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Volumn 31, Issue 5, 1996, Pages 993-1008

Antimicrobial peptides from Mirabilis jalapa and Amaranthus caudatus: Expression, processing, localization and biological activity in transgenic tobacco

Author keywords

antifungal; disease resistance; genetic engineering; precursor processing; protein sorting

Indexed keywords

ALTERNARIA LONGIPES; AMARANTHUS CAUDATUS; BOTRYOTINIA FUCKELIANA; BOTRYTIS; FUNGI IMPERFECTI; HORDEUM VULGARE SUBSP. VULGARE; MIRABILIS JALAPA; NICOTIANA TABACUM;

EID: 0030220499     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00040718     Document Type: Review
Times cited : (108)

References (56)
  • 2
    • 0026251845 scopus 로고
    • The barley lectin carboxyl-terminal propeptide is a vacuolar protein sorting determinant in plants
    • Bednarek SY, Raikhel NV: The barley lectin carboxyl-terminal propeptide is a vacuolar protein sorting determinant in plants. Plant Cell 3: 1195-1206 (1991).
    • (1991) Plant Cell , vol.3 , pp. 1195-1206
    • Bednarek, S.Y.1    Raikhel, N.V.2
  • 3
    • 0026930761 scopus 로고
    • Intracellular trafficking of secretory proteins
    • Bednarek SY, Raikhel NV: Intracellular trafficking of secretory proteins. Plant Mol Biol 20: 133-150 (1992).
    • (1992) Plant Mol Biol , vol.20 , pp. 133-150
    • Bednarek, S.Y.1    Raikhel, N.V.2
  • 4
    • 0025574861 scopus 로고
    • A carboxyl-terminal propeptide is necessary for proper sorting of barley lectin to vacuoles of tobacco
    • Bednarek SY, Wilkins TA, Dombrowski JE, Raikhel NV: A carboxyl-terminal propeptide is necessary for proper sorting of barley lectin to vacuoles of tobacco. Plant Cell 2: 1145-1155 (1990).
    • (1990) Plant Cell , vol.2 , pp. 1145-1155
    • Bednarek, S.Y.1    Wilkins, T.A.2    Dombrowski, J.E.3    Raikhel, N.V.4
  • 5
    • 0021771482 scopus 로고
    • Binary Agrobacterium vectors for plant transformation
    • Bevan M: Binary Agrobacterium vectors for plant transformation. Nucl Acids Res 12: 8711-8721 (1984).
    • (1984) Nucl Acids Res , vol.12 , pp. 8711-8721
    • Bevan, M.1
  • 7
    • 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: 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).
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0029347190 scopus 로고
    • Plant defensins: Novel antimicrobial peptides as components of the host defense system
    • Broekaert WF, Terras FRG, Cammue BPA, Osborn RW: Plant defensins: novel antimicrobial peptides as components of the host defense system. Plant Physiol 108: 1353-1358 (1995).
    • (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
  • 15
    • 0027564534 scopus 로고
    • Expression of the α-thionin gene from barley in tobacco confers enhanced resistance to bacterial pathogens
    • Carmona MJ, Molina A, Fernández JA, López-Fando J, Gárcia-Olmedo F: Expression of the α-thionin gene from barley in tobacco confers enhanced resistance to bacterial pathogens. Plant J. 3: 457-462 (1993).
    • (1993) Plant J. , vol.3 , pp. 457-462
    • Carmona, M.J.1    Molina, A.2    Fernández, J.A.3    López-Fando, J.4    Gárcia-Olmedo, F.5
  • 16
    • 0028168377 scopus 로고
    • A novel α-amylase inhibitor from amaranth (Amaranthus hypocondriacus) seeds
    • Chagolla-Lopez A, Blanco-Labra A, Patthy A, Sanchez R, Ponger S: A novel α-amylase inhibitor from amaranth (Amaranthus hypocondriacus) seeds. J Biol Chem 269: 23675-23680 (1994).
    • (1994) J Biol Chem , vol.269 , pp. 23675-23680
    • Chagolla-Lopez, A.1    Blanco-Labra, A.2    Patthy, A.3    Sanchez, R.4    Ponger, S.5
  • 17
    • 0026532891 scopus 로고
    • Short peptide domains target proteins to plant vacuoles
    • Chrispeels MJ, Raikhel NV: Short peptide domains target proteins to plant vacuoles. Cell 68: 613-616 (1992).
    • (1992) Cell , vol.68 , pp. 613-616
