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Volumn 21, Issue 2, 2012, Pages 313-325

Transformation of tobacco and Arabidopsis plants with Stellaria media genes encoding novel hevein-like peptides increases their resistance to fungal pathogens

Author keywords

Antifungal resistance; Antimicrobial peptide; Arabidopsis thaliana; Hevein like peptide; Stellaria media

Indexed keywords

ANTIMICROBIAL CATIONIC PEPTIDE; HEVEIN; PLANT LECTIN; VEGETABLE PROTEIN;

EID: 84859104690     PISSN: 09628819     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11248-011-9534-6     Document Type: Article
Times cited : (34)

References (59)
  • 1
  • 2
    • 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 Lett 350: 159-163.
    • (1994) FEBS Lett , vol.350 , pp. 159-163
    • Beintema, J.J.1
  • 4
    • 11944249594 scopus 로고
    • Wound-induced accumulation of mRNA containing a hevein sequence in laticifers of rubber tree (Hevea brasiliensis)
    • Broekaert I, Lee HI, Kush A, Chua NH, Raikhel N (1990) Wound-induced accumulation of mRNA containing a hevein sequence in laticifers of rubber tree (Hevea brasiliensis). Proc Natl Acad Sci USA 87: 7633-7637.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 7633-7637
    • Broekaert, I.1    Lee, H.I.2    Kush, A.3    Chua, N.H.4    Raikhel, N.5
  • 6
    • 0029347190 scopus 로고
    • Plant defensins: novel antimicrobial peptides as components of the host defense system
    • Broekaert WF, Terras FR, Cammue BP, Osborn RW (1995) Plant defensins: novel antimicrobial peptides as components of the host defense system. Plant Physiol 108: 1353-1358.
    • (1995) Plant Physiol , vol.108 , pp. 1353-1358
    • Broekaert, W.F.1    Terras, F.R.2    Cammue, B.P.3    Osborn, R.W.4
  • 10
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough SJ, Bent AF (1998) Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J 16: 735-743.
    • (1998) Plant J , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 11
    • 0033579483 scopus 로고    scopus 로고
    • Plant cyclotides: a unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif
    • Craik DJ, Daly NL, Bond T, Waine C (1999) Plant cyclotides: a unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. J Mol Biol 294: 1327-1336.
    • (1999) J Mol Biol , vol.294 , pp. 1327-1336
    • Craik, D.J.1    Daly, N.L.2    Bond, T.3    Waine, C.4
  • 12
    • 0030220499 scopus 로고    scopus 로고
    • Antimicrobial peptides from Mirabilis jalapa and Amaranthus caudatus: expression, processing, localization and biological activity in transgenic tobacco
    • De Bolle MF, Osborn RW, Goderis IJ, Noe L, Acland D, Hart CA, Torrekens S, van Leuven F, Broekaert WF (1996) Antimicrobial peptides from Mirabilis jalapa and Amaranthus caudatus: expression, processing, localization and biological activity in transgenic tobacco. Plant Mol Biol 31: 993-1008.
    • (1996) Plant Mol Biol , vol.31 , pp. 993-1008
    • de Bolle, M.F.1    Osborn, R.W.2    Goderis, I.J.3    Noe, L.4    Acland, D.5    Hart, C.A.6    Torrekens, S.7    van Leuven, F.8    Broekaert, W.F.9
  • 14
    • 0031128435 scopus 로고    scopus 로고
    • Overexpression of an endogenous thionin enhances resistance of Arabidopsis against Fusarium oxysporum
    • Epple P, Apel K, Bohlmann H (1997) Overexpression of an endogenous thionin enhances resistance of Arabidopsis against Fusarium oxysporum. Plant Cell 9: 509-520.
    • (1997) Plant Cell , vol.9 , pp. 509-520
    • Epple, P.1    Apel, K.2    Bohlmann, H.3
  • 20
    • 61549102815 scopus 로고    scopus 로고
    • Pomegranin, an antifungal peptide from pomegranate peels
    • Guo G, Wang HX, Ng TB (2009) Pomegranin, an antifungal peptide from pomegranate peels. Protein Pept Lett 16: 82-85.
    • (2009) Protein Pept Lett , vol.16 , pp. 82-85
    • Guo, G.1    Wang, H.X.2    Ng, T.B.3
  • 21
    • 58149200923 scopus 로고    scopus 로고
