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Volumn 31, Issue 2, 1999, Pages 557-567

Analysis of the SlyA-controlled expression, subcellular localization and pore-forming activity of a 34 kDa haemolysin (ClyA) from Escherichia coli K-12

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; HEMOLYSIN; SPACER DNA;

EID: 0032927728     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1999.01196.x     Document Type: Article
Times cited : (97)

References (27)
  • 1
    • 0029671024 scopus 로고    scopus 로고
    • Characterization of an RTX toxin from enterohemorrhagic Escherichia coli O157:H7
    • Bauer, M.E., and Welch, R.A. (1996) Characterization of an RTX toxin from enterohemorrhagic Escherichia coli O157:H7. Infect Immun 64: 167-175.
    • (1996) Infect Immun , vol.64 , pp. 167-175
    • Bauer, M.E.1    Welch, R.A.2
  • 2
    • 0018139740 scopus 로고
    • Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli
    • Benz, R., Janko, K., Boos, W., and Läuger, P. (1978) Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli. Biochim Biophys Acta 511: 305-319.
    • (1978) Biochim Biophys Acta , vol.511 , pp. 305-319
    • Benz, R.1    Janko, K.2    Boos, W.3    Läuger, P.4
  • 3
    • 0018378684 scopus 로고
    • Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli
    • Benz, R., Janko, K., and Läuger, P. (1979) Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli. Biochim Biophys Acta 551: 238-247.
    • (1979) Biochim Biophys Acta , vol.551 , pp. 238-247
    • Benz, R.1    Janko, K.2    Läuger, P.3
  • 4
    • 0024505102 scopus 로고
    • Pore formation by the Escherichia coli hemolysin: Evidence for an association-dissociation equilibrium of the pore-forming aggregates
    • Benz, R., Schmid, A., Wagner, W., and Goebel, W. (1989) Pore formation by the Escherichia coli hemolysin: evidence for an association-dissociation equilibrium of the pore-forming aggregates. Infect Immun 57: 887-895.
    • (1989) Infect Immun , vol.57 , pp. 887-895
    • Benz, R.1    Schmid, A.2    Wagner, W.3    Goebel, W.4
  • 5
    • 0029916264 scopus 로고    scopus 로고
    • Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin: Prototypes of pore-forming bacterial cytolysins
    • Bhakdi, S., Bayley, H., Valeva, A., Walev, I., Walker, B., Weller, U., Kehoe, M., and Palmer, M. (1996) Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin: prototypes of pore-forming bacterial cytolysins. Arch Microbiol 165: 73-79.
    • (1996) Arch Microbiol , vol.165 , pp. 73-79
    • Bhakdi, S.1    Bayley, H.2    Valeva, A.3    Walev, I.4    Walker, B.5    Weller, U.6    Kehoe, M.7    Palmer, M.8
  • 6
    • 0001858383 scopus 로고
    • The ionic current in solutions
    • Reading, MA: Addison-Wesley
    • Castellan, G.W. (1983) The ionic current in solutions. In Physical Chemistry. Reading, MA: Addison-Wesley, pp. 769-780.
    • (1983) Physical Chemistry , pp. 769-780
    • Castellan, G.W.1
  • 7
    • 0028941612 scopus 로고
    • Homologies between salmolysin and some bacterial regulatory proteins
    • Dehoux, P., and Cossart, P. (1995) Homologies between salmolysin and some bacterial regulatory proteins. Mol Microbiol 15: 591-592.
    • (1995) Mol Microbiol , vol.15 , pp. 591-592
    • Dehoux, P.1    Cossart, P.2
  • 8
    • 0030749399 scopus 로고    scopus 로고
    • The Escherichia coli K-12 sheA gene encodes a 34 kDa secreted haemolysin
    • Del Castillo, F.J., Leal, S.C., Moreno, F., and del Castillo, I. (1997) The Escherichia coli K-12 sheA gene encodes a 34 kDa secreted haemolysin. Mol Microbiol 25: 107-115.