    • Chrispeels, M.J.1    Raikhel, N.V.2
  • 18
    • 0000359996 scopus 로고
    • Plant gene expression in response to pathogens
    • Collinge DB, Slusarenko AJ: Plant gene expression in response to pathogens. Plant Mol Biol 9: 389-410 (1987).
    • (1987) Plant Mol Biol , vol.9 , pp. 389-410
    • Collinge, D.B.1    Slusarenko, A.J.2
  • 20
    • 0027661746 scopus 로고
    • Cloning and characterization of a cDNA encoding an antimicrobial chitin-binding protein from amaranth, Amaranthus caudatus
    • De Bolle MFC, David KMM, Rees SB, Vanderleyden J, Cammue BPA, Broekaert WF: Cloning and characterization of a cDNA encoding an antimicrobial chitin-binding protein from amaranth, Amaranthus caudatus. Plant Mol Biol 22: 1187-1190 (1993).
    • (1993) Plant Mol Biol , vol.22 , pp. 1187-1190
    • De Bolle, M.F.C.1    David, K.M.M.2    Rees, S.B.3    Vanderleyden, J.4    Cammue, B.P.A.5    Broekaert, W.F.6
  • 21
    • 0029328535 scopus 로고
    • Cloning and characterization of two cDNA clones encoding seed-specific antimicrobial peptides from Mirabilis jalapa L
    • De Bolle MFC, Eggermont K, Duncan RE, Osborn RW, Terras FRG, Broekaert WF: Cloning and characterization of two cDNA clones encoding seed-specific antimicrobial peptides from Mirabilis jalapa L. Plant Mol Biol 28: 713-721 (1995).
    • (1995) Plant Mol Biol , vol.28 , pp. 713-721
    • De Bolle, M.F.C.1    Eggermont, K.2    Duncan, R.E.3    Osborn, R.W.4    Terras, F.R.G.5    Broekaert, W.F.6
  • 22
    • 27044440776 scopus 로고
    • Mirabilis jalapa antimicrobial peptides and Raphanus sativus antifungal proteins: A comparative study of their structure and biological activities
    • Fritig B, Legrand M (eds) Kluwer Academic Publishers, Dordrecht
    • De Bolle MFC, Terras FRG, Cammue BPA, Rees SB, Broekaert WF: Mirabilis jalapa antimicrobial peptides and Raphanus sativus antifungal proteins: a comparative study of their structure and biological activities. In: Fritig B, Legrand M (eds) Mechanisms of Plant Defense Responses, pp. 433-436. Kluwer Academic Publishers, Dordrecht (1993).
    • (1993) Mechanisms of Plant Defense Responses , pp. 433-436
    • De Bolle, M.F.C.1    Terras, F.R.G.2    Cammue, B.P.A.3    Rees, S.B.4    Broekaert, W.F.5
  • 24
    • 0028005337 scopus 로고
    • Expression of biologically active hordothionins in tobacco. Effects of pre- and pro-sequences at the amino and carboxyl termini of the hordothionin precursor on mature protein expression and sorting
    • Florack DEA, Dirkse WG, Visser B, Heidekamp F, Stiekema WJ: Expression of biologically active hordothionins in tobacco. Effects of pre- and pro-sequences at the amino and carboxyl termini of the hordothionin precursor on mature protein expression and sorting. Plant Mol Biol 24: 83-96 (1994).
    • (1994) Plant Mol Biol , vol.24 , pp. 83-96
    • Florack, D.E.A.1    Dirkse, W.G.2    Visser, B.3    Heidekamp, F.4    Stiekema, W.J.5
  • 25
    • 0020574525 scopus 로고
    • A binary plant vector strategy based on separation of vir- and T-region of Agrobacterium tumefaciens Ti-plasmid
    • Hoekema A, Hirsch PR, Hooykaas PJJ, Schilperoort RA: A binary plant vector strategy based on separation of vir- and T-region of Agrobacterium tumefaciens Ti-plasmid. Nature 303: 179-180 (1983).
    • (1983) Nature , vol.303 , pp. 179-180
    • Hoekema, A.1    Hirsch, P.R.2    Hooykaas, P.J.J.3    Schilperoort, R.A.4
  • 26
    • 0026828751 scopus 로고
    • Proaleurain vacuolar targeting is mediated by short contiguous peptide interactions
    • Holwerda BC, Padgett HS, Rogers JC: Proaleurain vacuolar targeting is mediated by short contiguous peptide interactions. Plant Cell 4: 307-318 (1992).
    • (1992) Plant Cell , vol.4 , pp. 307-318
    • Holwerda, B.C.1    Padgett, H.S.2    Rogers, J.C.3
  • 29
    • 0023236892 scopus 로고
    • Duplication of CaMV 35S promoter sequences creates a strong enhancer for plant genes