    • PhytAMP: a database dedicated to antimicrobial plant peptides
    • (Database issue)
    • Hammami R, Ben Hamida J, Vergoten G, Fliss I (2009) PhytAMP: a database dedicated to antimicrobial plant peptides. Nucleic Acids Res 37(Database issue): D963-968.
    • (2009) Nucleic Acids Res , vol.37 , pp. 963-968
    • Hammami, R.1    Ben, H.J.2    Vergoten, G.3    Fliss, I.4
  • 23
    • 0034726049 scopus 로고    scopus 로고
    • Characteristics and antifungal activity of a chitin binding protein from Ginkgo biloba
    • Huang X, Xie W, Gong Z (2000) Characteristics and antifungal activity of a chitin binding protein from Ginkgo biloba. FEBS Lett 478: 123-126.
    • (2000) FEBS Lett , vol.478 , pp. 123-126
    • Huang, X.1    Xie, W.2    Gong, Z.3
  • 24
    • 0037134784 scopus 로고    scopus 로고
    • Two novel antifungal peptides distinct with a five-disulfide motif from the bark of Eucommia ulmoides Oliv
    • Huang RH, Xiang Y, Liu XZ, Zhang Y, Hu Z, Wang DC (2002) Two novel antifungal peptides distinct with a five-disulfide motif from the bark of Eucommia ulmoides Oliv. FEBS Lett 521: 87-90.
    • (2002) FEBS Lett , vol.521 , pp. 87-90
    • Huang, R.H.1    Xiang, Y.2    Liu, X.Z.3    Zhang, Y.4    Hu, Z.5    Wang, D.C.6
  • 25
    • 34547623918 scopus 로고    scopus 로고
    • Quality control of eukaryotic mRNA: safeguarding cells from abnormal mRNA function
    • Isken O, Maquat LE (2007) Quality control of eukaryotic mRNA: safeguarding cells from abnormal mRNA function. Genes Dev 21: 1833-1856.
    • (2007) Genes Dev , vol.21 , pp. 1833-1856
    • Isken, O.1    Maquat, L.E.2
  • 26
    • 77952241898 scopus 로고    scopus 로고
    • Expression of a plant defensin in rice confers resistance to fungal phytopathogens
    • Jha S, Chattoo BB (2010) Expression of a plant defensin in rice confers resistance to fungal phytopathogens. Transgenic Res 19: 373-384.
    • (2010) Transgenic Res , vol.19 , pp. 373-384
    • Jha, S.1    Chattoo, B.B.2
  • 27
    • 58349114242 scopus 로고    scopus 로고
    • Expression of Dm-AMP1 in rice confers resistance to Magnaporthe oryzae and Rhizoctonia solani
    • Jha S, Tank HG, Prasad BD, Chattoo BB (2009) Expression of Dm-AMP1 in rice confers resistance to Magnaporthe oryzae and Rhizoctonia solani. Transgenic Res 18: 59-69.
    • (2009) Transgenic Res , vol.18 , pp. 59-69
    • Jha, S.1    Tank, H.G.2    Prasad, B.D.3    Chattoo, B.B.4
  • 28
    • 13244279472 scopus 로고    scopus 로고
    • Rapid and reliable extraction of genomic DNA from various wild-type and transgenic plants
    • Kang TJ, Yang MS (2004) Rapid and reliable extraction of genomic DNA from various wild-type and transgenic plants. BMC Biotechnol 4: 20.
    • (2004) BMC Biotechnol , vol.4 , pp. 20
    • Kang, T.J.1    Yang, M.S.2
  • 29
    • 0037361851 scopus 로고    scopus 로고
    • C-terminal domain of a hevein-like protein from Wasabia japonica has potent antimicrobial activity
    • Kiba A, Saitoh H, Nishihara M, Omiya K, Yamamura S (2003) C-terminal domain of a hevein-like protein from Wasabia japonica has potent antimicrobial activity. Plant Cell Physiol 44: 296-303.
    • (2003) Plant Cell Physiol , vol.44 , pp. 296-303
    • Kiba, A.1    Saitoh, H.2    Nishihara, M.3    Omiya, K.4    Yamamura, S.5
  • 30
    • 78650384227 scopus 로고    scopus 로고
    • Transgenic tomato plants expressing recA and NLS-recA-licBM3 genes as a model for studying meiotic recombination
    • Komakhin R, Komakhina V, Milyukova N, Goldenkova-Pavlova I, Fadina O, Zhuchenko A (2010) Transgenic tomato plants expressing recA and NLS-recA-licBM3 genes as a model for studying meiotic recombination. Russ J Genet 46: 1440-1448.
    • (2010) Russ J Genet , vol.46 , pp. 1440-1448
    • Komakhin, R.1    Komakhina, V.2    Milyukova, N.3    Goldenkova-Pavlova, I.4    Fadina, O.5    Zhuchenko, A.6
  • 33
    • 13844322064 scopus 로고    scopus 로고