    • (1997) Mol Microbiol , vol.25 , pp. 107-115
    • Del Castillo, F.J.1    Leal, S.C.2    Moreno, F.3    Del Castillo, I.4
  • 9
    • 0002595586 scopus 로고
    • Pore-forming activity in the outer membrane of the chloroplast envelope
    • Flügge, U.I., and Benz, R. (1984) Pore-forming activity in the outer membrane of the chloroplast envelope. FEBS Lett 169: 85-89.
    • (1984) FEBS Lett , vol.169 , pp. 85-89
    • Flügge, U.I.1    Benz, R.2
  • 10
    • 0031450904 scopus 로고    scopus 로고
    • The molecular basis for the differential regulation of the hlyE-encoded haemolysin of Escherichia coli by FNR and HlyX lies in the improved activating region 1 contact of HlyX
    • Green, J., and Baldwin, M.L. (1997) The molecular basis for the differential regulation of the hlyE-encoded haemolysin of Escherichia coli by FNR and HlyX lies in the improved activating region 1 contact of HlyX. Microbiology 143: 3785-3793.
    • (1997) Microbiology , vol.143 , pp. 3785-3793
    • Green, J.1    Baldwin, M.L.2
  • 11
    • 0029744875 scopus 로고    scopus 로고
    • Synthesis, maturation and export of the E. coli hemolysin
    • Koronakis, V., and Hughes, C. (1996) Synthesis, maturation and export of the E. coli hemolysin. Med Microbiol Immunol 185: 65-71.
    • (1996) Med Microbiol Immunol , vol.185 , pp. 65-71
    • Koronakis, V.1    Hughes, C.2
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0030156042 scopus 로고    scopus 로고
    • Cytolytic toxins from gram-negative bacteria
    • Ludwig, A. (1996) Cytolytic toxins from gram-negative bacteria. Microbiologia SEM 12: 281-296.
    • (1996) Microbiologia SEM , vol.12 , pp. 281-296
    • Ludwig, A.1
  • 15
    • 0029589218 scopus 로고
    • SlyA, a regulatory protein of Salmonella typhimurium, induces a haemolytic and pore-forming protein in Escherichia coli
    • Ludwig, A., Tengel, C., Bauer, S., Bubert, A., Benz, R., Mollenkopf, H.-J., and Goebel, W. (1995) SlyA, a regulatory protein of Salmonella typhimurium, induces a haemolytic and pore-forming protein in Escherichia coli. Mol Gen Genet 249: 474-486.
    • (1995) Mol Gen Genet , vol.249 , pp. 474-486
    • Ludwig, A.1    Tengel, C.2    Bauer, S.3    Bubert, A.4    Benz, R.5    Mollenkopf, H.-J.6    Goebel, W.7
  • 16
    • 0029812094 scopus 로고    scopus 로고
    • Analysis of the in vivo activation of hemolysin (HlyA) from Escherichia coli
    • Ludwig, A., Garcia, F., Bauer, S., Jarchau, T., Benz, R., Hoppe, J., and Goebel, W. (1996) Analysis of the in vivo activation of hemolysin (HlyA) from Escherichia coli. J Bacteriol 178: 5422-5430.
    • (1996) J Bacteriol , vol.178 , pp. 5422-5430
    • Ludwig, A.1    Garcia, F.2    Bauer, S.3    Jarchau, T.4    Benz, R.5    Hoppe, J.6    Goebel, W.7
  • 17
    • 0000632797 scopus 로고
    • TnphoA: A transposon probe for protein export signals
    • Manoil, C., and Beckwith, J. (1985) TnphoA: a transposon probe for protein export signals. Proc Natl Acad Sci USA 82: 8129-8133.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 8129-8133
    • Manoil, C.1    Beckwith, J.2
  • 18
    • 0029867360 scopus 로고    scopus 로고
    • Induction of haemolytic activity in Escherichia coli by the slyA gene product
    • Oscarsson, J., Mizunoe, Y., Uhlin, B.E., and Haydon, D.J. (1996) Induction of haemolytic activity in Escherichia coli by the slyA gene product. Mol Microbiol 20: 191-199.
    • (1996) Mol Microbiol , vol.20 , pp. 191-199
    • Oscarsson, J.1    Mizunoe, Y.2    Uhlin, B.E.3    Haydon, D.J.4
  • 20
    • 0015126697 scopus 로고
    • Molecular sieving by the Bacillus megaterium cell wall and protoplast
