메뉴 건너뛰기




Volumn 12, Issue 5, 1999, Pages 401-409

Conductive properties and gating of channels formed by syringopeptin 25A, a bioactive lipodepsipeptide from Pseudomonas syringae pv. syringae, in planar lipid membranes

Author keywords

Selectivity

Indexed keywords

BACTERIAL TOXIN; PATHOGENESIS; SYRINGOPEPTIN;

EID: 0033135752     PISSN: 08940282     EISSN: None     Source Type: Journal    
DOI: 10.1094/mpmi.1999.12.5.401     Document Type: Article
Times cited : (31)

References (56)
  • 6
    • 0001765867 scopus 로고
    • Bacterial blotch disease of the cultivated mushroom is caused by an ion channel forming lipodepsipeptide toxin
    • Brodey, C. L., Rainey, P. B., Tester, M., and Johnstone, K. 1991. Bacterial blotch disease of the cultivated mushroom is caused by an ion channel forming lipodepsipeptide toxin. Mol. Plant-Microbe Interact. 4:407-411.
    • (1991) Mol. Plant-microbe Interact. , vol.4 , pp. 407-411
    • Brodey, C.L.1    Rainey, P.B.2    Tester, M.3    Johnstone, K.4
  • 7
    • 0026024029 scopus 로고
    • Modification of lysine residues of s. Aureus α-toxin: Effects on its channel forming properties
    • Cescatti, L., Pederzolli, C., and Menestrina, G. 1991. Modification of lysine residues of S. aureus α-toxin: Effects on its channel forming properties. J. Membr. Biol. 119:53-64.
    • (1991) J. Membr. Biol. , vol.119 , pp. 53-64
    • Cescatti, L.1    Pederzolli, C.2    Menestrina, G.3
  • 8
    • 0017743694 scopus 로고
    • Relaxation and fluctuations of membrane currents that flow through drug-operated ion channels
    • Colquohun, D., and Hawkes, A. G. 1977. Relaxation and fluctuations of membrane currents that flow through drug-operated ion channels. Proc. R. Soc. Lond. B 199:231-262.
    • (1977) Proc. R. Soc. Lond. B , vol.199 , pp. 231-262
    • Colquohun, D.1    Hawkes, A.G.2
  • 9
    • 0033135036 scopus 로고    scopus 로고
    • The interaction of lipodepsipeptide toxins from pseudomonas syringae pv. Syringae with biological and model membranes: A comparison of syringotoxin, syringomycin, and two syringopeptins
    • Dalla Serra, M., Fagiuoli, G., Nordera, P., Bernhart, I., Della Volpe, C., Di Giorgio, D., Ballio, A., and Menestrina, G. 1999. The interaction of lipodepsipeptide toxins from Pseudomonas syringae pv. syringae with biological and model membranes: A comparison of syringotoxin, syringomycin, and two syringopeptins. Mol. Plant-Microbe Interact. 12:391-400.
    • (1999) Mol. Plant-microbe Interact. , vol.12 , pp. 391-400
    • Dalla Serra, M.1    Fagiuoli, G.2    Nordera, P.3    Bernhart, I.4    Della Volpe, C.5    Di Giorgio, D.6    Ballio, A.7    Menestrina, G.8
  • 10
    • 0021272091 scopus 로고
    • Studies on the mechanism of action of channel-forming colicins using artificial membranes
    • Davidson, V. L., Brunden, K. R., Cramer, W. A., and Cohen, F. S. 1984. Studies on the mechanism of action of channel-forming colicins using artificial membranes. J. Membr. Biol. 79:105-118.
    • (1984) J. Membr. Biol. , vol.79 , pp. 105-118
    • Davidson, V.L.1    Brunden, K.R.2    Cramer, W.A.3    Cohen, F.S.4
  • 12
    • 0001312185 scopus 로고    scopus 로고
    • Syringopeptins, Pseudomonas syringae pv. Syringae phytotoxins, resemble syringomycin in closing stomata
    • Di Giorgio, D., Camoni, L., Mott, K. A., Takemoto, J. Y., and Ballio, A. 1996a. Syringopeptins, Pseudomonas syringae pv. syringae phytotoxins, resemble syringomycin in closing stomata. Plant Pathol. 45:564-571.
