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Volumn 50, Issue 25, 2002, Pages 7258-7263

A novel defensin encoded by a mungbean cDNA exhibits insecticidal activity against bruchid

Author keywords

Bruchid resistance; Defensin; In vitro translation; Mungbean

Indexed keywords

COMPLEMENTARY DNA; CYSTEINE; DEFENSIN; DEFENSIN PROTEINS, PLANT; HYBRID PROTEIN; INSECTICIDE; SIGNAL PEPTIDE; VEGETABLE PROTEIN;

EID: 0037021614     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf020527q     Document Type: Article
Times cited : (92)

References (40)
  • 1
    • 0001163253 scopus 로고
    • Insecticidal activity and lectin homology of arcelin seed protein
    • Osborn, T. C.; Alexander, D. C.; Sun, S. S. M.; Cardona, C.; Bliss, F. A. Insecticidal activity and lectin homology of arcelin seed protein. Science 1988, 240, 207-210.
    • (1988) Science , vol.240 , pp. 207-210
    • Osborn, T.C.1    Alexander, D.C.2    Sun, S.S.M.3    Cardona, C.4    Bliss, F.A.5
  • 3
    • 0344762026 scopus 로고    scopus 로고
    • Molecular characterization of a bean α-amylase inhibitor that inhibits the α-amylase of the Mexican bean weevil Zabrotes subfasciatus
    • Grossi-de-Sa, M. F.; Mirkov, T. E.; Ishimoto, M.; Colucci, G.; Bateman, K. S.; Chrispeels, M. J. Molecular characterization of a bean α-amylase inhibitor that inhibits the α-amylase of the Mexican bean weevil Zabrotes subfasciatus. Planta 1997, 203, 295-303.
    • (1997) Planta , vol.203 , pp. 295-303
    • Grossi-de-Sa, M.F.1    Mirkov, T.E.2    Ishimoto, M.3    Colucci, G.4    Bateman, K.S.5    Chrispeels, M.J.6
  • 4
    • 0029245095 scopus 로고
    • Purification and properties of storage proteins (vicilins) from cowpea (Vigna unguiculata) seeds which are susceptible or resistant to the bruchid beetle Callosobruchus maculatus
    • Macedo, M. L. R.; Fernandes, K. V. S.; Sales, M. P.; Xavier-Filho, J. Purification and properties of storage proteins (vicilins) from cowpea (Vigna unguiculata) seeds which are susceptible or resistant to the bruchid beetle Callosobruchus maculatus. Braz. J. Med. Biol. Res. 1995, 28, 183-190.
    • (1995) Braz. J. Med. Biol. Res. , vol.28 , pp. 183-190
    • Macedo, M.L.R.1    Fernandes, K.V.S.2    Sales, M.P.3    Xavier-Filho, J.4
  • 5
    • 0000180578 scopus 로고
    • Protease inhibitors in plants: Genes for improving defenses against insects and pathogens
    • Ryan, C. A. Protease inhibitors in plants: Genes for improving defenses against insects and pathogens. Annu. Rev. Phytopathol. 1990, 28, 425-449.
    • (1990) Annu. Rev. Phytopathol. , vol.28 , pp. 425-449
    • Ryan, C.A.1
  • 6
    • 0031111489 scopus 로고    scopus 로고
    • Biological effects of canatoxin in different insect models: Evidence for a proteolytic activation of the toxin by insect cathepsinlike enzymes
    • Carlini, C. R.; Oliveira, A. E. A.; Azambuja, P.; Xavier-Filho, J.; Wells, M. A. Biological effects of canatoxin in different insect models: Evidence for a proteolytic activation of the toxin by insect cathepsinlike enzymes. J. Econ. Entomol. 1997, 90, 340-348.
    • (1997) J. Econ. Entomol. , vol.90 , pp. 340-348
    • Carlini, C.R.1    Oliveira, A.E.A.2    Azambuja, P.3    Xavier-Filho, J.4    Wells, M.A.5
  • 8
    • 0029347190 scopus 로고
