메뉴 건너뛰기




Volumn 50, Issue 2, 2002, Pages 283-294

Tobacco-expressed Brassica juncea chitinase BjCHI1 shows antifungal activity in vitro

Author keywords

Aspergillus infection; Caterpillar feeding; Chitin binding domain; Fungal induction; PR protein; Tobacco transformation

Indexed keywords

CATALYSIS; COLORIMETRIC ANALYSIS; DNA; FUNGI; LIQUID CHROMATOGRAPHY;

EID: 0036717162     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1016067200148     Document Type: Article
Times cited : (24)

References (45)
  • 1
    • 0026556040 scopus 로고
    • The primary structure of stinging nettle (Urtica dioica) agglutinin, A two-domain member of the hevein family
    • Beintema, J.J. and Peumans, W.J. 1992. The primary structure of stinging nettle (Urtica dioica) agglutinin, A two-domain member of the hevein family. FEBS Lett. 299: 131-134.
    • (1992) FEBS Lett. , vol.299 , pp. 131-134
    • Beintema, J.J.1    Peumans, W.J.2
  • 2
    • 0002458124 scopus 로고
    • Induction of hydrolases as a defense reaction against pathogens
    • J.L. Key and T. Kosuge (Eds) Alan R. Liss, New York
    • Boller, T. 1985. Induction of hydrolases as a defense reaction against pathogens. In: J.L. Key and T. Kosuge (Eds) Cellular and Molecular Biology of Plant Stress, Alan R. Liss, New York, pp. 247-262.
    • (1985) Cellular and Molecular Biology of Plant Stress , pp. 247-262
    • Boller, T.1
  • 3
    • 0002643289 scopus 로고
    • Biochemical analysis of chitinase and β-1,3-glucanases
    • S.J. Gurr, M.J. Mcpherson and D.J. Bowles (Eds) IRL Press, Oxford
    • Boller, T. 1992. Biochemical analysis of chitinase and β-1,3-glucanases. In: S.J. Gurr, M.J. Mcpherson and D.J. Bowles (Eds) Molecular Plant Pathology: A Practical Approach, vol. II, IRL Press, Oxford, pp. 23-30.
    • (1992) Molecular Plant Pathology: A Practical Approach , vol.2 , pp. 23-30
    • Boller, T.1
  • 4
    • 0002886806 scopus 로고
    • Chitinase in bean leaves: Induction by ethylene, purification, properties, and possible function
    • Boller, T., Gehri, A., Mauch, F. and Vögeli, U. 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    Vögeli, 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
  • 7
    • 0000431179 scopus 로고
    • A chitin-binding lectin from stinging nettle rhizomes with antifungal properties
    • Broekaert, W.F., Van Parijs, J., Leyns, F., Joos, H. and Peumans, W.J. 1989. A chitin-binding lectin from stinging nettle rhizomes with antifungal properties. Science 245: 1100-1102.
    • (1989) Science , vol.245 , pp. 1100-1102
    • Broekaert, W.F.1    Van Parijs, J.2    Leyns, F.3    Joos, H.4    Peumans, W.J.5
  • 8
    • 0031471181 scopus 로고    scopus 로고
    • Primary structure and expression of acidic (class II) chitinase in potato
    • Büchter, R., Strömberg. A., Schmelzer, E. and Kombrink, E. 1997. Primary structure and expression of acidic (class II) chitinase in potato. Plant Mol. Biol. 35: 749-761.
    • (1997) Plant Mol. Biol. , vol.35 , pp. 749-761
    • Büchter, R.1    Strömberg, A.2    Schmelzer, E.3    Kombrink, E.4
  • 9
    • 0025718126 scopus 로고
    • Lectin, lectin genes and their role in plant defense
    • Chrispeels, M.J. and Raikhel, N.V. 1991. Lectin, lectin genes and their role in plant defense. Plant Cell 3: 1-9.
    • (1991) Plant Cell , vol.3 , pp. 1-9
    • Chrispeels, M.J.1    Raikhel, N.V.2
  • 12
    • 0033150357 scopus 로고    scopus 로고
    • Processing, targeting and antifungal activity of stinging nettle agglutinin in transgenic tobacco