    • (1996) Plant Pathol. , vol.45 , pp. 564-571
    • Di Giorgio, D.1    Camoni, L.2    Mott, K.A.3    Takemoto, J.Y.4    Ballio, A.5
  • 15
    • 0017363554 scopus 로고
    • Electrically gated ionic channels in lipid bilayers
    • Ehrenstein, G., and Lecar, H. 1977. Electrically gated ionic channels in lipid bilayers. Q. Rev. Biophys. 10:1-34.
    • (1977) Q. Rev. Biophys. , vol.10 , pp. 1-34
    • Ehrenstein, G.1    Lecar, H.2
  • 17
    • 0031054321 scopus 로고    scopus 로고
    • The effect of sterols on the sensitivity of membranes to the channel-forming antifungal antibiotic, syringomycin E
    • Feigin, A. M., Schagina, L. V., Takemoto, J. Y., Teeter, J. H., and Brand, J. G. 1997. The effect of sterols on the sensitivity of membranes to the channel-forming antifungal antibiotic, syringomycin E. Biochim. Biophys. Acta 1324:102-110.
    • (1997) Biochim. Biophys. Acta , vol.1324 , pp. 102-110
    • Feigin, A.M.1    Schagina, L.V.2    Takemoto, J.Y.3    Teeter, J.H.4    Brand, J.G.5
  • 18
    • 0030030826 scopus 로고    scopus 로고
    • Properties of voltage-gated ion channels formed by syringomycin E in planar lipid bilayers
    • Feigin, A. M., Takemoto, J. Y., Wangspa, R., Teeter, J. H., and Brand, J. G. 1996. Properties of voltage-gated ion channels formed by syringomycin E in planar lipid bilayers. J. Membr. Biol. 149:41-47.
    • (1996) J. Membr. Biol. , vol.149 , pp. 41-47
    • Feigin, A.M.1    Takemoto, J.Y.2    Wangspa, R.3    Teeter, J.H.4    Brand, J.G.5
  • 19
    • 37049071855 scopus 로고
    • Isolation and structural elucidation of syringostatins, phytotoxins produced by pseudomonas syringae pv. Syringae lilac isolate
    • Fukuchi, N., Isogai, A., Nakayama, J., Takayama, S., and Yamashita, S. 1992. Isolation and structural elucidation of syringostatins, phytotoxins produced by Pseudomonas syringae pv. syringae lilac isolate. J. Chem. Soc. Perkin Trans. 1:875-880.
    • (1992) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 875-880
    • Fukuchi, N.1    Isogai, A.2    Nakayama, J.3    Takayama, S.4    Yamashita, S.5
  • 20
    • 0025234618 scopus 로고
    • Structure of phytotoxin syringomycin produced by a sugar cane isolate of Pseudomonas syringae pv. Syringae
    • Fukuchi, N., Isogai, A., Yamashita, S., Suyama, K., Takemoto, J. Y., and Suzuki, A. 1990. Structure of phytotoxin syringomycin produced by a sugar cane isolate of Pseudomonas syringae pv. syringae. Tetrahedron Lett. 31:1589-1592.
    • (1990) Tetrahedron Lett. , vol.31 , pp. 1589-1592
    • Fukuchi, N.1    Isogai, A.2    Yamashita, S.3    Suyama, K.4    Takemoto, J.Y.5    Suzuki, A.6
  • 22
    • 0345570658 scopus 로고
    • Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: Relevance to translocation of proteins across membranes
    • Hoch, D. H., Romero-Mira, M., Ehrlich, B. E., Finkelstein, A., Das-Gupta, B. R., and Simpson, L. L. 1985. Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: Relevance to translocation of proteins across membranes. Proc. Natl. Acad. Sci. USA 82:1692-1696.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1692-1696
    • Hoch, D.H.1    Romero-Mira, M.2    Ehrlich, B.E.3    Finkelstein, A.4    Das-Gupta, B.R.5    Simpson, L.L.6
  • 23
    • 0031127790 scopus 로고    scopus 로고
    • Lipopeptide phytotoxins produced by pseudomonas syringae pv. Syringae: Comparison of the biosurfactant and ion channel-forming activities of syringopeptin and syringomycin
    • Hutchison, M. L., and Gross, D. C. 1997. Lipopeptide phytotoxins produced by Pseudomonas syringae pv. syringae: Comparison of the biosurfactant and ion channel-forming activities of syringopeptin and syringomycin. Mol. Plant-Microbe Interact. 10:347-354.