    • Plant defensins: Novel antimicrobial peptides as components of the host defense system
    • Broekaert, W. F.; Terras, F. R. G.; Cammue, B. P. A.; Osborn, R. W. Plant defensins: Novel antimicrobial peptides as components of the host defense system. Plant Physiol. 1995, 108, 1353-1358.
    • (1995) Plant Physiol. , vol.108 , pp. 1353-1358
    • Broekaert, W.F.1    Terras, F.R.G.2    Cammue, B.P.A.3    Osborn, R.W.4
  • 11
    • 0001102666 scopus 로고
    • Improved separation and toxicity analysis methods for purothionins
    • Jones, B. L.; Lookhart, G. L.; Johnson, D. E. Improved separation and toxicity analysis methods for purothionins. Cereal Chem. 1985, 62, 327-331.
    • (1985) Cereal Chem. , vol.62 , pp. 327-331
    • Jones, B.L.1    Lookhart, G.L.2    Johnson, D.E.3
  • 12
    • 0001737737 scopus 로고
    • Inheritance of resistance to infestation with azuki bean weevil in Vigna sublobata and successful incorporation to V. radiata
    • Kitamura, K.; Ishimoto, M.; Sawa, M. Inheritance of resistance to infestation with azuki bean weevil in Vigna sublobata and successful incorporation to V. radiata. Jpn. J. Breed. 1988, 38, 459-464.
    • (1988) Jpn. J. Breed. , vol.38 , pp. 459-464
    • Kitamura, K.1    Ishimoto, M.2    Sawa, M.3
  • 13
    • 85006118805 scopus 로고
    • Patterns of resistance to bean weevils (Bruchidae) in Vigna radiata-mungo-sublobata complex inform the breeding of new resistant varieties
    • Fujii, K.; Ishimoto, M.; Kitamura, K. Patterns of resistance to bean weevils (Bruchidae) in Vigna radiata-mungo-sublobata complex inform the breeding of new resistant varieties. Appl. Entomol. Zool. 1989, 24, 126-132.
    • (1989) Appl. Entomol. Zool. , vol.24 , pp. 126-132
    • Fujii, K.1    Ishimoto, M.2    Kitamura, K.3
  • 14
    • 0024978113 scopus 로고
    • A small-scale procedure for the rapid isolation of plant RNAs
    • Verwocrd, T. C.; Dekker, B. M. M.; Hockema, A. A small-scale procedure for the rapid isolation of plant RNAs. Nucleic Acids Res. 1989, 17, 2362.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 2362
    • Verwocrd, T.C.1    Dekker, B.M.M.2    Hockema, A.3
  • 16
    • 0028171162 scopus 로고
    • Ultrafast DNA Recovery from agarose by centrifugation through a paper slurry
    • Chuang, S. E.; Blattner, F. R. Ultrafast DNA Recovery from agarose by centrifugation through a paper slurry. Biotechniques 1994, 17, 634-636.
    • (1994) Biotechniques , vol.17 , pp. 634-636
    • Chuang, S.E.1    Blattner, F.R.2
  • 18
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0000401178 scopus 로고
    • Artificial seed system for bioassay of cowpea weevil (Coleoptera: Bruchidae) growth and development
    • Shade, R. E.; Murdock, L. L.; Foard, D. E.; Pomeroy, M. A. Artificial seed system for bioassay of cowpea weevil (Coleoptera: Bruchidae) growth and development. Environ. Entomol. 1986, 15, 1286-1291.
    • (1986) Environ. Entomol. , vol.15 , pp. 1286-1291
    • Shade, R.E.1    Murdock, L.L.2    Foard, D.E.3    Pomeroy, M.A.4
  • 20
    • 0025080513 scopus 로고
    • γ-purothionins: Amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm
    • Colilla, F. J.; Rocher, A.; Mendez, E. γ-purothionins: Amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm. FEBS Lett. 1990, 270, 191-194.
    • (1990) FEBS Lett. , vol.270 , pp. 191-194
