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Volumn 235, Issue 1-2, 1999, Pages 121-129

Fungal proteinase expression in the interaction of the plant pathogen Magnaporthe poae with its host

Author keywords

Subtilisin

Indexed keywords

FUNGAL PROTEIN; PROTEINASE; SUBTILISIN;

EID: 0032788654     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(99)00201-2     Document Type: Article
Times cited : (59)

References (41)
  • 1
    • 0018144557 scopus 로고
    • Phenylboronic acid as a ligand for biospecific chromatography of serine proteinases
    • Akparov V.H., Stepanov V.M. Phenylboronic acid as a ligand for biospecific chromatography of serine proteinases. J. Chromatogr. 155:1978;329-336.
    • (1978) J. Chromatogr. , vol.155 , pp. 329-336
    • Akparov, V.H.1    Stepanov, V.M.2
  • 3
    • 0001642662 scopus 로고
    • Evidence for the requirement of extracellular protease in the pathogenic interaction of Pyrenopeziza brassicae with oilseed rape
    • Ball A.M., Ashby A.M., Daniels M.J., Ingram D.S., Johnstone K. Evidence for the requirement of extracellular protease in the pathogenic interaction of Pyrenopeziza brassicae with oilseed rape. Physiol. Mol. Plant Pathol. 38:1991;147-161.
    • (1991) Physiol. Mol. Plant Pathol. , vol.38 , pp. 147-161
    • Ball, A.M.1    Ashby, A.M.2    Daniels, M.J.3    Ingram, D.S.4    Johnstone, K.5
  • 4
    • 0025092644 scopus 로고
    • Identification of Beauveria bassiana extracellular protease as a virulence factor in pathogenicity toward the migratory grasshopper, Melanoplus sanguinipes
    • Bidochka M.J., Khachatourians G.G. Identification of Beauveria bassiana extracellular protease as a virulence factor in pathogenicity toward the migratory grasshopper, Melanoplus sanguinipes. J. Invertebr. Pathol. 56:1990;362-370.
    • (1990) J. Invertebr. Pathol. , vol.56 , pp. 362-370
    • Bidochka, M.J.1    Khachatourians, G.G.2
  • 5
    • 0029053258 scopus 로고
    • A basic serine protease from Paecilomyces lilacinus with biological activity against Meloidogyne hapla eggs
    • Bonants P.J.M., Fitters P.F.L., Thijs H., den Belder E., Waalwijk C., Henfling J.W.D.M. A basic serine protease from Paecilomyces lilacinus with biological activity against Meloidogyne hapla eggs. Microbiology. 141:1995;775-784.
    • (1995) Microbiology , vol.141 , pp. 775-784
    • Bonants, P.J.M.1    Fitters, P.F.L.2    Thijs, H.3    Den Belder, E.4    Waalwijk, C.5    Henfling, J.W.D.M.6
  • 6
    • 0019363396 scopus 로고
    • Organization and expression of eucaryotic split genes coding for proteins
    • Breathnach R., Chambon P. Organization and expression of eucaryotic split genes coding for proteins. Annu. Rev. Biochem. 50:1981;349-383.
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 349-383
    • Breathnach, R.1    Chambon, P.2
  • 7
    • 0000565575 scopus 로고    scopus 로고
    • Identification of Magnaporthe poae by PCR and examination of its relationship to other fungi by analysis of their nuclear rDNA ITS-1 regions
    • Bunting T.E., Plumley K.A., Clarke B.B., Hillman B.I. Identification of Magnaporthe poae by PCR and examination of its relationship to other fungi by analysis of their nuclear rDNA ITS-1 regions. Phytopathology. 86:1996;398-404.
    • (1996) Phytopathology , vol.86 , pp. 398-404
    • Bunting, T.E.1    Plumley, K.A.2    Clarke, B.B.3    Hillman, B.I.4
  • 8
    • 0027351945 scopus 로고
    • Structural models of primary cell walls in flowering plants: Consistency of molecular structure with the physical properties of the walls during growth
    • Carpita N.C., Gibeaut D.M. Structural models of primary cell walls in flowering plants: consistency of molecular structure with the physical properties of the walls during growth. Plant J. 3:1993;1-30.
    • (1993) Plant J. , vol.3 , pp. 1-30
    • Carpita, N.C.1    Gibeaut, D.M.2
  • 9
    • 0028534966 scopus 로고
    • Arabidopsis thaliana expresses three divergent Srp54 genes
