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Volumn 17, Issue 1, 1999, Pages 64-73

Heterologous expression of the avirulence gene product, NIP1, from the barley pathogen Rhynchosporium secalis

Author keywords

[No Author keywords available]

Indexed keywords

BARLEY; ESCHERICHIA COLI; FUNGAL CELL CULTURE; FUNGAL GENE; GENE PRODUCT; HETEROLOGOUS PRODUCT; PLANT PATHOLOGY; PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; RECOMBINANT PROTEIN; RHYNCHOSPORIUM SECALIS;

EID: 0345713191     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1999.1098     Document Type: Article
Times cited : (11)

References (47)
  • 1
    • 0028852788 scopus 로고
    • Defense responses of plants to pathogens
    • J. H. Andrews, & I. C. Tommerup. London: Academic Press
    • Kombrink E., Somssich I. E. Defense responses of plants to pathogens. Andrews J. H., Tommerup I. C. Advances in Botanical Research. 1995;1-34 Academic Press, London.
    • (1995) Advances in Botanical Research , pp. 1-34
    • Kombrink, E.1    Somssich, I.E.2
  • 3
    • 0001119910 scopus 로고
    • Current status of the gene-for-gene concept
    • Flor H. H. Current status of the gene-for-gene concept. Annu. Rev. Phytopathol. 9:1971;275-296.
    • (1971) Annu. Rev. Phytopathol. , vol.9 , pp. 275-296
    • Flor, H.H.1
  • 4
    • 0011985520 scopus 로고
    • Specific recognition in gene-for-gene host-parasite systems
    • Keen N. T. Specific recognition in gene-for-gene host-parasite systems. Adv. Plant Pathol. 1:1982;35-82.
    • (1982) Adv. Plant Pathol. , vol.1 , pp. 35-82
    • Keen, N.T.1
  • 5
    • 0030451577 scopus 로고    scopus 로고
    • Fungal infection of plants
    • Knogge W. Fungal infection of plants. Plant Cell. 8:1996;1711-1722.
    • (1996) Plant Cell , vol.8 , pp. 1711-1722
    • Knogge, W.1
  • 6
    • 0004934717 scopus 로고    scopus 로고
    • Molecular characterization of fungal avirulence
    • I. R. Crute, & E. B. Holub. Wallingford: CAB International
    • Knogge W., Marie C. Molecular characterization of fungal avirulence. Crute I. R., Holub E. B. The Gene-for-Gene Relationship in Plant-Parasite Interactions. 1997;329-346 CAB International, Wallingford.
    • (1997) The Gene-for-Gene Relationship in Plant-Parasite Interactions , pp. 329-346
    • Knogge, W.1    Marie, C.2
  • 7
    • 0030476760 scopus 로고    scopus 로고
    • A ligand-receptor mechanism in plant-pathogen recognition
    • Lamb C. A ligand-receptor mechanism in plant-pathogen recognition. Science. 274:1996;2038-2039.
    • (1996) Science , vol.274 , pp. 2038-2039
    • Lamb, C.1
  • 9
    • 0027326649 scopus 로고
    • Identification of a novel high-affinity binding site for N-acetylchitooligosaccharide elicitor in the membrane fraction from suspension-cultured rice cells
    • Shibuya N., Kaku H., Kuchitsu K., Maliarik M. J. Identification of a novel high-affinity binding site for N-acetylchitooligosaccharide elicitor in the membrane fraction from suspension-cultured rice cells. FEBS Lett. 329:1993;75-78.
    • (1993) FEBS Lett. , vol.329 , pp. 75-78
    • Shibuya, N.1    Kaku, H.2    Kuchitsu, K.3    Maliarik, M.J.4
  • 10
    • 0027967403 scopus 로고
    • High affinity binding of a fungal oligopeptide elicitor to parsley plasma membranes triggers multiple defense responses
    • Nürnberger T., Nennstiel D., Jabs T., Sacks W. R., Hahlbrock K., Scheel D. High affinity binding of a fungal oligopeptide elicitor to parsley plasma membranes triggers multiple defense responses. Cell. 78:1994;449-460.