    • Colilla, F.J.1    Rocher, A.2    Mendez, E.3
  • 22
    • 0031436066 scopus 로고    scopus 로고
    • An antimicrobial peptide from the Australian native Hardenbergia violacea provides the first functionally characterized member of a subfamily of plant defensins
    • Harrison, S. J.; Marcus, J. P.; Goulter, K. C.; Green, J. L.; Maclean, D. J.; Manners, J. M. An antimicrobial peptide from the Australian native Hardenbergia violacea provides the first functionally characterized member of a subfamily of plant defensins. Aust. J. Plant Physiol. 1997, 24, 571-578.
    • (1997) Aust. J. Plant Physiol. , vol.24 , pp. 571-578
    • Harrison, S.J.1    Marcus, J.P.2    Goulter, K.C.3    Green, J.L.4    Maclean, D.J.5    Manners, J.M.6
  • 23
    • 0032544607 scopus 로고    scopus 로고
    • Novel defensin subfamily from spinach (Spinacia oleracea)
    • Segura, A.; Moreno, M.; Molina, A.; Garcia-Olmedo, F. Novel defensin subfamily from spinach (Spinacia oleracea). FEBS Lett. 1998, 435, 159-162.
    • (1998) FEBS Lett. , vol.435 , pp. 159-162
    • Segura, A.1    Moreno, M.2    Molina, A.3    Garcia-Olmedo, F.4
  • 27
    • 0025080513 scopus 로고
    • γ-purothionins: Amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm
    • Colilla, F. J.; Rocher, A.; Mendez, E. γ-purothionins: Amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm. FEBS Lett. 1990, 270, 191-194.
    • (1990) FEBS Lett. , vol.270 , pp. 191-194
    • Colilla, F.J.1    Rocher, A.2    Mendez, E.3
  • 28
    • 0025670589 scopus 로고
    • Primary structure and inhibition of protein synthesis in eukaryotic cell-free system of a novel thionin, γ-hordothionin, from barley endosperm
    • Mendez, E.; Moreno, A.; Colilla, F.; Pelaez, F.; Limas, G. G.; Mendez, R.; Soriano, F.; Salinas, M.; de Haro, C. Primary structure and inhibition of protein synthesis in eukaryotic cell-free system of a novel thionin, γ-hordothionin, from barley endosperm, Eur. J. Biochem. 1990, 194, 533-539.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 533-539
    • Mendez, E.1    Moreno, A.2    Colilla, F.3    Pelaez, F.4    Limas, G.G.5    Mendez, R.6    Soriano, F.7    Salinas, M.8    De Haro, C.9
  • 29
    • 0025976182 scopus 로고
    • A new family of small (5 kDa) protein inhibitors of insect α-amylases from seeds or sorghum (Sorghum bicolor (L.) Moench) have sequence homologies with wheat γ-purothionins
    • Bloch, C., Jr.; Richardson, M. A new family of small (5 kDa) protein inhibitors of insect α-amylases from seeds or sorghum (Sorghum bicolor (L.) Moench) have sequence homologies with wheat γ-purothionins. FEBS Lett. 1991, 279, 101-104.
    • (1991) FEBS Lett. , vol.279 , pp. 101-104
    • Bloch C., Jr.1    Richardson, M.2
  • 30
    • 0028924455 scopus 로고
    • Amino acid sequence and disulphide-bridge pattern of three γ-thionins from Sorghum bicolor
    • Nitti, G.; Orru, S.; Bloch, C., Jr.; Morhy, L.; Marino, G.; Pucci, P. Amino acid sequence and disulphide-bridge pattern of three γ-thionins from Sorghum bicolor. Eur. J. Biochem. 1995, 228, 250-256.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 250-256
    • Nitti, G.1    Orru, S.2    Bloch C., Jr.3    Morhy, L.4    Marino, G.5    Pucci, P.6
  • 31
    • 0032436013 scopus 로고    scopus 로고
    • Functional and structural features of γ-zeathionins, a new class of sodium channel blockers