    • Chu B., Lindstrom J.T., Belanger F.C. Arabidopsis thaliana expresses three divergent Srp54 genes. Plant Physiol. 106:1994;1157-1162.
    • (1994) Plant Physiol. , vol.106 , pp. 1157-1162
    • Chu, B.1    Lindstrom, J.T.2    Belanger, F.C.3
  • 12
    • 0000220264 scopus 로고
    • Ultrastructural localization of a cuticle degrading protease produced by the entomopathogenic fungus Metarhizium anisopliae during penetration of host (Manduca sexta) cuticle
    • Goettel M.S., St. Leger R.J., Rizzo N.W., Staples R.C., Roberts D.W. Ultrastructural localization of a cuticle degrading protease produced by the entomopathogenic fungus Metarhizium anisopliae during penetration of host (Manduca sexta) cuticle. Gen. Microbiol. 135:1989;2233-2239.
    • (1989) Gen. Microbiol. , vol.135 , pp. 2233-2239
    • Goettel, M.S.1    St. Leger, R.J.2    Rizzo, N.W.3    Staples, R.C.4    Roberts, D.W.5
  • 13
    • 0019258624 scopus 로고
    • Elution of proteins from sodium dodecyl sulfate-polyacrylamide gels, removal of sodium dodecyl sulfate, and renaturation of enzymatic activity: Results with sigma subunit of Escherichia coli RNA polymerase, wheat germ DNA topoisomerase, and other enzymes
    • Hager D.A., Burgess R.B. Elution of proteins from sodium dodecyl sulfate-polyacrylamide gels, removal of sodium dodecyl sulfate, and renaturation of enzymatic activity: results with sigma subunit of Escherichia coli RNA polymerase, wheat germ DNA topoisomerase, and other enzymes. Anal. Biochem. 109:1980;76-86.
    • (1980) Anal. Biochem. , vol.109 , pp. 76-86
    • Hager, D.A.1    Burgess, R.B.2
  • 14
    • 0019951316 scopus 로고
    • An acid protease produced by Monilinia fructigena in vitro and in infected apple fruits, and its possible role in pathogenesis
    • Hislop E.C., Paver J.L., Keon J.P.R. An acid protease produced by Monilinia fructigena in vitro and in infected apple fruits, and its possible role in pathogenesis. J. Gen. Microbiol. 128:1982;799-807.
    • (1982) J. Gen. Microbiol. , vol.128 , pp. 799-807
    • Hislop, E.C.1    Paver, J.L.2    Keon, J.P.R.3
  • 15
    • 0342902663 scopus 로고
    • Geographic distribution, host range and symptomatology of patch diseases caused by soilborne ectotrophic fungi
    • B.B. Clarke, & A.B. Gould. St. Paul: American Phytopathological Society
    • Jackson N. Geographic distribution, host range and symptomatology of patch diseases caused by soilborne ectotrophic fungi. Clarke B.B., Gould A.B. Turfgrass Patch Diseases Caused by Ectotrophic Root-Infecting Fungi. 1993;17-39 American Phytopathological Society, St. Paul.
    • (1993) Turfgrass Patch Diseases Caused by Ectotrophic Root-Infecting Fungi , pp. 17-39
    • Jackson, N.1
  • 16
    • 0027119999 scopus 로고
    • Nucleotide sequence of a genomic and a cDNA clone encoding an extracellular alkaline protease of Aspergillus fumigatis
    • Jaton-Ogay K., Suter M., Crameri R., Falchetto R., Faith A., Monod M. Nucleotide sequence of a genomic and a cDNA clone encoding an extracellular alkaline protease of Aspergillus fumigatis. FEMS Microbiol. Lett. 92:1992;163-168.
    • (1992) FEMS Microbiol. Lett. , vol.92 , pp. 163-168
    • Jaton-Ogay, K.1    Suter, M.2    Crameri, R.3    Falchetto, R.4    Faith, A.5    Monod, M.6
  • 17
    • 0345605058 scopus 로고
    • Influence of temperature-soil water status interactions on the development of summer patch in Poa spp.
    • Kackley K.E., Grybauskas A.P., Hill R.L., Dernoeden P.H. Influence of temperature-soil water status interactions on the development of summer patch in Poa spp. Phytopathology. 80:1990;650-654.
    • (1990) Phytopathology , vol.80 , pp. 650-654
    • Kackley, K.E.1    Grybauskas, A.P.2    Hill, R.L.3    Dernoeden, P.H.4
  • 18
    • 0028980724 scopus 로고
    • Isolation of the chitinolytic bacteria Xanthomonas maltophilia and Serratia marcescens as biological control agents for summer patch disease of turfgrass
    • Kobayashi D.Y., Guglielmoni M., Clarke B.B. Isolation of the chitinolytic bacteria Xanthomonas maltophilia and Serratia marcescens as biological control agents for summer patch disease of turfgrass. Soil Biol. Biochem. 27:1995;1479-1487.