    • (1994) Cell , vol.78 , pp. 449-460
    • Nürnberger, T.1    Nennstiel, D.2    Jabs, T.3    Sacks, W.R.4    Hahlbrock, K.5    Scheel, D.6
  • 11
    • 0009504058 scopus 로고
    • Plant disease resistance genes: Unravelling how they work
    • Hammond-Kosack K. E., Jones J. D. G. Plant disease resistance genes: Unravelling how they work. Can. J. Bot. 73:1995;S495-S505.
    • (1995) Can. J. Bot. , vol.73
    • Hammond-Kosack, K.E.1    Jones, J.D.G.2
  • 12
    • 0029978777 scopus 로고    scopus 로고
    • Plant disease resistance genes - Structure, function and evolution
    • Jones J. D. G. Plant disease resistance genes - Structure, function and evolution. Curr. Opin. Biotechnol. 1996;155-160.
    • (1996) Curr. Opin. Biotechnol. , pp. 155-160
    • Jones, J.D.G.1
  • 13
    • 0031194195 scopus 로고    scopus 로고
    • Recognition of bacterial avirulence proteins occurs inside the plant cell: A general phenomenon in resistance to bacterial diseases
    • Bonas U., van den Ackerveken G. Recognition of bacterial avirulence proteins occurs inside the plant cell: A general phenomenon in resistance to bacterial diseases. Plant J. 12:1997;1-7.
    • (1997) Plant J. , vol.12 , pp. 1-7
    • Bonas, U.1    Van Den Ackerveken, G.2
  • 14
    • 0027998238 scopus 로고
    • The enigmatic avirulence genes of phytopathogenic bacteria
    • J. L. Dangl. Berlin: Springer-Verlag
    • Dangl J. L. The enigmatic avirulence genes of phytopathogenic bacteria. Dangl J. L. Bacterial Pathogenesis of Plants and Animals. 1994;99-118 Springer-Verlag, Berlin.
    • (1994) Bacterial Pathogenesis of Plants and Animals , pp. 99-118
    • Dangl, J.L.1
  • 17
    • 0029085967 scopus 로고
    • The race-specific elicitor, NIP1, from the barley pathogen, Rhynchosporium secalis, determines avirulence on host plants of the Rrs1 resistance genotype
    • Rohe M., Gierlich A., Hermann H., Hahn M., Schmidt B., Rosahl S., Knogge W. The race-specific elicitor, NIP1, from the barley pathogen, Rhynchosporium secalis, determines avirulence on host plants of the Rrs1 resistance genotype. EMBO J. 14:1995;4168-4177.
    • (1995) EMBO J. , vol.14 , pp. 4168-4177
    • Rohe, M.1    Gierlich, A.2    Hermann, H.3    Hahn, M.4    Schmidt, B.5    Rosahl, S.6    Knogge, W.7
  • 18
    • 0027692110 scopus 로고
    • Cultivar-specific elicitation of barley defense reactions by the phytotoxic peptide NIP1 from Rhynchosporium secalis
    • Hahn M., Jüngling S., Knogge W. Cultivar-specific elicitation of barley defense reactions by the phytotoxic peptide NIP1 from Rhynchosporium secalis. Mol. Plant-Microbe Interact. 6:1993;745-754.
    • (1993) Mol. Plant-Microbe Interact. , vol.6 , pp. 745-754
    • Hahn, M.1    Jüngling, S.2    Knogge, W.3
  • 19
    • 0016167677 scopus 로고
    • β-Galactosidase from termination and deletion mutant strains
    • Villarejo M. R., Zabin I. β-Galactosidase from termination and deletion mutant strains. J. Bacteriol. 120:1974;466-474.
    • (1974) J. Bacteriol. , vol.120 , pp. 466-474
    • Villarejo, M.R.1    Zabin, I.2
  • 21
    • 0023091932 scopus 로고
    • Baculovirus expression vectors: The requirements for high level expression of proteins including glycoproteins
    • Matsuura Y., Possee R. D., Overton H. A., Bishop D. H. L. Baculovirus expression vectors: The requirements for high level expression of proteins including glycoproteins. J. Gen. Virol. 68:1987;1233-1250.