    • (1997) Mol. Plant-microbe Interact. , vol.10 , pp. 347-354
    • Hutchison, M.L.1    Gross, D.C.2
  • 24
    • 0029328261 scopus 로고
    • Role of biosurfactant and ion channel-forming activities of syringomycin in transmembrane ion flux: A model for the mechanism of action in the plantpathogen interaction
    • Hutchison, M. L., Tester, M. A., and Gross, D. C. 1995. Role of biosurfactant and ion channel-forming activities of syringomycin in transmembrane ion flux: A model for the mechanism of action in the plantpathogen interaction. Mol. Plant-Microbe Interact. 8:610-620.
    • (1995) Mol. Plant-microbe Interact. , vol.8 , pp. 610-620
    • Hutchison, M.L.1    Tester, M.A.2    Gross, D.C.3
  • 26
    • 0005063966 scopus 로고
    • Syringostatins, novel phytotoxins produced by Pseudomonas syringae pv. Syringae
    • Isogai, A., Fukuchi, N., Yamashita, S., Suyama, K., and Suzuki, A. 1990a. Syringostatins, novel phytotoxins produced by Pseudomonas syringae pv. syringae. Agric. Biol. Chem. 53:3117-3119.
    • (1990) Agric. Biol. Chem. , vol.53 , pp. 3117-3119
    • Isogai, A.1    Fukuchi, N.2    Yamashita, S.3    Suyama, K.4    Suzuki, A.5
  • 27
    • 0025125761 scopus 로고
    • Structures of syringostatins A and B, novel phytotoxins produced by Pseudomonas syringae pv. Syringae isolated from lilac blights
    • Isogai, A., Fukuchi, N., Yamashita, S., Suyama, K., and Suzuki, A. 1990b. Structures of syringostatins A and B, novel phytotoxins produced by Pseudomonas syringae pv. syringae isolated from lilac blights. Tetrahedron Lett. 31:695-698.
    • (1990) Tetrahedron Lett. , vol.31 , pp. 695-698
    • Isogai, A.1    Fukuchi, N.2    Yamashita, S.3    Suyama, K.4    Suzuki, A.5
  • 29
    • 0345347820 scopus 로고    scopus 로고
    • Use of lipid bilayer membranes to detect pore formation by toxins
    • V. L. Clark and P. M. Bavoil, eds. Academic Press, San Diego, CA.
    • Kagan, B. L., and Sokolov, Y. 1997. Use of lipid bilayer membranes to detect pore formation by toxins. Pages 395-409 in: Bacterial Pathogenesis. V. L. Clark and P. M. Bavoil, eds. Academic Press, San Diego, CA.
    • (1997) Bacterial Pathogenesis , pp. 395-409
    • Kagan, B.L.1    Sokolov, Y.2
  • 32
    • 0028258799 scopus 로고
    • Iturins, a special class of pore-forming lipopeptides: Biological and physicochemical properties
    • Maget-Dana, R., and Peypoux, F. 1994. Iturins, a special class of pore-forming lipopeptides: Biological and physicochemical properties. Toxicology 87:151-174.
    • (1994) Toxicology , vol.87 , pp. 151-174
    • Maget-Dana, R.1    Peypoux, F.2
  • 33
    • 0025361221 scopus 로고
    • Iturin lipopeptides: Interaction of mycosubtilin with lipids in planar membranes and mixed monolayers
    • Maget-Dana, R., and Ptak, M. 1990. Iturin lipopeptides: Interaction of mycosubtilin with lipids in planar membranes and mixed monolayers. Biochim. Biophys. Acta 1023:34-40.
    • (1990) Biochim. Biophys. Acta , vol.1023 , pp. 34-40
    • Maget-Dana, R.1    Ptak, M.2
  • 34
    • 0028918703 scopus 로고
    • Interactions of surfactins with membrane models
    • Maget-Dana, R., and Ptak, M. 1995. Interactions of surfactins with membrane models. Biophys. J. 68:1937-1943.
    • (1995) Biophys. J. , vol.68 , pp. 1937-1943
    • Maget-Dana, R.1    Ptak, M.2
  • 35
    • 0021813091 scopus 로고
    • Pore-forming properties of iturin A, a lipopeptide antibiotic
    • Maget-Dana, R., Ptak, M., Peypoux, F., and Michel, G. 1985b. Pore-forming properties of iturin A, a lipopeptide antibiotic. Biochim. Biophys. Acta 815:405-409.
