메뉴 건너뛰기




Volumn 404, Issue , 1996, Pages 547-555

Saponin detoxification by plant pathogenic fungi

Author keywords

[No Author keywords available]

Indexed keywords

SAPONIN; TOMATINE;

EID: 0030479329     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4899-1367-8_45     Document Type: Conference Paper
Times cited : (15)

References (44)
  • 2
    • 0025931138 scopus 로고
    • Triterpenoid saponins discovered between 1987 and 1989
    • S.B. Mahato and A.K. Nandy, Triterpenoid saponins discovered between 1987 and 1989, Phytochemistry 30:1357 (1991).
    • (1991) Phytochemistry , vol.30 , pp. 1357
    • Mahato, S.B.1    Nandy, A.K.2
  • 4
    • 0023064090 scopus 로고
    • The chemistry and biological significance of saponins in food and feedingstuffs
    • K.R. Price, I.T. Johnson, and G.R. Fenwick, The chemistry and biological significance of saponins in food and feedingstuffs, CRC Crit. Rev. Food Sci. Nutr. 26:27 (1987).
    • (1987) CRC Crit. Rev. Food Sci. Nutr. , vol.26 , pp. 27
    • Price, K.R.1    Johnson, I.T.2    Fenwick, G.R.3
  • 5
    • 0001959521 scopus 로고
    • Saponins
    • J.P. D'Mello, C.M. Duffus, and J.H. Duffus, eds., The Royal Society of Cambridge, Cambridge
    • G.R. Fenwick, K.R. Price, C. Tsukamota, and K. Okubo, Saponins, in: Toxic Substances in Crop Plants, J.P. D'Mello, C.M. Duffus, and J.H. Duffus, eds., The Royal Society of Cambridge, Cambridge, pp. 285-327, (1992).
    • (1992) Toxic Substances in Crop Plants , pp. 285-327
    • Fenwick, G.R.1    Price, K.R.2    Tsukamota, C.3    Okubo, K.4
  • 6
    • 0002440522 scopus 로고
    • Preformed substances as plant protectants
    • R. Heitefuss and P.H. Williams, eds., Springer-Verlag, Berlin
    • F. Schönbeck and E. Schlösser, Preformed substances as plant protectants, in: Physiological Plant Pathology, R. Heitefuss and P.H. Williams, eds., Springer-Verlag, Berlin, pp. 653-678 (1976).
    • (1976) Physiological Plant Pathology , pp. 653-678
    • Schönbeck, F.1    Schlösser, E.2
  • 7
    • 0000334309 scopus 로고
    • Two classes of plant antibiotics: Phytoalexins versus "phytoanticipins"
    • H.D. VanEtten, J.W. Mansfield, J.A. Bailey, and E.E. Farmer, Two classes of plant antibiotics: phytoalexins versus "phytoanticipins", The Plant Cell 9:1191 (1994).
    • (1994) The Plant Cell , vol.9 , pp. 1191
    • VanEtten, H.D.1    Mansfield, J.W.2    Bailey, J.A.3    Farmer, E.E.4
  • 8
    • 0000368099 scopus 로고
    • Production of tomatine and rishitin in tomato plants inoculated with Fusarium oxysporum f.sp. lycopersici
    • D.J. McCance and R.B. Drysdale, Production of tomatine and rishitin in tomato plants inoculated with Fusarium oxysporum f.sp. lycopersici, Physiol. Mol. Plant Pathol. 7:221 (1975).
    • (1975) Physiol. Mol. Plant Pathol. , vol.7 , pp. 221
    • McCance, D.J.1    Drysdale, R.B.2
  • 9
    • 0001313896 scopus 로고
    • Synthesis and metabolism of α-tomatine in tomato isolines in relation to resistance to Verticillium albo-atrum
    • G.F.
    • G.F. Pegg, G.F. and S. Woodward, Synthesis and metabolism of α-tomatine in tomato isolines in relation to resistance to Verticillium albo-atrum, Physiol. Mol. Plant. Pathol. 28:187 (1986).