    • Defensins-components of the innate immune system in plants
    • Lay FT, Anderson MA (2005) Defensins-components of the innate immune system in plants. Curr Protein Pept Sci 6: 85-101.
    • (2005) Curr Protein Pept Sci , vol.6 , pp. 85-101
    • Lay, F.T.1    Anderson, M.A.2
  • 35
    • 0038693563 scopus 로고    scopus 로고
    • Cys/Gly-rich proteins with a putative single chitin-binding domain from oat (Avena sativa) seeds
    • Li SS, Claeson P (2003) Cys/Gly-rich proteins with a putative single chitin-binding domain from oat (Avena sativa) seeds. Phytochemistry 63: 249-255.
    • (2003) Phytochemistry , vol.63 , pp. 249-255
    • Li, S.S.1    Claeson, P.2
  • 36
    • 58549102353 scopus 로고    scopus 로고
    • Brassiparin, an antifungal peptide from Brassica parachinensis seeds
    • Lin P, Ng TB (2009) Brassiparin, an antifungal peptide from Brassica parachinensis seeds. J Appl Microbiol 106: 554-563.
    • (2009) J Appl Microbiol , vol.106 , pp. 554-563
    • Lin, P.1    Ng, T.B.2
  • 38
    • 0030997078 scopus 로고    scopus 로고
    • Purification, characterisation and cDNA cloning of an antimicrobial peptide from Macadamia integrifolia
    • Marcus JP, Goulter KC, Green JL, Harrison SJ, Manners JM (1997) Purification, characterisation and cDNA cloning of an antimicrobial peptide from Macadamia integrifolia. Eur J Biochem 244: 743-749.
    • (1997) Eur J Biochem , vol.244 , pp. 743-749
    • Marcus, J.P.1    Goulter, K.C.2    Green, J.L.3    Harrison, S.J.4    Manners, J.M.5
  • 39
    • 0032755341 scopus 로고    scopus 로고
    • MiAMP1, a novel protein from Macadamia integrifolia adopts a Greek key beta-barrel fold unique amongst plant antimicrobial proteins
    • McManus AM, Nielsen KJ, Marcus JP, Harrison SJ, Green JL, Manners JM, Craik DJ (1999) MiAMP1, a novel protein from Macadamia integrifolia adopts a Greek key beta-barrel fold unique amongst plant antimicrobial proteins. J Mol Biol 293: 629-638.
    • (1999) J Mol Biol , vol.293 , pp. 629-638
    • McManus, A.M.1    Nielsen, K.J.2    Marcus, J.P.3    Harrison, S.J.4    Green, J.L.5    Manners, J.M.6    Craik, D.J.7
  • 40
    • 0027507001 scopus 로고
    • Lipid transfer proteins (nsLTPs) from barley and maize leaves are potent inhibitors of bacterial and fungal plant pathogens
    • Molina A, Segura A, Garcia-Olmedo F (1993) Lipid transfer proteins (nsLTPs) from barley and maize leaves are potent inhibitors of bacterial and fungal plant pathogens. FEBS Lett 316: 119-122.
    • (1993) FEBS Lett , vol.316 , pp. 119-122
    • Molina, A.1    Segura, A.2    Garcia-Olmedo, F.3
  • 41
    • 0036281211 scopus 로고    scopus 로고
    • Processing of gene expression data generated by quantitative real-time RT-PCR
    • Muller PY, Janovjak H, Miserez AR, Dobbie Z (2002) Processing of gene expression data generated by quantitative real-time RT-PCR. Biotechniques 32: 1372-1379.
    • (2002) Biotechniques , vol.32 , pp. 1372-1379
    • Muller, P.Y.1    Janovjak, H.2    Miserez, A.R.3    Dobbie, Z.4
  • 42
    • 0015666367 scopus 로고
    • Nutrition of plant cells and organs in vitro
    • Murashige T (1973) Nutrition of plant cells and organs in vitro. In Vitro 9: 81-85.
    • (1973) In Vitro , vol.9 , pp. 81-85
    • Murashige, T.1
  • 43
    • 0031048304 scopus 로고    scopus 로고
    • Characterization of a new antifungal chitin-binding peptide from sugar beet leaves
    • Nielsen KK, Nielsen JE, Madrid SM, Mikkelsen JD (1997) Characterization of a new antifungal chitin-binding peptide from sugar beet leaves. Plant Physiol 113: 83-91.
    • (1997) Plant Physiol , vol.113 , pp. 83-91
    • Nielsen, K.K.1    Nielsen, J.E.2    Madrid, S.M.3    Mikkelsen, J.D.4
  • 45
    • 34249919394 scopus 로고
    • Hevein: an antifungal protein from rubber-tree (Hevea brasiliensis) latex
    • Parijs J, Broekaert W, Goldstein I, Peumans W (1991) Hevein: an antifungal protein from rubber-tree (Hevea brasiliensis) latex. Planta 183: 258-264.