    • Scherrer, R., and Gerhardt, P. (1971) Molecular sieving by the Bacillus megaterium cell wall and protoplast. J Bacteriol 107: 718-735.
    • (1971) J Bacteriol , vol.107 , pp. 718-735
    • Scherrer, R.1    Gerhardt, P.2
  • 21
    • 0028937570 scopus 로고
    • Molecular analysis of the plasmid-encoded hemolysin of Escherichia coli O157:H7 strain EDL 933
    • Schmidt, H., Beutin, L., and Karch, H. (1995) Molecular analysis of the plasmid-encoded hemolysin of Escherichia coli O157:H7 strain EDL 933. Infect Immun 63: 1055-1061.
    • (1995) Infect Immun , vol.63 , pp. 1055-1061
    • Schmidt, H.1    Beutin, L.2    Karch, H.3
  • 22
    • 0029996175 scopus 로고    scopus 로고
    • Analysis of the EHEC hly operon and its location in the physical map of the large plasmid of enterohaemorrhagic Escherichia coli O157:H7
    • Schmidt, H., Kernbach, C., and Karch, H. (1996a) Analysis of the EHEC hly operon and its location in the physical map of the large plasmid of enterohaemorrhagic Escherichia coli O157:H7. Microbiology 142: 907-914.
    • (1996) Microbiology , vol.142 , pp. 907-914
    • Schmidt, H.1    Kernbach, C.2    Karch, H.3
  • 23
    • 0029908717 scopus 로고    scopus 로고
    • Pore-forming properties of the plasmid-encoded hemolysin of enterohemorrhagic Escherichia coli O157:H7
    • Schmidt, H., Maier, E., Karch, H., and Benz, R. (1996b) Pore-forming properties of the plasmid-encoded hemolysin of enterohemorrhagic Escherichia coli O157:H7. Eur J Biochem 241: 594-601.
    • (1996) Eur J Biochem , vol.241 , pp. 594-601
    • Schmidt, H.1    Maier, E.2    Karch, H.3    Benz, R.4
  • 24
    • 0000845013 scopus 로고
    • Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBR322
    • Sutcliffe, J.G. (1978) Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBR322. Proc Natl Acad Sci USA 75: 3737-3741.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 3737-3741
    • Sutcliffe, J.G.1
  • 25
    • 0030668089 scopus 로고    scopus 로고
    • The Rap and Hor proteins of Erwinia, Serratia and Yersinia: A novel subgroup in a growing superfamily of proteins regulating diverse physiological processes in bacterial pathogens
    • Thomson, N.R., Cox, A., Bycroft, B.W., Stewart, G.S.A.B., Williams, P., and Salmond, G.P.C. (1997) The Rap and Hor proteins of Erwinia, Serratia and Yersinia: a novel subgroup in a growing superfamily of proteins regulating diverse physiological processes in bacterial pathogens. Mol Microbiol 26: 531-544.
    • (1997) Mol Microbiol , vol.26 , pp. 531-544
    • Thomson, N.R.1    Cox, A.2    Bycroft, B.W.3    Stewart, G.S.A.B.4    Williams, P.5    Salmond, G.P.C.6
  • 26
    • 0002832111 scopus 로고
    • Pore-forming toxins of gram-positive bacteria
    • Roth, J.A., Bolin, C.A., Brogden, K.A., Minion, F.C., and Wannemuehler, M.J. (eds). Washington, DC: American Society for Microbiology Press
    • Tweten, R.K. (1995) Pore-forming toxins of gram-positive bacteria. In Virulence Mechanisms of Bacterial Pathogens. Roth, J.A., Bolin, C.A., Brogden, K.A., Minion, F.C., and Wannemuehler, M.J. (eds). Washington, DC: American Society for Microbiology Press, pp. 207-229.
    • (1995) Virulence Mechanisms of Bacterial Pathogens , pp. 207-229
    • Tweten, R.K.1
  • 27
    • 0026080402 scopus 로고
    • Pore-forming cytolysins of gram-negative bacteria
    • Welch, R.A. (1991) Pore-forming cytolysins of gram-negative bacteria. Mol Microbiol 5: 521-528.
    • (1991) Mol Microbiol , vol.5 , pp. 521-528
    • Welch, R.A.1


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