    • (1986) Physiol. Mol. Plant. Pathol. , vol.28 , pp. 187
    • Pegg, G.F.1    Woodward, S.2
  • 10
    • 37049041816 scopus 로고
    • Action of saponin on biological membranes
    • A.D. Bangham, and R.W. Home, Action of saponin on biological membranes, Nature, 196:952 (1962).
    • (1962) Nature , vol.196 , pp. 952
    • Bangham, A.D.1    Home, R.W.2
  • 11
    • 0000840869 scopus 로고
    • Electron microscopic observations on Rous sarcoma virus and cell membranes
    • R.R. Dourmaskin, R.M. Dougherty, and R.J.C. Harris, Electron microscopic observations on Rous sarcoma virus and cell membranes, Nature 194:1116 (1962).
    • (1962) Nature , vol.194 , pp. 1116
    • Dourmaskin, R.R.1    Dougherty, R.M.2    Harris, R.J.C.3
  • 12
    • 0001480421 scopus 로고
    • Destablization of liposome membranes by the steroidal glycoalkaloid α-tomatine
    • J.G. Roddick, and R.B. Drysdale, Destablization of liposome membranes by the steroidal glycoalkaloid α-tomatine, Phytochemistry 23:543 (1984).
    • (1984) Phytochemistry , vol.23 , pp. 543
    • Roddick, J.G.1    Drysdale, R.B.2
  • 13
    • 0000044342 scopus 로고
    • Electrolyte leakage from plant and fungal tissues and disruption of liposome membranes by α-tomatine
    • C.C. Steel and R.B. Drysdale, Electrolyte leakage from plant and fungal tissues and disruption of liposome membranes by α-tomatine, Phytochemistry 27:1025 (1988).
    • (1988) Phytochemistry , vol.27 , pp. 1025
    • Steel, C.C.1    Drysdale, R.B.2
  • 14
    • 0345583195 scopus 로고
    • Role of saponins in antifungal resistance V. Enzymatic activation of avenacosides
    • H.U. Lüning and E. Schlösser, Role of saponins in antifungal resistance V. Enzymatic activation of avenacosides, Z. Pflanzenkrankh. Pflanzenschutz 82:699 (1975).
    • (1975) Z. Pflanzenkrankh. Pflanzenschutz , vol.82 , pp. 699
    • Lüning, H.U.1    Schlösser, E.2
  • 15
    • 0017404401 scopus 로고
    • Desgluco-avenacosid-A und -B, biologisch aktive Nuatigeninglycoside
    • R. Tschesche and W. Wiemann, Desgluco-avenacosid-A und -B, biologisch aktive Nuatigeninglycoside, Chem. Ber. 110:2416 (1977).
    • (1977) Chem. Ber. , vol.110 , pp. 2416
    • Tschesche, R.1    Wiemann, W.2
  • 16
    • 0000449964 scopus 로고
    • The stromacentre in Avena plastids and aggregation of β-glucosidase responsible for the activation of oat-leaf saponins
    • A. Nisius, The stromacentre in Avena plastids and aggregation of β-glucosidase responsible for the activation of oat-leaf saponins, Planta 173:474 (1988).
    • (1988) Planta , vol.173 , pp. 474
    • Nisius, A.1
  • 17
    • 0028535437 scopus 로고
    • Avenacosidase from oat: Purification, sequence analysis and biochemical characterisation of a new member of the BGA family of β-glucosidases
    • S. Gus-Mayer, H. Brunner, H.A.W. Schneider-Poetsch, and W. Rüdiger, Avenacosidase from oat: purification, sequence analysis and biochemical characterisation of a new member of the BGA family of β-glucosidases, Plant Mol. Biol. 26:909 (1994).
