메뉴 건너뛰기




Volumn 59, Issue 12, 2008, Pages 3475-3484

Brassica juncea chitinase BjCHI1 inhibits growth of fungal phytopathogens and agglutinates Gram-negative bacteria

Author keywords

Bacterial agglutination; Chitin binding domain; Chloroplast transformation; Indian mustard; Lectin; Phytopathogens; Pichia expressed proteins; Transplastomic tobacco

Indexed keywords

CHITINASE; RECOMBINANT PROTEIN; VEGETABLE PROTEIN;

EID: 51749086433     PISSN: 00220957     EISSN: 14602431     Source Type: Journal    
DOI: 10.1093/jxb/ern197     Document Type: Article
Times cited : (33)

References (36)
  • 1
    • 0027969049 scopus 로고
    • Structural features of plant chitinases and chitin-binding proteins
    • Beintema JJ. 1994. Structural features of plant chitinases and chitin-binding proteins. FEBS Letters 350, 159-163.
    • (1994) FEBS Letters , vol.350 , pp. 159-163
    • Beintema, J.J.1
  • 2
    • 0026556040 scopus 로고
    • The primary structure of stinging nettle (Urtica dioica) agglutinin, A two-domain member of the hevein family
    • Beintema JJ, Peumans WJ. 1992. The primary structure of stinging nettle (Urtica dioica) agglutinin, A two-domain member of the hevein family. FEBS Letters 299, 131-134.
    • (1992) FEBS Letters , vol.299 , pp. 131-134
    • Beintema, J.J.1    Peumans, W.J.2
  • 3
    • 0002458124 scopus 로고
    • Induction of hydrolases as a defence reaction against pathogens
    • Key JL, Kosuge T, eds, New York: Alan R Liss
    • Boller T. 1985. Induction of hydrolases as a defence reaction against pathogens. In: Key JL, Kosuge T, eds. Cellular and molecular biology of plant stress. New York: Alan R Liss, 247-262.
    • (1985) Cellular and molecular biology of plant stress , pp. 247-262
    • Boller, T.1
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72, 248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0031528585 scopus 로고    scopus 로고
    • Cross-linking activities of galectins and other multivalent lectins
    • Brewer CF. 1997. Cross-linking activities of galectins and other multivalent lectins. Trends in Glycoscience and Glycotechnology 9, 155-165.
    • (1997) Trends in Glycoscience and Glycotechnology , vol.9 , pp. 155-165
    • Brewer, C.F.1
  • 6
    • 0000431179 scopus 로고
    • A chitin-binding lectin from stinging nettle rhizomes with antifungal properties
    • Broekaert WF, Van Parijs J, Leyns F, Joos H, Peumans WJ. 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
  • 7
    • 15444365716 scopus 로고    scopus 로고
    • Expression of an agglutinating chitinase BjCHI1 with two chitin-binding domains is R. solani-inducible and confers fungal protection in transgenic potato
    • Chye ML, Zhao KJ, He ZM, Ramalingam S, Fung KL. 2005. Expression of an agglutinating chitinase BjCHI1 with two chitin-binding domains is R. solani-inducible and confers fungal protection in transgenic potato. Planta 220, 717-730.
    • (2005) Planta , vol.220 , pp. 717-730
    • Chye, M.L.1    Zhao, K.J.2    He, Z.M.3    Ramalingam, S.4    Fung, K.L.5
  • 11
    • 0036717162 scopus 로고    scopus 로고
    • Tobacco-expressed Brassica juncea chitinase BjCHI1 shows antifungal activity in vitro
    • Fung KL, Zhao KJ, He ZM, Chye ML. 2002. Tobacco-expressed Brassica juncea chitinase BjCHI1 shows antifungal activity in vitro. Plant Molecular Biology 50, 283-294.
    • (2002) Plant Molecular Biology , vol.50 , pp. 283-294
    • Fung, K.L.1    Zhao, K.J.2    He, Z.M.3    Chye, M.L.4
  • 12
    • 19444380294 scopus 로고    scopus 로고
    • Engineering plants with increaseddisease resistance: How are we going to express it?
    • Gurr SJ, Rushton PJ. 2005. Engineering plants with increaseddisease resistance: how are we going to express it? Trends in Biotechnology 23, 283-290.
    • (2005) Trends in Biotechnology , vol.23 , pp. 283-290
    • Gurr, S.J.1    Rushton, P.J.2
  • 13
    • 0025178843 scopus 로고
    • Investigation of endotoxin binding cationic proteins from granulocytes: Agglutination of erythrocytes sensitized with Re-LPS
    • Hirata M, Yoshida M, Inada K, Kirikae T. 1990. Investigation of endotoxin binding cationic proteins from granulocytes: agglutination of erythrocytes sensitized with Re-LPS. Advances in Experimental Medicine and Biology 256, 287-299.
    • (1990) Advances in Experimental Medicine and Biology , vol.256 , pp. 287-299
    • Hirata, M.1    Yoshida, M.2    Inada, K.3    Kirikae, T.4
  • 15
    • 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
  • 16
    • 0026668497 scopus 로고