    • (1995) Soil Biol. Biochem. , vol.27 , pp. 1479-1487
    • Kobayashi, D.Y.1    Guglielmoni, M.2    Clarke, B.B.3
  • 19
    • 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
  • 20
    • 85011112888 scopus 로고
    • Magnaporthe poae sp. nov., a hyphopodiate fungus with a Phialophora conidial state, from grass roots in the United States
    • Landschoot P.J., Jackson N. Magnaporthe poae sp. nov., a hyphopodiate fungus with a Phialophora conidial state, from grass roots in the United States. Mycol. Res. 93:1989;59-62.
    • (1989) Mycol. Res. , vol.93 , pp. 59-62
    • Landschoot, P.J.1    Jackson, N.2
  • 21
    • 0345098889 scopus 로고
    • Ecology and epidemiology of ectotrophic root-infecting fungi associated with patch diseases of turfgrasses
    • B.B. Clarke, & A.B. Gould. St. Paul: American Phytopathological Society
    • Landschoot P.J., Gould A.B., Clarke B.B. Ecology and epidemiology of ectotrophic root-infecting fungi associated with patch diseases of turfgrasses. Clarke B.B., Gould A.B. Turfgrass Patch Diseases Caused by Ectotrophic Root-Infecting Fungi. 1993;73-105 American Phytopathological Society, St. Paul.
    • (1993) Turfgrass Patch Diseases Caused by Ectotrophic Root-Infecting Fungi , pp. 73-105
    • Landschoot, P.J.1    Gould, A.B.2    Clarke, B.B.3
  • 22
    • 0028002354 scopus 로고
    • Purification and characterization of an endophytic fungal proteinase that is abundantly expressed in the infected host grass
    • Lindstrom J.T., Belanger F.C. Purification and characterization of an endophytic fungal proteinase that is abundantly expressed in the infected host grass. Plant Physiol. 106:1994;7-16.
    • (1994) Plant Physiol. , vol.106 , pp. 7-16
    • Lindstrom, J.T.1    Belanger, F.C.2
  • 23
    • 0000822516 scopus 로고
    • A novel fungal protease expressed in endophytic infection of Poa species
    • Lindstrom J.T., Sun S., Belanger F.C. A novel fungal protease expressed in endophytic infection of Poa species. Plant Physiol. 102:1993;645-650.
    • (1993) Plant Physiol. , vol.102 , pp. 645-650
    • Lindstrom, J.T.1    Sun, S.2    Belanger, F.C.3
  • 25
    • 0030136788 scopus 로고    scopus 로고
    • Three extracellular proteases from Cochliobolus carbonum: Cloning and targeted disruption of ALP1
    • Murphy J.M., Walton J.D. Three extracellular proteases from Cochliobolus carbonum: cloning and targeted disruption of ALP1. Mol. Plant-Microbe Interact. 9:1996;290-297.
    • (1996) Mol. Plant-Microbe Interact. , vol.9 , pp. 290-297
    • Murphy, J.M.1    Walton, J.D.2
  • 26
    • 0028819455 scopus 로고
    • Molecular dissection of fungal phytopathogenicity
    • Oliver R., Osbourn A. Molecular dissection of fungal phytopathogenicity. Microbiology. 141:1995;1-9.
    • (1995) Microbiology , vol.141 , pp. 1-9
    • Oliver, R.1    Osbourn, A.2
  • 27
    • 0028144296 scopus 로고
    • Isolation, characterization, and cloning of cDNA and the gene for an elastinolytic serine proteinase from Aspergillus flavus
    • Ramesh M.V., Sirakova T., Kolattukudy P.E. Isolation, characterization, and cloning of cDNA and the gene for an elastinolytic serine proteinase from Aspergillus flavus. Infect. Immun. 62:1994;79-85.
    • (1994) Infect. Immun. , vol.62 , pp. 79-85
    • Ramesh, M.V.1    Sirakova, T.2    Kolattukudy, P.E.3
  • 29
    • 0030220480 scopus 로고    scopus 로고
    • Mutualistic fungal endophytes express a proteinase that is homologous to proteases suspected to be important in fungal pathogenicity
    • Reddy P.V., Lam C.K., Belanger F.C. Mutualistic fungal endophytes express a proteinase that is homologous to proteases suspected to be important in fungal pathogenicity. Plant Physiol. 111:1996;1209-1218.
    • (1996) Plant Physiol. , vol.111 , pp. 1209-1218
    • Reddy, P.V.1    Lam, C.K.2    Belanger, F.C.3
  • 30
    • 0022432484 scopus 로고
    • Rapid transfer of DNA from agarose gels to nylon membranes