    • Kay R, Chan A, Daly M, McPherson J: Duplication of CaMV 35S promoter sequences creates a strong enhancer for plant genes. Science 236: 1299-1302 (1987).
    • (1987) Science , vol.236 , pp. 1299-1302
    • Kay, R.1    Chan, A.2    Daly, M.3    McPherson, J.4
  • 30
    • 33644535944 scopus 로고
    • Pathogenesis-related proteins of plants
    • Linthorst HJM: Pathogenesis-related proteins of plants. Crit Rev Plant Sci 10: 123-150 (1991).
    • (1991) Crit Rev Plant Sci , vol.10 , pp. 123-150
    • Linthorst, H.J.M.1
  • 31
    • 0028208314 scopus 로고
    • Osmotin overexpression in potato delays the development of disease symptons
    • Liu D, Raghothama KG, Hasegawa PM, Bressan RA: Osmotin overexpression in potato delays the development of disease symptons. Proc Natl Acad Sci USA 91: 1888-1892 (1994).
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1888-1892
    • Liu, D.1    Raghothama, K.G.2    Hasegawa, P.M.3    Bressan, R.A.4
  • 32
    • 0026023554 scopus 로고
    • Propeptide of a precursor to a plant vacuolar protein required for vacuolar targeting
    • Matsuoka K, Nakamura K: Propeptide of a precursor to a plant vacuolar protein required for vacuolar targeting. Proc Natl Acad Sci USA 88: 834-838 (1991).
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 834-838
    • Matsuoka, K.1    Nakamura, K.2
  • 33
    • 0001324867 scopus 로고
    • Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combinations of chitinase and β-1.3-glucanase
    • Mauch F, Mauch-Mani B, Boller T: Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combinations of chitinase and β-1.3-glucanase. Plant Physiol 88: 936-942 (1988).
    • (1988) Plant Physiol , vol.88 , pp. 936-942
    • Mauch, F.1    Mauch-Mani, B.2    Boller, T.3
  • 36
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco tissue cultures
    • Murashige T, Skoog F: A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiol Plant 15: 473-497 (1962).
    • (1962) Physiol Plant , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 37
    • 0025935356 scopus 로고
    • High-level expression of tobacco chitinase gene in Nicotiana sylvestris. Susceptibility of transgenic plants to Cercospora nicotianae infection
    • Neuhaus J-M, Ahl-Goy P, Hinz U, Flores S, Meins F Jr: High-level expression of tobacco chitinase gene in Nicotiana sylvestris. Susceptibility of transgenic plants to Cercospora nicotianae infection. Plant Mol Biol 16: 141-151 (1991).
    • (1991) Plant Mol Biol , vol.16 , pp. 141-151
    • Neuhaus, J.-M.1    Ahl-Goy, P.2    Hinz, U.3    Flores, S.4    Meins Jr., F.5
  • 38
    • 0028002143 scopus 로고
    • Mutation analysis of the C-terminal vacuolar targeting peptide of tobacco chitinase: Low specificity of the sorting system, and gradual transition between intracellular retention and secretion into the extracellular space
    • Neuhaus J-M, Pietrzak M, Boller T: Mutation analysis of the C-terminal vacuolar targeting peptide of tobacco chitinase: low specificity of the sorting system, and gradual transition between intracellular retention and secretion into the extracellular space. Plant J 5: 45-54 (1994).
    • (1994) Plant J , vol.5 , pp. 45-54
    • Neuhaus, J.-M.1    Pietrzak, M.2    Boller, T.3
  • 39
    • 0025840612 scopus 로고
    • A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole
    • Neuhaus J-M, Sticher L, Meins F Jr, Boller T: A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole. Proc Natl Acad Sci USA 88: 10362-10366 (1991).
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10362-10366
    • Neuhaus, J.-M.1    Sticher, L.2    Meins Jr., F.3    Boller, T.4
  • 40
    • 0027631006 scopus 로고
    • An acidic class III chitinase in sugar beet: Induction by Cercospora beticola, characterization, and expression in transgenic tobacco plants