    • (1985) Biochim. Biophys. Acta , vol.815 , pp. 405-409
    • Maget-Dana, R.1    Ptak, M.2    Peypoux, F.3    Michel, G.4
  • 37
    • 0022504362 scopus 로고
    • Ionic channels formed by Staphylococcus aureus alpha-toxin: Voltage dependent inhibition by di- and trivalent cations
    • Menestrina, G. 1986. Ionic channels formed by Staphylococcus aureus alpha-toxin: Voltage dependent inhibition by di- and trivalent cations. J. Membr. Biol. 90:177-190.
    • (1986) J. Membr. Biol. , vol.90 , pp. 177-190
    • Menestrina, G.1
  • 38
    • 0007091026 scopus 로고
    • Electrophysiological methods for the study of toxin-membrane interaction
    • J. E. Alouf and J. H. Freer, eds. Academic Press, London
    • Menestrina, G. 1991. Electrophysiological methods for the study of toxin-membrane interaction. Pages 215-241 in: Sourcebook of Bacterial Protein Toxins. J. E. Alouf and J. H. Freer, eds. Academic Press, London.
    • (1991) Sourcebook of Bacterial Protein Toxins , pp. 215-241
    • Menestrina, G.1
  • 39
    • 0023666566 scopus 로고
    • Escherichia coli haemolysin forms voltage-dependent channels in lipid membranes
    • Menestrina, G., Mackman, N., Holland, I. B., and Bhakdi, S. 1987. Escherichia coli haemolysin forms voltage-dependent channels in lipid membranes. Biochim. Biophys. Acta 905:109-117.
    • (1987) Biochim. Biophys. Acta , vol.905 , pp. 109-117
    • Menestrina, G.1    Mackman, N.2    Holland, I.B.3    Bhakdi, S.4
  • 40
    • 0024707952 scopus 로고
    • Voltage-dependent gating properties of the channel formed by E. Coli hemolysin in planar lipid membranes
    • Menestrina, G., and Ropele, M. 1989. Voltage-dependent gating properties of the channel formed by E. coli hemolysin in planar lipid membranes. Biosci. Rep. 9:465-473.
    • (1989) Biosci. Rep. , vol.9 , pp. 465-473
    • Menestrina, G.1    Ropele, M.2
  • 41
    • 0015459562 scopus 로고
    • Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties
    • Montal, M., and Mueller, P. 1972. Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties. Proc. Natl. Acad. Sci. USA 69:3561-3566.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 3561-3566
    • Montal, M.1    Mueller, P.2
  • 42
    • 0017421326 scopus 로고
    • Conductance fluctuations and ionic pores in membranes
    • Neher, E., and Stevens, C. F. 1977. Conductance fluctuations and ionic pores in membranes. Annu. Rev. Biophys. Bioeng. 6:345-381.
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 345-381
    • Neher, E.1    Stevens, C.F.2
  • 43
    • 12044252647 scopus 로고
    • Structure determination of tolaasin, an extracellular lipodepsipeptide produced by the mushroom pathogen pseudomonas tolaasi Paine
    • Nutkins, J. C., Mortishire-Smith, R. J., Packman, L. C., Brodey, C. L., Rainey, P. B., Johnstone, K., and Williams, D. H. 1991. Structure determination of tolaasin, an extracellular lipodepsipeptide produced by the mushroom pathogen Pseudomonas tolaasi Paine. J. Am. Chem. Soc. 113:2621-2627.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 2621-2627
    • Nutkins, J.C.1    Mortishire-Smith, R.J.2    Packman, L.C.3    Brodey, C.L.4    Rainey, P.B.5    Johnstone, K.6    Williams, D.H.7
  • 44
    • 0022644643 scopus 로고
    • Revised structure of mycosubtilin, a peptidolipid antibiotic from bacillus subtilis
    • Peypoux, F., Pommier, M. T., Marion, D., Ptak, M., Das, C., and Michel, G. 1986. Revised structure of mycosubtilin, a peptidolipid antibiotic from Bacillus subtilis. J. Antibiot. 39:636-641.