    • (1991) Planta , vol.183 , pp. 258-264
    • Parijs, J.1    Broekaert, W.2    Goldstein, I.3    Peumans, W.4
  • 46
    • 0032570316 scopus 로고    scopus 로고
    • Structural studies of Impatiens balsamina antimicrobial protein (Ib-AMP1)
    • Patel SU, Osborn R, Rees S, Thornton JM (1998) Structural studies of Impatiens balsamina antimicrobial protein (Ib-AMP1). Biochemistry 37: 983-990.
    • (1998) Biochemistry , vol.37 , pp. 983-990
    • Patel, S.U.1    Osborn, R.2    Rees, S.3    Thornton, J.M.4
  • 47
    • 0032999903 scopus 로고    scopus 로고
    • Salicylic acid-independent plant defence pathways
    • Pieterse CM, van Loon LC (1999) Salicylic acid-independent plant defence pathways. Trends Plant Sci 4: 52-58.
    • (1999) Trends Plant Sci , vol.4 , pp. 52-58
    • Pieterse, C.M.1    van Loon, L.C.2
  • 50
    • 0032174012 scopus 로고    scopus 로고
    • Jasmonate and salicylate as global signals for defense gene expression
    • Reymond P, Farmer EE (1998) Jasmonate and salicylate as global signals for defense gene expression. Curr Opin Plant Biol 1: 404-411.
    • (1998) Curr Opin Plant Biol , vol.1 , pp. 404-411
    • Reymond, P.1    Farmer, E.E.2
  • 51
    • 0032987350 scopus 로고    scopus 로고
    • A new antifungal peptide from the seeds of Phytolacca americana: characterization, amino acid sequence and cDNA cloning
    • Shao F, Hu Z, Xiong YM, Huang QZ, Wang CG, Zhu RH, Wang DC (1999) A new antifungal peptide from the seeds of Phytolacca americana: characterization, amino acid sequence and cDNA cloning. Biochim Biophys Acta 1430: 262-268.
    • (1999) Biochim Biophys Acta , vol.1430 , pp. 262-268
    • Shao, F.1    Hu, Z.2    Xiong, Y.M.3    Huang, Q.Z.4    Wang, C.G.5    Zhu, R.H.6    Wang, D.C.7
  • 52
    • 54049126446 scopus 로고    scopus 로고
    • Transgenic tobacco and peanut plants expressing a mustard defensin show resistance to fungal pathogens
    • Swathi Anuradha T, Divya K, Jami SK, Kirti PB (2008) Transgenic tobacco and peanut plants expressing a mustard defensin show resistance to fungal pathogens. Plant Cell Rep 27: 1777-1786.
    • (2008) Plant Cell Rep , vol.27 , pp. 1777-1786
    • Swathi, A.T.1    Divya, K.2    Jami, S.K.3    Kirti, P.B.4
  • 56
    • 0033981958 scopus 로고    scopus 로고
    • Specific binding sites for an antifungal plant defensin from Dahlia (Dahlia merckii) on fungal cells are required for antifungal activity
    • Thevissen K, Osborn RW, Acland DP, Broekaert WF (2000) Specific binding sites for an antifungal plant defensin from Dahlia (Dahlia merckii) on fungal cells are required for antifungal activity. Mol Plant Microbe Interact 13: 54-61.
    • (2000) Mol Plant Microbe Interact , vol.13 , pp. 54-61
    • Thevissen, K.1    Osborn, R.W.2    Acland, D.P.3    Broekaert, W.F.4
  • 58
    • 0037163895 scopus 로고    scopus 로고
    • Five disulfide bridges stabilize a hevein-type antimicrobial peptide from the bark of spindle tree (Euonymus europaeus L.)
    • van den Bergh KP, Proost P, van Damme J, Coosemans J, van Damme EJ, Peumans WJ (2002) Five disulfide bridges stabilize a hevein-type antimicrobial peptide from the bark of spindle tree (Euonymus europaeus L.). FEBS Lett 530: 181-185.
    • (2002) FEBS Lett , vol.530 , pp. 181-185
    • van den Bergh, K.P.1    Proost, P.2    van Damme, J.3    Coosemans, J.4    van Damme, E.J.5    Peumans, W.J.6
  • 59
    • 33845435000 scopus 로고    scopus 로고
    • Agrobacterium-mediated transformation of Arabidopsis thaliana using the floral dip method
    • Zhang X, Henriques R, Lin SS, Niu QW, Chua NH (2006) Agrobacterium-mediated transformation of Arabidopsis thaliana using the floral dip method. Nat Protoc 1: 641-646.
    • (2006) Nat Protoc , vol.1 , pp. 641-646
    • Zhang, X.1    Henriques, R.2    Lin, S.S.3    Niu, Q.W.4    Chua, N.H.5


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