    • (1994) Plant Mol. Biol. , vol.26 , pp. 909
    • Gus-Mayer, S.1    Brunner, H.2    Schneider-Poetsch, H.A.W.3    Rüdiger, W.4
  • 18
    • 0028307973 scopus 로고
    • The amino acid sequence previously attributed to a protein kinase or a TCP1-related molecular chaperone and co-purified with phytochrome is a β-glucosidase
    • S. Gus-Mayer, H. Brunner, H.A.W. Schneider-Poetsch, F. Lottspeich, C. Eckerskorn, R. Grimm, and W. Rüdiger, The amino acid sequence previously attributed to a protein kinase or a TCP1-related molecular chaperone and co-purified with phytochrome is a β-glucosidase, FEBS Letts. 347:51 (1994).
    • (1994) FEBS Letts. , vol.347 , pp. 51
    • Gus-Mayer, S.1    Brunner, H.2    Schneider-Poetsch, H.A.W.3    Lottspeich, F.4    Eckerskorn, C.5    Grimm, R.6    Rüdiger, W.7
  • 19
    • 0001751010 scopus 로고
    • Role of saponins in antifungal resistance. III. Tomatin dependant development of fruit rot organisms on tomato fruits
    • E. Schlösser, Role of saponins in antifungal resistance. III. Tomatin dependant development of fruit rot organisms on tomato fruits, Z. Pflanzenkrankh. Pflanzenschutz 82:476 (1975).
    • (1975) Z. Pflanzenkrankh. Pflanzenschutz , vol.82 , pp. 476
    • Schlösser, E.1
  • 20
    • 0001062111 scopus 로고
    • The sensitivity of fungi to α-tomatine
    • P.A. Arneson and R.D. Durbin, The sensitivity of fungi to α-tomatine, Phytopathology 58:536 (1968).
    • (1968) Phytopathology , vol.58 , pp. 536
    • Arneson, P.A.1    Durbin, R.D.2
  • 22
    • 0001643814 scopus 로고
    • An enzymic basis for pathogen specificity in Ophiobolus graminis
    • E.M. Turner, An enzymic basis for pathogen specificity in Ophiobolus graminis, J. Exp. Bot. 12:169 (1961).
    • (1961) J. Exp. Bot. , vol.12 , pp. 169
    • Turner, E.M.1
  • 23
    • 0000895221 scopus 로고
    • Pathogenicity of take-all fungus to oats: Its relationship to the concentration and detoxification of the four avenacins
    • W.M.L. Crombie, L. Crombie, J.B. Green, and J.A. Lucas, Pathogenicity of take-all fungus to oats: its relationship to the concentration and detoxification of the four avenacins, Phytochemistry 25:2075 (1986).
    • (1986) Phytochemistry , vol.25 , pp. 2075
    • Crombie, W.M.L.1    Crombie, L.2    Green, J.B.3    Lucas, J.A.4
  • 24
    • 0001038858 scopus 로고
    • Partial characterization of avenacinase from Gaeumannomyces graminis var. avenae
    • J.M., and M.J. Daniels
    • A.E. Osbourn, B.R. Clarke, J.M. Dow, J.M., and M.J. Daniels, Partial characterization of avenacinase from Gaeumannomyces graminis var. avenae, Physiol. Mol. Plant Pathol. 38:301 (1991).
    • (1991) Physiol. Mol. Plant Pathol. , vol.38 , pp. 301
    • Osbourn, A.E.1    Clarke, B.R.2    Dow, J.M.3
  • 25
    • 0028946960 scopus 로고
    • Host range of a plant pathogenic fungus determined by a saponin detoxifying enzyme
    • P. Bowyer, B.R. Clarke, P. Lunness, M.J. Daniels, and A.E. Osbourn, Host range of a plant pathogenic fungus determined by a saponin detoxifying enzyme, Science 267:371 (1995).
    • (1995) Science , vol.267 , pp. 371
    • Bowyer, P.1    Clarke, B.R.2    Lunness, P.3    Daniels, M.J.4    Osbourn, A.E.5
  • 26
    • 0014696180 scopus 로고
    • Purification and properties of a fungal β-glucosidase acting on α-tomatine
    • R.D. Durbin and J.F. Uchytil, Purification and properties of a fungal β-glucosidase acting on α-tomatine, Biochim. Biophys. Acta 191:176 (1969).