    • Does, M.P., Houterman, P.M., Dekker, H.L. and Cornelissen, B.J.C. 1999. Processing, targeting and antifungal activity of stinging nettle agglutinin in transgenic tobacco. Plant Physiol. 120: 421-431.
    • (1999) Plant Physiol. , vol.120 , pp. 421-431
    • Does, M.P.1    Houterman, P.M.2    Dekker, H.L.3    Cornelissen, B.J.C.4
  • 14
    • 0033290243 scopus 로고    scopus 로고
    • Aggressive and defensive roles for chitinases
    • P. Jollès and R.A.A. Muzzarelli (Eds) Birkhäuser, Basel, Switzerland
    • Gooday, G.W. 1999. Aggressive and defensive roles for chitinases. In: P. Jollès and R.A.A. Muzzarelli (Eds) Chitin and Chitinases, Birkhäuser, Basel, Switzerland, pp. 157-170.
    • (1999) Chitin and Chitinases , pp. 157-170
    • Gooday, G.W.1
  • 17
    • 0027666351 scopus 로고
    • The N-terminal cysteine-rich domain of tobacco class I chitinase is essential for chitin binding but not for catalytic or antifungal activity
    • Iseli, B., Boller, T. and Neuhaus, J.-M. 1993. The N-terminal cysteine-rich domain of tobacco class I chitinase is essential for chitin binding but not for catalytic or antifungal activity. Plant Physiol. 103: 221-226.
    • (1993) Plant Physiol. , vol.103 , pp. 221-226
    • Iseli, B.1    Boller, T.2    Neuhaus, J.-M.3
  • 18
    • 0030065364 scopus 로고    scopus 로고
    • Characterization of two class II chitinase genes from peanut and expression studies in transgenic tobacco plants
    • Kellmann, J.W., Kleinow, T., Engelhardt, K., Philipp, C., Wegener, D., Schell, J. and Schreier, P.H. 1996. Characterization of two class II chitinase genes from peanut and expression studies in transgenic tobacco plants. Plant Mol. Biol. 30: 351-358.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 351-358
    • Kellmann, J.W.1    Kleinow, T.2    Engelhardt, K.3    Philipp, C.4    Wegener, D.5    Schell, J.6    Schreier, P.H.7
  • 19
    • 0025261346 scopus 로고
    • Laticifer specific gene expression of Hevea brasiliensis (rubber tree)
    • Kush, A., Goyvaerts, E., Chye, M.-L. and Chua, N.-H. 1990. Laticifer specific gene expression of Hevea brasiliensis (rubber tree). Proc. Natl. Acad. Sci. USA 87: 1787-1790.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1787-1790
    • Kush, A.1    Goyvaerts, E.2    Chye, M.-L.3    Chua, N.-H.4
  • 20
    • 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
  • 21
    • 0026668497 scopus 로고
    • The gene for stinging nettle lectin (Urtica dioica agglutinin) encodes both a lectin and a chitinase
    • Lerner, D.R. and Raikhel, N.V. 1992. The gene for stinging nettle lectin (Urtica dioica agglutinin) encodes both a lectin and a chitinase. J. Biol. Chem. 267: 11085-11091.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11085-11091
    • Lerner, D.R.1    Raikhel, N.V.2
  • 23
  • 24
    • 0029141130 scopus 로고
    • Citrus rootstock responses to herbivory by larvae of the sugarcane rootstock borer weevil (Diaprepes abbreviatus)
    • Mayer, R.T., Shapiro, J.P., Berdis, E., Hearn, C.J., McCollum, T.G., McDonald, R.E. and Doostdar, H. 1995. Citrus rootstock responses to herbivory by larvae of the sugarcane rootstock borer weevil (Diaprepes abbreviatus). Physiol. Plant. 94: 164-173.
    • (1995) Physiol. Plant. , vol.94 , pp. 164-173
    • Mayer, R.T.1    Shapiro, J.P.2    Berdis, E.3    Hearn, C.J.4    McCollum, T.G.5    McDonald, R.E.6    Doostdar, H.7
  • 26
    • 0001868197 scopus 로고
    • Analysis of gene expression in transgenic plants
    • S.B. Gelvin and R.A. Schilperoort (Eds) Kluwer Academic Publishers, Dordrecht, Netherlands
    • Nagy, F., Kay, S.A. and Chua, N.H. 1988. Analysis of gene expression in transgenic plants. In: S.B. Gelvin and R.A. Schilperoort (Eds) Plant Molecular Biology Manual, Kluwer Academic Publishers, Dordrecht, Netherlands, pp. B4: 1-29.