    • (1987) J. Gen. Virol. , vol.68 , pp. 1233-1250
    • Matsuura, Y.1    Possee, R.D.2    Overton, H.A.3    Bishop, D.H.L.4
  • 22
    • 0023881356 scopus 로고
    • Trends in the development of baculovirus expression vectors
    • Luckow V. A., Summers M. D. Trends in the development of baculovirus expression vectors. Bio/Technology. 6:1988;47-55.
    • (1988) Bio/Technology , vol.6 , pp. 47-55
    • Luckow, V.A.1    Summers, M.D.2
  • 23
    • 0026335593 scopus 로고
    • Expression of protein kinase C isotypes using baculovirus vectors
    • Stabel S., Schaap D., Parker P. J. Expression of protein kinase C isotypes using baculovirus vectors. Methods Enzymol. 200:1991;670-673.
    • (1991) Methods Enzymol. , vol.200 , pp. 670-673
    • Stabel, S.1    Schaap, D.2    Parker, P.J.3
  • 24
    • 0026575323 scopus 로고
    • Expression of a pheromone-binding protein in insect cells using a baculovirus vector
    • Krieger J., Raming K., Prestwich G. D., Frith D., Stabel S., Breer H. Expression of a pheromone-binding protein in insect cells using a baculovirus vector. Eur. J. Biochem. 203:1992;161-166.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 161-166
    • Krieger, J.1    Raming, K.2    Prestwich, G.D.3    Frith, D.4    Stabel, S.5    Breer, H.6
  • 26
    • 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. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum H., Beier H., Gross H. J. Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis. 8:1987;93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 29
    • 0000728604 scopus 로고
    • Purification and characterization of peptides from Rhynchosporium secalis inducing necrosis in barley
    • Wevelsiep L., Kogel K. H., Knogge W. Purification and characterization of peptides from Rhynchosporium secalis inducing necrosis in barley. Physiol. Mol. Plant Pathol. 39:1991;471-482.
    • (1991) Physiol. Mol. Plant Pathol. , vol.39 , pp. 471-482
    • Wevelsiep, L.1    Kogel, K.H.2    Knogge, W.3
  • 32
    • 0032007853 scopus 로고    scopus 로고
    • Strategies for optimizing heterologous protein expression in Escherichia coli
    • Hannig G., Makrides S. C. Strategies for optimizing heterologous protein expression in Escherichia coli. Trends Biotechnol. 16:1998;54-60.
    • (1998) Trends Biotechnol. , vol.16 , pp. 54-60
    • Hannig, G.1    Makrides, S.C.2
  • 33
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides S. C. Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev. 60:1996;512-538.
    • (1996) Microbiol. Rev. , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 35
    • 0021010433 scopus 로고
    • Production of human β interferon in insect cells infected with a baculovirus expression vector
    • Smith G. E., Summers M. D., Fraser M. J. Production of human β interferon in insect cells infected with a baculovirus expression vector. Mol. Cell. Biol. 3:1983;2156-2165.
    • (1983) Mol. Cell. Biol. , vol.3 , pp. 2156-2165
    • Smith, G.E.1    Summers, M.D.2    Fraser, M.J.3
  • 36
    • 0028287188 scopus 로고
    • Engineering proteins to facilitate bioprocessing
    • Nygren P. A., Stahl S., Uhlen M. Engineering proteins to facilitate bioprocessing. Trends Biotechnol. 12:1994;184-188.
    • (1994) Trends Biotechnol. , vol.12 , pp. 184-188
    • Nygren, P.A.1    Stahl, S.2    Uhlen, M.3
  • 37
    • 0021811719 scopus 로고
    • Direct cloning of the trx-B gene that encodes thioredoxin reductase