    • (1969) Biochim. Biophys. Acta , vol.191 , pp. 176
    • Durbin, R.D.1    Uchytil, J.F.2
  • 27
    • 0000692447 scopus 로고
    • The detoxification of α-tomatine by Fusarium oxysporum f.sp. lycopersici
    • J.E. Ford, D.J. McCance, and R.B. Drysdale, The detoxification of α-tomatine by Fusarium oxysporum f.sp. lycopersici, Phytochemistry 16:545 (1977).
    • (1977) Phytochemistry , vol.16 , pp. 545
    • Ford, J.E.1    McCance, D.J.2    Drysdale, R.B.3
  • 28
    • 85025059841 scopus 로고
    • Toxicity of tomatine to Botrytis cinerea, in relation to latency
    • K. Verhoeff and J.I. Liem, Toxicity of tomatine to Botrytis cinerea, in relation to latency, Phytopath. Z. 82:333 (1975).
    • (1975) Phytopath. Z. , vol.82 , pp. 333
    • Verhoeff, K.1    Liem, J.I.2
  • 29
    • 37049095446 scopus 로고
    • Isolation of avenacins A-1, A-2, B-1 and B-2 from oat roots: Structures of their aglycones, the avenestergenins
    • L. Crombie, W.M.L. Crombie, and D.A. Whiting, Isolation of avenacins A-1, A-2, B-1 and B-2 from oat roots: structures of their aglycones, the avenestergenins, J. Chem. Soc., Chem. Commun. 244:246 (1984).
    • (1984) J. Chem. Soc., Chem. Commun. , vol.244 , pp. 246
    • Crombie, L.1    Crombie, W.M.L.2    Whiting, D.A.3
  • 30
    • 0001483321 scopus 로고
    • Structures of the oat root resistance factors to take-all disease, avenacins A-1, A-2, B-1 and B-2 and their companion substances
    • L. Crombie, W.M.L. Crombie, and D.A. Whiting, Structures of the oat root resistance factors to take-all disease, avenacins A-1, A-2, B-1 and B-2 and their companion substances, J. Chem. Soc. Perkin Trans. I: 1917 (1986).
    • (1986) J. Chem. Soc. Perkin Trans. I , pp. 1917
    • Crombie, L.1    Crombie, W.M.L.2    Whiting, D.A.3
  • 31
    • 0000069890 scopus 로고
    • Distribution of the avenacins A-1, A-2, B-1 and B-2 in oat roots: Their fungicidal activity towards take-all fungus
    • W.M.L. Crombie and L. Crombie, Distribution of the avenacins A-1, A-2, B-1 and B-2 in oat roots: their fungicidal activity towards take-all fungus, Phytochemistry 25:2069 (1986).
    • (1986) Phytochemistry , vol.25 , pp. 2069
    • Crombie, W.M.L.1    Crombie, L.2
  • 32
    • 0009265958 scopus 로고
    • The nature of the resistance of oats to the take-all fungus. III. Distribution of the inhibitor in oat seeedlings
    • E.M. Turner, The nature of the resistance of oats to the take-all fungus. III. Distribution of the inhibitor in oat seeedlings, J. Exp. Bot. 11:403 (1960).
    • (1960) J. Exp. Bot. , vol.11 , pp. 403
    • Turner, E.M.1
  • 33
    • 0000241187 scopus 로고
    • Studies on roots. I. Properties and distribution of fluorescent constituents in Avena roots
    • R.H. Goodwin and B.M. Pollock, Studies on roots. I. Properties and distribution of fluorescent constituents in Avena roots, Am. J. Bot. 4:516 (1954).
    • (1954) Am. J. Bot. , vol.4 , pp. 516
    • Goodwin, R.H.1    Pollock, B.M.2
  • 34
    • 0028251295 scopus 로고
    • An oat species lacking avenacin is susceptible to infection by Gaeumannomyces graminis var. tritici
    • A.E. Osbourn, B.R. Clarke, P. Lunness, P.R. Scott and M.J. Daniels, An oat species lacking avenacin is susceptible to infection by Gaeumannomyces graminis var. tritici, Physiol. Mol. Plant Pathol. 45:457 (1994).