    • Nielsen KK, Mikkelsen JD, Kragh KM, Bojsen K: An acidic class III chitinase in sugar beet: induction by Cercospora beticola, characterization, and expression in transgenic tobacco plants. Mol Plant-Microbe Interact 6: 495-506 (1993).
    • (1993) Mol Plant-Microbe Interact , vol.6 , pp. 495-506
    • Nielsen, K.K.1    Mikkelsen, J.D.2    Kragh, K.M.3    Bojsen, K.4
  • 41
    • 0021919918 scopus 로고
    • Identification of DNA sequences required for activity of the cauliflower mosaic virus 35S promoter
    • Odell JT, Nagy F, Chua N-H: Identification of DNA sequences required for activity of the cauliflower mosaic virus 35S promoter. Nature 313: 810-812 (1985).
    • (1985) Nature , vol.313 , pp. 810-812
    • Odell, J.T.1    Nagy, F.2    Chua, N.-H.3
  • 47
    • 0026192098 scopus 로고
    • Transgenic tobacco plants expressing yeast-derived invertase in either the cytosol, vacuole or apoplast: A powerful tool for studying sucrose metabolism and sink/source interactions
    • Sonnewald U, Brauer M, von Schaewen A, Stitt M, Willmitzer L: Transgenic tobacco plants expressing yeast-derived invertase in either the cytosol, vacuole or apoplast: a powerful tool for studying sucrose metabolism and sink/source interactions. Plant J 1: 95-106 (1991).
    • (1991) Plant J , vol.1 , pp. 95-106
    • Sonnewald, U.1    Brauer, M.2    Von Schaewen, A.3    Stitt, M.4    Willmitzer, L.5
  • 49
    • 0025449585 scopus 로고
    • The pFF plasmids: Cassettes utilizing CaMV sequences for expression of foreign genes in plants
    • Timmermans MCP, Maliga P, Vieira J, Messing J: The pFF plasmids: cassettes utilizing CaMV sequences for expression of foreign genes in plants. J Biotechnol 14: 333-344 (1991).
    • (1991) J Biotechnol , vol.14 , pp. 333-344
    • Timmermans, M.C.P.1    Maliga, P.2    Vieira, J.3    Messing, J.4
  • 51
    • 0026823307 scopus 로고
    • Sorting of proteins to the vacuoles of plants
    • Vitale A, Chrispeels MJ: Sorting of proteins to the vacuoles of plants. BioEssays 14: 151-160 (1992).
    • (1992) BioEssays , vol.14 , pp. 151-160
    • Vitale, A.1    Chrispeels, M.J.2
  • 53
    • 0027182485 scopus 로고
    • A simple method of preparing plant samples for PCR
    • Wang H, Qi M, Cutler AJ: A simple method of preparing plant samples for PCR. Nucl Acids Res 17: 4153-4154 (1993).
    • (1993) Nucl Acids Res , vol.17 , pp. 4153-4154
    • Wang, H.1    Qi, M.2    Cutler, A.J.3
  • 54
    • 0025405663 scopus 로고
    • Role of propeptide glycan in post-translational processing and transport of barley lectin to vacuoles in transgenic tobacco
    • Wilkins TA, Bednarek SY, Raikhel NV: Role of propeptide glycan in post-translational processing and transport of barley lectin to vacuoles in transgenic tobacco. Plant Cell 2: 301-313 (1990).
    • (1990) Plant Cell , vol.2 , pp. 301-313
    • Wilkins, T.A.1    Bednarek, S.Y.2    Raikhel, N.V.3
  • 55
    • 0025358272 scopus 로고
    • A mutant neomycin phosphotransferase II gene reduces the resistance of transformants to antibiotic selection pressure
    • Yenofsky RL, Fine M, Pellow JW: A mutant neomycin phosphotransferase II gene reduces the resistance of transformants to antibiotic selection pressure. Proc Natl Acad Sci USA 87: 3435-3439 (1990).
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3435-3439
    • Yenofsky, R.L.1    Fine, M.2    Pellow, J.W.3
  • 56
    • 0028001451 scopus 로고
    • Enhanced protection against fungal attack by constitutive co-expression of chitinase and glucanase genes in transgenic tobacco
    • Zhu Q, Maher EA, Masoud S, Dixon RA, Lamb CJ: Enhanced protection against fungal attack by constitutive co-expression of chitinase and glucanase genes in transgenic tobacco. Bio/technology 12: 807-812 (1994).
    • (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


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