    • (1986) J. Antibiot. , vol.39 , pp. 636-641
    • Peypoux, F.1    Pommier, M.T.2    Marion, D.3    Ptak, M.4    Das, C.5    Michel, G.6
  • 45
    • 0020037498 scopus 로고
    • Action of peptidolipidic antibiotics of the iturin group on erythrocytes. Effect of some lipids on haemolysis
    • Quentin, M. J., Besson, F., Peypoux, F., and Michel, G. 1982. Action of peptidolipidic antibiotics of the iturin group on erythrocytes. Effect of some lipids on haemolysis. Biochim. Biophys. Acta 684: 207-211.
    • (1982) Biochim. Biophys. Acta , vol.684 , pp. 207-211
    • Quentin, M.J.1    Besson, F.2    Peypoux, F.3    Michel, G.4
  • 46
    • 0024455884 scopus 로고
    • Electrical properties and molecular architecture of the channel formed by E. Coli hemolysin in planar lipid membranes
    • Ropele, M., and Menestrina, G. 1989. Electrical properties and molecular architecture of the channel formed by E. coli hemolysin in planar lipid membranes. Biochim. Biophys. Acta 985:9-18.
    • (1989) Biochim. Biophys. Acta , vol.985 , pp. 9-18
    • Ropele, M.1    Menestrina, G.2
  • 48
    • 0018236743 scopus 로고
    • Colicin K acts by forming voltage-dependent channels in phospholipid bilayer membranes
    • Schein, S. J., Kagan, B. L., and Finkelstein, A. 1978. Colicin K acts by forming voltage-dependent channels in phospholipid bilayer membranes. Nature 276:159-163.
    • (1978) Nature , vol.276 , pp. 159-163
    • Schein, S.J.1    Kagan, B.L.2    Finkelstein, A.3
  • 50
    • 0018172830 scopus 로고
    • On the physico-chemical basis of voltage-dependent molecular gating mechanisms in biological membranes
    • Schwarz, G. 1978. On the physico-chemical basis of voltage-dependent molecular gating mechanisms in biological membranes. J. Membr. Biol. 43:127-148.
    • (1978) J. Membr. Biol. , vol.43 , pp. 127-148
    • Schwarz, G.1
  • 52
    • 0025797129 scopus 로고
    • Ionic channels induced by surfactin in planar lipid bilayer membranes
    • Sheppard, J. D., Jumarie, C., Cooper, D. G., and Laprade, R. 1991. Ionic channels induced by surfactin in planar lipid bilayer membranes. Biochim. Biophys. Acta 1064:13-23.
    • (1991) Biochim. Biophys. Acta , vol.1064 , pp. 13-23
    • Sheppard, J.D.1    Jumarie, C.2    Cooper, D.G.3    Laprade, R.4
  • 53
    • 0031042584 scopus 로고    scopus 로고
    • A novel method for structure-based predictions of ion channel conductance properties
    • Smart, O. S., Breed, J., Smith, G. R., and Sansom, M. S. P. 1997. A novel method for structure-based predictions of ion channel conductance properties. Biophys. J. 72:1109-1126.
    • (1997) Biophys. J. , vol.72 , pp. 1109-1126
    • Smart, O.S.1    Breed, J.2    Smith, G.R.3    Sansom, M.S.P.4
  • 54
    • 0030023476 scopus 로고    scopus 로고
    • Effect of heterogeneity of hydrophobic moieties on surface activity of lychenysin A, a lipopeptide biosurfactant form Bacillus licheniformis BAS50
    • Yakimov, M. M., Fredrickson, H. L., and Timmis, K. N. 1996. Effect of heterogeneity of hydrophobic moieties on surface activity of lychenysin A, a lipopeptide biosurfactant form Bacillus licheniformis BAS50. Biotechnol. Appl. Biochem. 23:13-18.
    • (1996) Biotechnol. Appl. Biochem. , vol.23 , pp. 13-18
    • Yakimov, M.M.1    Fredrickson, H.L.2    Timmis, K.N.3
  • 55
    • 0000326892 scopus 로고
    • Effect of syringotoxin on the permeability of bilayer lipid membranes
    • Ziegler, W., Pavlovkin, J., and Pokornj, J. 1984. Effect of syringotoxin on the permeability of bilayer lipid membranes. Biologia (Bratislava) 39:693-699.
    • (1984) Biologia (Bratislava) , vol.39 , pp. 693-699
    • Ziegler, W.1    Pavlovkin, J.2    Pokornj, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.