    • Russel M., Model P. Direct cloning of the trx-B gene that encodes thioredoxin reductase. J. Bacteriol. 163:1985;238-242.
    • (1985) J. Bacteriol. , vol.163 , pp. 238-242
    • Russel, M.1    Model, P.2
  • 38
    • 0027739665 scopus 로고
    • Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli
    • Derman A. I., Prinz W. A., Belin D., Beckwith J. Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science. 262:1993;1744-1747.
    • (1993) Science , vol.262 , pp. 1744-1747
    • Derman, A.I.1    Prinz, W.A.2    Belin, D.3    Beckwith, J.4
  • 39
    • 0029017155 scopus 로고
    • Escherichia coli alkaline phosphatase localized to the cytoplasm slowly acquires enzymatic activity in cells whose growth has been suspended: A caution for gene fusion studies
    • Derman A. I., Beckwith J. Escherichia coli alkaline phosphatase localized to the cytoplasm slowly acquires enzymatic activity in cells whose growth has been suspended: A caution for gene fusion studies. J. Bacteriol. 177:1995;3764-3770.
    • (1995) J. Bacteriol. , vol.177 , pp. 3764-3770
    • Derman, A.I.1    Beckwith, J.2
  • 40
    • 0031060711 scopus 로고    scopus 로고
    • Hydrophobins: Proteins that change the nature of the fungal surface
    • Wessels J. G. Hydrophobins: proteins that change the nature of the fungal surface. Adv. Microbial Physiol. 38:1997;1-45.
    • (1997) Adv. Microbial Physiol. , vol.38 , pp. 1-45
    • Wessels, J.G.1
  • 41
    • 0028045183 scopus 로고
    • Developmental regulation of fungal wall formation
    • Wessels J. G. H. Developmental regulation of fungal wall formation. Annu. Rev. Phytopathol. 32:1994;413-437.
    • (1994) Annu. Rev. Phytopathol. , vol.32 , pp. 413-437
    • Wessels, J.G.H.1
  • 42
    • 0345073927 scopus 로고    scopus 로고
    • Fungal hydrophobins: Proteins that function at an interface
    • Wessels J. G. H. Fungal hydrophobins: proteins that function at an interface. Trends Plant Sci. 1:1996;9-15.
    • (1996) Trends Plant Sci. , vol.1 , pp. 9-15
    • Wessels, J.G.H.1
  • 43
    • 0027549454 scopus 로고
    • Cerato-ulmin, a toxin involved in Dutch elm diseases, is a fungal hydrophobin
    • Stringer M. A., Timberlake W. E. Cerato-ulmin, a toxin involved in Dutch elm diseases, is a fungal hydrophobin. Plant Cell. 5:1993;145-146.
    • (1993) Plant Cell , vol.5 , pp. 145-146
    • Stringer, M.A.1    Timberlake, W.E.2
  • 44
    • 0028230115 scopus 로고
    • Virus-associated down-regulation of the gene encoding cryparin, an abundant cell-surface protein from the chestnut blight fungus, Cryphonectria parasitica
    • Zhang L., Villalon D., Sun Y., Kazmierczak P., van Alfen N. K. Virus-associated down-regulation of the gene encoding cryparin, an abundant cell-surface protein from the chestnut blight fungus, Cryphonectria parasitica. Gene. 139:1994;59-64.
    • (1994) Gene , vol.139 , pp. 59-64
    • Zhang, L.1    Villalon, D.2    Sun, Y.3    Kazmierczak, P.4    Van Alfen, N.K.5
  • 45
    • 0030053545 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of the Trichoderma reesei hydrophobin HFBI
    • Nakari-Setälä T., Aro N., Kalkkinen N., Alatalo E., Penttila M. Genetic and biochemical characterization of the Trichoderma reesei hydrophobin HFBI. Eur. J. Biochem. 235:1996;248-255.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 248-255
    • Nakari-Setälä, T.1    Aro, N.2    Kalkkinen, N.3    Alatalo, E.4    Penttila, M.5


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