    • (1988) Plant Molecular Biology Manual , vol.B4 , pp. 1-29
    • Nagy, F.1    Kay, S.A.2    Chua, N.H.3
  • 28
    • 0025840612 scopus 로고
    • A short C-terminal sequence is necessary and sufficient for the targeting of chitinase to the plant vacuole
    • Neuhaus, J.M., Sticher, L., Meins, F. and Boller, T. 1991. A short C-terminal sequence is necessary and sufficient for the targeting of chitinase to the plant vacuole. Proc. Natl. Acad. Sci. USA 88: 10362-10366.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10362-10366
    • Neuhaus, J.M.1    Sticher, L.2    Meins, F.3    Boller, T.4
  • 29
    • 0029379651 scopus 로고
    • Lectins as plant defense proteins
    • Peumans, W.J. and Van Damme, E.J.M. 1995. Lectins as plant defense proteins. Plant Physiol. 109: 347-352.
    • (1995) Plant Physiol. , vol.109 , pp. 347-352
    • Peumans, W.J.1    Van Damme, E.J.M.2
  • 30
    • 0026933301 scopus 로고
    • Cloning and characterization of a pathogen-induced chitinase in Brassica napus
    • Rasmussen, U., Bojsen, K. and Collinge, D.B. 1992. Cloning and characterization of a pathogen-induced chitinase in Brassica napus. Plant Mol. Biol. 20: 277-287.
    • (1992) Plant Mol. Biol. , vol.20 , pp. 277-287
    • Rasmussen, U.1    Bojsen, K.2    Collinge, D.B.3
  • 31
    • 0001194009 scopus 로고
    • Plant and bacterial chitinases differ in antifungal activity
    • Roberts, W.K. and Selitrennikoff, C.P. 1988. Plant and bacterial chitinases differ in antifungal activity. J. Gen. Microbiol. 134: 169-176.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 169-176
    • Roberts, W.K.1    Selitrennikoff, C.P.2
  • 32
    • 0000004426 scopus 로고
    • Disease resistance
    • K.S. Labana, S.S. Banga and S.K. Banga (Eds) Springer-Verlag, Berlin
    • Saharan, G.S. 1993. Disease resistance. In: K.S. Labana, S.S. Banga and S.K. Banga (Eds) Breeding Oilseed Brassicas, Springer-Verlag, Berlin, pp. 181-205.
    • (1993) Breeding Oilseed Brassicas , pp. 181-205
    • Saharan, G.S.1
  • 34
    • 0001519173 scopus 로고
    • Plant chitinases are potent inhibitors of fungal growth
    • Schlumbaum, A., Mauch, F., Vögeli, U. and Boller, T. 1986. Plant chitinases are potent inhibitors of fungal growth. Nature 324: 365-367.
    • (1986) Nature , vol.324 , pp. 365-367
    • Schlumbaum, A.1    Mauch, F.2    Vögeli, U.3    Boller, T.4
  • 35
    • 0028925252 scopus 로고
    • Processed products of the hevein precursor in the latex of the rubber free (Hevea brasiliensis)
    • Soedjanaatmadja, U.M.S., Subroto, T. and Beintema, J.J. 1995. Processed products of the hevein precursor in the latex of the rubber free (Hevea brasiliensis). FEBS Lett. 363: 211-213.
    • (1995) FEBS Lett. , vol.363 , pp. 211-213
    • Soedjanaatmadja, U.M.S.1    Subroto, T.2    Beintema, J.J.3
  • 36
    • 0027572807 scopus 로고
    • Posttranslational processing of a new class of hydroxyproline-containing proteins
    • Sticher, L., Hofsteenge, J., Neuhaus, J.-M., Boller, T. and Meins, F. Jr. 1993. Posttranslational processing of a new class of hydroxyproline-containing proteins. Plant Physiol. 101: 1239-1247.
    • (1993) Plant Physiol. , vol.101 , pp. 1239-1247
    • Sticher, L.1    Hofsteenge, J.2    Neuhaus, J.-M.3    Boller, T.4    Meins Jr., F.5
  • 37
    • 0018608845 scopus 로고
    • The effect of beta-glucuronidase and chitinase on the cell wall of Aspergillus niger and Aspergillus fumigatus
