hilgenberg, W.2
  • 26
    • 0006058217 scopus 로고
    • Tryptophan oxidizing enzyme and basic peroxidase isoenzymes in Arabidopsis thaliana (L.) Heynh.: Are they identical?
    • Ludwig-Müller J, Hilgenberg W (1992) Tryptophan oxidizing enzyme and basic peroxidase isoenzymes in Arabidopsis thaliana (L.) Heynh.: are they identical? Plant Cell Physiol 33: 1115-1125
    • (1992) Plant Cell Physiol , vol.33 , pp. 1115-1125
    • Ludwig-Müller, J.1    Hilgenberg, W.2
  • 27
    • 0039185568 scopus 로고    scopus 로고
    • Indole glucosinolate and auxin biosynthesis in Arabidopsis thaliana L. glucosinolate mutants and the development of the clubroot disease
    • Ludwig-Müller J, Pieper K, Ruppel M, Cohen JD, Epstein E, Kiddle G, Bennett R (1999) Indole glucosinolate and auxin biosynthesis in Arabidopsis thaliana L. glucosinolate mutants and the development of the clubroot disease. Planta 208: 409-419
    • (1999) Planta , vol.208 , pp. 409-419
    • Ludwig-Müller, J.1    Pieper, K.2    Ruppel, M.3    Cohen, J.D.4    Epstein, E.5    Kiddle, G.6    Bennett, R.7
  • 28
    • 0342871969 scopus 로고    scopus 로고
    • Glucosinolate content in susceptible and tolerant Chinese cabbage varieties during the development of the clubroot disease
    • Ludwig-Müller J, Schubert B, Pieper K, Ihmig S, Hilgenberg W (1997) Glucosinolate content in susceptible and tolerant Chinese cabbage varieties during the development of the clubroot disease. Phytochemistry 44: 407-414
    • (1997) Phytochemistry , vol.44 , pp. 407-414
    • Ludwig-Müller, J.1    Schubert, B.2    Pieper, K.3    Ihmig, S.4    Hilgenberg, W.5
  • 29
    • 0000914718 scopus 로고
    • Isomers of zeatin and zeatin riboside in clubroot tissue: Evidence for trans-zeatin biosynthesis by Plasmodiophora brassicae
    • Müller P, Hilgenberg W (1986) Isomers of zeatin and zeatin riboside in clubroot tissue: evidence for trans-zeatin biosynthesis by Plasmodiophora brassicae. Physiol Plant 66: 245-250
    • (1986) Physiol Plant , vol.66 , pp. 245-250
    • Müller, P.1    Hilgenberg, W.2
  • 30
    • 0019321718 scopus 로고
    • Rapid isolation of high molecular weight plant DNA
    • Murray MG, Thompson WF (1980) Rapid isolation of high molecular weight plant DNA. Nucleic Acids Res 8: 4321-4325
    • (1980) Nucleic Acids Res , vol.8 , pp. 4321-4325
    • Murray, M.G.1    Thompson, W.F.2
  • 31
    • 0027431896 scopus 로고
    • Arabidopsis thaliana auxotrophs reveal a tryptophan-independent biosynthetic pathway for indole-3-acetic acid
    • Normanly J, Cohen JD, Fink GR (1993) Arabidopsis thaliana auxotrophs reveal a tryptophan-independent biosynthetic pathway for indole-3-acetic acid. Proc Natl Acad Sci USA 90: 10355-10374
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10355-10374
    • Normanly, J.1    Cohen, J.D.2    Fink, G.R.3
  • 32
    • 0031252198 scopus 로고    scopus 로고
    • Arabidopsis mutants resistant to the auxin effects of indole-3-acetonitrile are defective in the nitrilase encoded by the NIT1 gene
    • Normanly J, Grisafi P, Fink GR, Bartel B (1997) Arabidopsis mutants resistant to the auxin effects of indole-3-acetonitrile are defective in the nitrilase encoded by the NIT1 gene. Plant Cell 9: 1781-1790
    • (1997) Plant Cell , vol.9 , pp. 1781-1790
    • Normanly, J.1    Grisafi, P.2    Fink, G.R.3    Bartel, B.4
  • 33
    • 0029108316 scopus 로고
    • Rethinking auxin biosynthesis and metabolism
    • Normanly J, Slovin JP, Cohen JD (1995) Rethinking auxin biosynthesis and metabolism. Plant Physiol 107: 323-329
    • (1995) Plant Physiol , vol.107 , pp. 323-329
    • Normanly, J.1    Slovin, J.P.2    Cohen, J.D.3
  • 34
    • 0005564476 scopus 로고
    • Nitrilase activity in clubroot diseased plants
    • Rausch T, Butcher DN, Hilgenberg W (1981) Nitrilase activity in clubroot diseased plants. Physiol Plant 52: 467-470
    • (1981) Physiol Plant , vol.52 , pp. 467-470
    • Rausch, T.1    Butcher, D.N.2    Hilgenberg, W.3
  • 35
    • 84986979972 scopus 로고
    • Indole-3-methylglucosinolate biosynthesis and metabolism in clubroot diseased plants
    • Rausch T, Butcher DN, Hilgenberg W (1983) Indole-3-methylglucosinolate biosynthesis and metabolism in clubroot diseased plants. Physiol Plant 58: 93-100
    • (1983) Physiol Plant , vol.58 , pp. 93-100
    • Rausch, T.1    Butcher, D.N.2    Hilgenberg, W.3
  • 36
    • 0000067054 scopus 로고
    • The conversion of 3-indolemethylglucosinolate to 3-indoleacetonitrile by myrosinase and its relevance to the clubroot disease of the Cruciferae
    • Searle LM, Chamberlain K, Rausch T, Butcher DN (1982) The conversion of 3-indolemethylglucosinolate to 3-indoleacetonitrile by myrosinase and its relevance to the clubroot disease of the Cruciferae. J Exp Bot 33: 935-942
    • (1982) J Exp Bot , vol.33 , pp. 935-942
    • Searle, L.M.1    Chamberlain, K.2    Rausch, T.3    Butcher, D.N.4
  • 37
    • 0025169698 scopus 로고
    • Multiple coordinate controls contribute to a balanced expression of ribulose-1,5-bisphosphate carboxylase/oxygenase subunits in rye leaves
    • Winter U, Feierabend J (1990) Multiple coordinate controls contribute to a balanced expression of ribulose-1,5-bisphosphate carboxylase/oxygenase subunits in rye leaves. Eur J Biochem 187: 445-453
    • (1990) Eur J Biochem , vol.187 , pp. 445-453
    • Winter, U.1    Feierabend, J.2
  • 38
    • 0030575183 scopus 로고    scopus 로고
    • The 32 kDa tonoplast polypeptide D, associated with the V-type H+-ATPase of Mesembryanthemum crystallinum L. in the CAM state: A proteolytically processed subunit B?
    • Zhigang A, Löw R, Rausch T, Lüttge U, Ratajczak R (1996) The 32 kDa tonoplast polypeptide D, associated with the V-type H+-ATPase of Mesembryanthemum crystallinum L. in the CAM state: a proteolytically processed subunit B? FEBS Lett 389: 314-318
    • (1996) FEBS Lett , vol.389 , pp. 314-318
    • Zhigang, A.1    Löw, R.2    Rausch, T.3    Lüttge, U.4    Ratajczak, R.5


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