    • Reed K.C., Mann D.A. Rapid transfer of DNA from agarose gels to nylon membranes. Nucleic Acids Res. 13:1985;7207-7221.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 7207-7221
    • Reed, K.C.1    Mann, D.A.2
  • 32
    • 0002837584 scopus 로고
    • The role of cuticle-degrading proteases in fungal pathogenesis of insects
    • St. Leger R.J. The role of cuticle-degrading proteases in fungal pathogenesis of insects. Can. J. Bot. 73:(Suppl. 1):1995;S1119-S1125.
    • (1995) Can. J. Bot. , vol.73 , Issue.SUPPL. 1
    • St. Leger, R.J.1
  • 33
    • 0023109127 scopus 로고
    • Characterization of cuticle-degrading proteases produced by the entomopathogen Metarhizium anisopliae
    • St. Leger R.J., Charnley A.K., Cooper R.M. Characterization of cuticle-degrading proteases produced by the entomopathogen Metarhizium anisopliae. Arch. Biochem. Biophys. 253:1987;221-232.
    • (1987) Arch. Biochem. Biophys. , vol.253 , pp. 221-232
    • St. Leger, R.J.1    Charnley, A.K.2    Cooper, R.M.3
  • 34
    • 13344279428 scopus 로고    scopus 로고
    • Characterization and ultrastructural localization of chitinases from Metarhizium anisopliae, M. flavoviride, and Beauveria bassiana during fungal invasion of host (Manduca sexta) cuticle
    • St. Leger R.J., Joshi L., Bidochka M.J., Rizzo N.W., Roberts D.W. Characterization and ultrastructural localization of chitinases from Metarhizium anisopliae, M. flavoviride, and Beauveria bassiana during fungal invasion of host (Manduca sexta) cuticle. Appl. Environ. Microbiol. 62:1996;907-912.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 907-912
    • St. Leger, R.J.1    Joshi, L.2    Bidochka, M.J.3    Rizzo, N.W.4    Roberts, D.W.5
  • 35
    • 0030808167 scopus 로고    scopus 로고
    • Adaptation of proteases and carbohydrases of saprophytic, phytopathogenic and entomopathogenic fungi to the requirements of their ecological niches
    • St. Leger R.J., Joshi L., Roberts D.W. Adaptation of proteases and carbohydrases of saprophytic, phytopathogenic and entomopathogenic fungi to the requirements of their ecological niches. Microbiology. 143:1997;1983-1992.
    • (1997) Microbiology , vol.143 , pp. 1983-1992
    • St. Leger, R.J.1    Joshi, L.2    Roberts, D.W.3
  • 36
    • 0027230493 scopus 로고
    • The alkaline protease of Aspergillus fumigatus is not a virulence determinant in two murine models of invasive pulmonary aspergillosis
    • Tang C.M., Cohen J., Krausz T., Van Noorden S., Holden D.W. The alkaline protease of Aspergillus fumigatus is not a virulence determinant in two murine models of invasive pulmonary aspergillosis. Infect. Immun. 61:1993;1650-1656.
    • (1993) Infect. Immun. , vol.61 , pp. 1650-1656
    • Tang, C.M.1    Cohen, J.2    Krausz, T.3    Van Noorden, S.4    Holden, D.W.5
  • 38
    • 0026002141 scopus 로고
    • Proteases and their involvement in the infection and immobilization of nematodes by the nematophagous fungus Arthrobotrys oligospora
    • Tunlid A., Jansson S. Proteases and their involvement in the infection and immobilization of nematodes by the nematophagous fungus Arthrobotrys oligospora. Appl. Environ. Microbiol. 57:1991;2868-2872.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 2868-2872
    • Tunlid, A.1    Jansson, S.2
  • 39
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14:1986;4683-4690.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 40
    • 0028007674 scopus 로고
    • Deconstructing the cell wall
    • Walton J.D. Deconstructing the cell wall. Plant Physiol. 104:1994;1113-1118.
    • (1994) Plant Physiol. , vol.104 , pp. 1113-1118
    • Walton, J.D.1
  • 41
    • 0038320648 scopus 로고
    • Antiserum prepared with acrylamide gel used as adjuvant
    • Weintraub M., Raymond S. Antiserum prepared with acrylamide gel used as adjuvant. Science. 142:1963;1677-1678.
    • (1963) Science , vol.142 , pp. 1677-1678
    • Weintraub, M.1    Raymond, S.2


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