    • Thomas K.R., Davis, B. and Mills, I. 1979. The effect of beta-glucuronidase and chitinase on the cell wall of Aspergillus niger and Aspergillus fumigatus. Microbios 25: 111-123.
    • (1979) Microbios , vol.25 , pp. 111-123
    • Thomas, K.R.1    Davis, B.2    Mills, I.3
  • 38
    • 0032430834 scopus 로고    scopus 로고
    • Separate jasmonate-dependent and salicylate-dependent defense-response pathways in Arabidopsis are essential for resistance to distinct microbial pathogens
    • Thomma, B.P.H.J., Eggermont, K., Penninckx, I.A.M.A., Mauch-Mani, B., Vogelsang, R., Cammue, B.P.A. and Broekaert, W.F. 1998. Separate jasmonate-dependent and salicylate-dependent defense-response pathways in Arabidopsis are essential for resistance to distinct microbial pathogens. Proc. Natl. Acad. Sci. USA 95: 15107-15111.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15107-15111
    • Thomma, B.P.H.J.1    Eggermont, K.2    Penninckx, I.A.M.A.3    Mauch-Mani, B.4    Vogelsang, R.5    Cammue, B.P.A.6    Broekaert, W.F.7
  • 39
    • 34249919394 scopus 로고
    • Hevein: An antifungal protein from rubber-tree (Hevea brasiliensis) latex
    • Van Parijs, J., Broekaert, W. F., Goldstein, I. J. and Peumans W. J. 1991. Hevein: an antifungal protein from rubber-tree (Hevea brasiliensis) latex. Planta 183: 258-264.
    • (1991) Planta , vol.183 , pp. 258-264
    • Van Parijs, J.1    Broekaert, W.F.2    Goldstein, I.J.3    Peumans, W.J.4
  • 41
    • 0025604145 scopus 로고
    • Dye-labeled substrates for the assay and detection of chitinase and lysozyme activity
    • Wirth, S. and Wolf, G.A. 1990. Dye-labeled substrates for the assay and detection of chitinase and lysozyme activity. J. Microbiol. Meth. 12: 197-205.
    • (1990) J. Microbiol. Meth. , vol.12 , pp. 197-205
    • Wirth, S.1    Wolf, G.A.2
  • 42
    • 0025721792 scopus 로고
    • Evolution of a family of N-acetylglucosamine-binding proteins containing the disulfide-rich domain of wheat germ agglutinin
    • Wright, H.T., Sandrasegaram, G. and Wright, C.S. 1991. Evolution of a family of N-acetylglucosamine-binding proteins containing the disulfide-rich domain of wheat germ agglutinin. J. Mol. Evol. 33: 283-294.
    • (1991) J. Mol. Evol. , vol.33 , pp. 283-294
    • Wright, H.T.1    Sandrasegaram, G.2    Wright, C.S.3
  • 43
    • 0028484871 scopus 로고
    • Molecular analysis of two cDNA clones encoding acidic class I chitinase in maize
    • Wu, S., Kriz, A.L. and Widholm, J.M. 1994. Molecular analysis of two cDNA clones encoding acidic class I chitinase in maize. Plant Physiol. 105: 1097-1105.
    • (1994) Plant Physiol. , vol.105 , pp. 1097-1105
    • Wu, S.1    Kriz, A.L.2    Widholm, J.M.3
  • 44
    • 0033179935 scopus 로고    scopus 로고
    • Methyl jasmonate induces expression of a novel Brassica juncea chitinase with two chitin-binding domains
    • Zhao, K.J. and Chye, M.L. 1999. Methyl jasmonate induces expression of a novel Brassica juncea chitinase with two chitin-binding domains. Plant Mol. Biol. 40: 1009-1018.
    • (1999) Plant Mol. Biol. , vol.40 , pp. 1009-1018
    • Zhao, K.J.1    Chye, M.L.2
  • 45
    • 0028001451 scopus 로고
    • Enhanced protection against fungal attack by constitutive co-expression of chitinase and glucanase genes in trangenic tobacco
    • Zhu, Q., Maher, E.A., Masoud, S., Dixon, R.A. and Lamb, C.J. 1994. Enhanced protection against fungal attack by constitutive co-expression of chitinase and glucanase genes in trangenic tobacco. Bio/technology 12: 807-812.
    • (1994) Bio/technology , vol.12 , pp. 807-812
    • Zhu, Q.1    Maher, E.A.2    Masoud, S.3    Dixon, R.A.4    Lamb, C.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.