    • Kushmerick, C.; de Souza Castro, M.; Santos Cruz, J.; Bloch, C., Jr.; Beirao, P. S. L. Functional and structural features of γ-zeathionins, a new class of sodium channel blockers. FEBS Lett. 1998, 440, 302-306.
    • (1998) FEBS Lett. , vol.440 , pp. 302-306
    • Kushmerick, C.1    De Souza Castro, M.2    Santos Cruz, J.3    Bloch C., Jr.4    Beirao, P.S.L.5
  • 32
    • 0030935921 scopus 로고    scopus 로고
    • Fabatins: New antimicrobial plant peptides
    • Zhang, Y.; Lewis, K. Fabatins: New antimicrobial plant peptides. FEMS Microbiol. Lett. 1997, 149, 59-64.
    • (1997) FEMS Microbiol. Lett. , vol.149 , pp. 59-64
    • Zhang, Y.1    Lewis, K.2
  • 33
    • 0030265843 scopus 로고    scopus 로고
    • Fruit-specific expression of a defensin-type gene family in bell pepper. Upregulation during ripening and upon wounding
    • Meyer, B.; Houlne, G.; Pozueta-Romero, J.; Schantz, M. L.; Schantz, R. Fruit-specific expression of a defensin-type gene family in bell pepper. Upregulation during ripening and upon wounding. Plant Physiol. 1996, 112, 615-622.
    • (1996) Plant Physiol. , vol.112 , pp. 615-622
    • Meyer, B.1    Houlne, G.2    Pozueta-Romero, J.3    Schantz, M.L.4    Schantz, R.5
  • 34
    • 0025461638 scopus 로고
    • Stored mRNA in cotyledons of Vigna unguiculata seeds: Nucleotide sequence of cloned cDNA for a stored mRNA and induction of its synthesis by precocious germination
    • Ishibashi, N.; Yamauchi, D.; Minamikawa, T. Stored mRNA in cotyledons of Vigna unguiculata seeds: Nucleotide sequence of cloned cDNA for a stored mRNA and induction of its synthesis by precocious germination. Plant Mol. Biol. 1990, 15, 59-64.
    • (1990) Plant Mol. Biol. , vol.15 , pp. 59-64
    • Ishibashi, N.1    Yamauchi, D.2    Minamikawa, T.3
  • 35
    • 0026183530 scopus 로고
    • The Fusarium solani-induced expression of a pea gene family encoding high cysteine content proteins
    • Chiang, C. C.; Hadwiger, L. A. The Fusarium solani-induced expression of a pea gene family encoding high cysteine content proteins. Mol. Plant Microb. Interact. 1991, 4, 324-331.
    • (1991) Mol. Plant Microb. Interact. , vol.4 , pp. 324-331
    • Chiang, C.C.1    Hadwiger, L.A.2
  • 37
    • 0028519172 scopus 로고
    • Characterization of a predominantly pistil-expressed gene encoding a gamma-thionin-like protein of Petunia inflata
    • Karunanandaa, B.; Singh, A.; Kao, T. H. Characterization of a predominantly pistil-expressed gene encoding a gamma-thionin-like protein of Petunia inflata. Plant Mol. Biol. 1994, 26, 459-464.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 459-464
    • Karunanandaa, B.1    Singh, A.2    Kao, T.H.3
  • 40
    • 0031842957 scopus 로고    scopus 로고
    • Genetic localization of a bruchid resistance gene and its relationship to insecticidal cyclopeptide alkaloids, the vignatic acids, in mungbean (Vigna radiata L. Wilczek)
    • Kaga, A.; Ishimoto, M. Genetic localization of a bruchid resistance gene and its relationship to insecticidal cyclopeptide alkaloids, the vignatic acids, in mungbean (Vigna radiata L. Wilczek). Mol. Gen. Genet. 1998, 258, 378-384.
    • (1998) Mol. Gen. Genet. , vol.258 , pp. 378-384
    • Kaga, A.1    Ishimoto, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.