    • (1994) Physiol. Mol. Plant Pathol. , vol.45 , pp. 457
    • Osbourn, A.E.1    Clarke, B.R.2    Lunness, P.3    Scott, P.R.4    Daniels, M.J.5
  • 35
    • 0002679958 scopus 로고
    • Avenacin, an antimicrobial substance isolated from Avena saliva
    • J.V. Maizel, H.J. Burkhardt, and H.K. Mitchell, Avenacin, an antimicrobial substance isolated from Avena saliva, Biochemistry 3:424 (1964).
    • (1964) Biochemistry , vol.3 , pp. 424
    • Maizel, J.V.1    Burkhardt, H.J.2    Mitchell, H.K.3
  • 38
    • 0005932633 scopus 로고
    • Transformation of Gaeumannomyces graminis to benomyl resistance
    • J.M. Henson, N.K. Blake, and A.L. Pilgeram, Transformation of Gaeumannomyces graminis to benomyl resistance, Curr. Genet. 14:113 (1988).
    • (1988) Curr. Genet. , vol.14 , pp. 113
    • Henson, J.M.1    Blake, N.K.2    Pilgeram, A.L.3
  • 39
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • B. Henrissat, A classification of glycosyl hydrolases based on amino acid sequence similarities, Biochem. J. 280:309 (1991).
    • (1991) Biochem. J. , vol.280 , pp. 309
    • Henrissat, B.1
  • 40
    • 14744272350 scopus 로고
    • Cloning and amplification of the gene encoding an extracellular β-glucosidase from Trichoderma reesei: Evidence for improved rates of saccharification of cellulosic substrates
    • C.C. Barnett, R.M. Berka, and T. Fowler, Cloning and amplification of the gene encoding an extracellular β-glucosidase from Trichoderma reesei: evidence for improved rates of saccharification of cellulosic substrates, Bio/Technology 9:562 (1991).
    • (1991) Bio/Technology , vol.9 , pp. 562
    • Barnett, C.C.1    Berka, R.M.2    Fowler, T.3
  • 41
    • 0024254393 scopus 로고
    • Nucleotide sequence of Saccharomycopsis fibuligera genes for extracellular β-glucosidases as expressed in Saccharomyces cerevisiae
    • M. Machida, I. Ohtsuki, S. Fukui, and I. Yamashita, Nucleotide sequence of Saccharomycopsis fibuligera genes for extracellular β-glucosidases as expressed in Saccharomyces cerevisiae, Appl. Env. Microbiol. 54:3147 (1988).
    • (1988) Appl. Env. Microbiol. , vol.54 , pp. 3147
    • Machida, M.1    Ohtsuki, I.2    Fukui, S.3    Yamashita, I.4
  • 42
    • 0022423552 scopus 로고
    • Nucleotide sequence of Candida pelliculosa β-glucosidase gene
    • C. Kohchi and A. Toh-e, Nucleotide sequence of Candida pelliculosa β-glucosidase gene, Nucleic Acids Res. 13:6273 (1985).
    • (1985) Nucleic Acids Res. , vol.13 , pp. 6273
    • Kohchi, C.1    Toh-e, A.2
  • 43
    • 0019270823 scopus 로고
    • Isolation and structure of a tryptic glycopeptide from the active site of β-glucosidase A3 from Aspergillus wentii
    • E. Bause and G. Legler, Isolation and structure of a tryptic glycopeptide from the active site of β-glucosidase A3 from Aspergillus wentii, Biochim. Biophys. Acta 626:459 (1980).
    • (1980) Biochim. Biophys. Acta , vol.626 , pp. 459
    • Bause, E.1    Legler, G.2
  • 44
    • 0014288718 scopus 로고
    • Studies on the mode of action of tomatine as a fungitoxic agent
    • P.A. Arneson and R.D. Durbin, Studies on the mode of action of tomatine as a fungitoxic agent, Plant Physiol. 1968, 43, 683-686.
    • (1968) Plant Physiol. , vol.43 , pp. 683-686
    • Arneson, P.A.1    Durbin, R.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.