    • The gene for stinging nettle lectin (Urtica dioica agglutinin) encodes both a lectin and a chitinase
    • Lerner DR, Raikhel NV. 1992. The gene for stinging nettle lectin (Urtica dioica agglutinin) encodes both a lectin and a chitinase. Journal of Biological Chemistry 267, 11085-11091.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 11085-11091
    • Lerner, D.R.1    Raikhel, N.V.2
  • 18
    • 1542368230 scopus 로고    scopus 로고
    • Plastid transformation in higher plants
    • Maliga P. 2004. Plastid transformation in higher plants. Annual Review of Plant Biology 55, 289-313.
    • (2004) Annual Review of Plant Biology , vol.55 , pp. 289-313
    • Maliga, P.1
  • 20
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco tissue cultures
    • Murashige T, Skoog F. 1962. A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiologia Plantarum 15, 473-497.
    • (1962) Physiologia Plantarum , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 21
    • 0001868197 scopus 로고
    • Analysis of gene expression in transgenic plants
    • Gelvin SB, Schilperoot RA, eds, Dordrecht: Kluwer Academic Publishers
    • Nagy F, Kay SA, Chua NH. 1988. Analysis of gene expression in transgenic plants. In: Gelvin SB, Schilperoot RA, eds. Plant molecular biology manual, B4. Dordrecht: Kluwer Academic Publishers, 1-29.
    • (1988) Plant molecular biology manual, B4 , pp. 1-29
    • Nagy, F.1    Kay, S.A.2    Chua, N.H.3
  • 23
    • 0036384632 scopus 로고    scopus 로고
    • Analysis of chloroplast transformed tobacco plants with cry1Ia5 under rice psbA transcriptional elements reveal high level expression of Bt toxin without imposing yield penalty and stable inheritance of transplastome
    • Reddy VS, Leelavathi S, Selvapandiyan A, Raman R, Giovanni F, Shukla V, Bhatnagar RK. 2002. Analysis of chloroplast transformed tobacco plants with cry1Ia5 under rice psbA transcriptional elements reveal high level expression of Bt toxin without imposing yield penalty and stable inheritance of transplastome. Molecular Breeding 9, 259-269.
    • (2002) Molecular Breeding , vol.9 , pp. 259-269
    • Reddy, V.S.1    Leelavathi, S.2    Selvapandiyan, A.3    Raman, R.4    Giovanni, F.5    Shukla, V.6    Bhatnagar, R.K.7
  • 26
    • 0001519173 scopus 로고
    • Plant chitinases are potent inhibitor of fungal growth
    • Schlumbaum A, Mauch F, Vögeli U, Boller T. 1986. Plant chitinases are potent inhibitor 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
  • 27
    • 0027398358 scopus 로고
    • High-frequency plastid transformation in tobacco by selection for a chimeric aadA gene
    • Svab Z, Maliga P. 1993. High-frequency plastid transformation in tobacco by selection for a chimeric aadA gene. Proceedings of the National Academy of Sciences, USA 90, 913-917.
    • (1993) Proceedings of the National Academy of Sciences, USA , vol.90 , pp. 913-917
    • Svab, Z.1    Maliga, P.2
  • 29
  • 32
    • 34249919394 scopus 로고
    • Hevein: An antifungal protein from rubber-tree (Hevea brasiliensis) latex
    • Van Parijs J, Broekaert WF, Goldstein IJ, Peumans WJ. 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
  • 33
    • 0025604145 scopus 로고
    • Dye-labelled substrates for the assay and detection of chitinase and lysozyme activity
    • Wirth SJ, Wolf GA. 1990. Dye-labelled substrates for the assay and detection of chitinase and lysozyme activity. Journal of Microbiological Methods 12, 197-205.
    • (1990) Journal of Microbiological Methods , vol.12 , pp. 197-205
    • Wirth, S.J.1    Wolf, G.A.2
  • 34
    • 0025721792 scopus 로고
    • Evolution of a family of N-acetylglucosamine binding proteins containing the disulfide-rich domain of wheat germ agglutinin
    • Wright HT, Sandrasegaram G, Wright CS. 1991. Evolution of a family of N-acetylglucosamine binding proteins containing the disulfide-rich domain of wheat germ agglutinin. Journal of Molecular Evolution 33, 283-294.
    • (1991) Journal of Molecular Evolution , vol.33 , pp. 283-294
    • Wright, H.T.1    Sandrasegaram, G.2    Wright, C.S.3
  • 35
    • 0033179935 scopus 로고    scopus 로고
    • Methyl jasmonate induces expression of a novel Brassica juncea chitinase with two chitin-binding domains
    • Zhao KJ, Chye ML. 1999. Methyl jasmonate induces expression of a novel Brassica juncea chitinase with two chitin-binding domains. Plant Molecular Biology 40, 1009-1018.
    • (1999) Plant Molecular Biology , vol.40 , pp. 1009-1018
    • Zhao, K.J.1    Chye, M.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.