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Volumn 179, Issue 22, 1997, Pages 6994-7003

General secretion pathway (eps) genes required for toxin secretion and outer membrane biogenesis in Vibrio cholerae

Author keywords

[No Author keywords available]

Indexed keywords

CHITINASE; ENTEROTOXIN; PROTEINASE;

EID: 0030785514     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.22.6994-7003.1997     Document Type: Article
Times cited : (165)

References (74)
  • 1
    • 0029797933 scopus 로고    scopus 로고
    • Fimbrial biogenesis genes of Pseudomonas aeruginosa: PilW and pilX increase the similarity of type 4 fimbriae to the GSP protein-secretion systems and pulY1 encodes a gonococcal PilC homologue
    • Alm, R. A., J. P. Hallinan, A. A. Watson, and J. S. Mattick. 1996. Fimbrial biogenesis genes of Pseudomonas aeruginosa: pilW and pilX increase the similarity of type 4 fimbriae to the GSP protein-secretion systems and pulY1 encodes a gonococcal PilC homologue. Mol. Microbiol. 22:161-173.
    • (1996) Mol. Microbiol. , vol.22 , pp. 161-173
    • Alm, R.A.1    Hallinan, J.P.2    Watson, A.A.3    Mattick, J.S.4
  • 2
    • 0026074370 scopus 로고
    • Protein secretion in Pseudomonas aeruginosa: The xcpA gene encodes an integral inner membrane protein homologous to Klebsiella pneumoniae secretion function protein PulO
    • Bally, M., G. Ball, A. Badere, and A. Lazdunski. 1991. Protein secretion in Pseudomonas aeruginosa: the xcpA gene encodes an integral inner membrane protein homologous to Klebsiella pneumoniae secretion function protein PulO. J. Bacteriol. 173:479-486.
    • (1991) J. Bacteriol. , vol.173 , pp. 479-486
    • Bally, M.1    Ball, G.2    Badere, A.3    Lazdunski, A.4
  • 3
    • 0026505643 scopus 로고
    • Protein secretion in Pseudomonas aeruginosa: Characterization of seven xcp genes and processing of secretory apparatus components by prepilin peptidase
    • Bally, M., A. Filloux, M. Akrim, G. Ball, A. Lazdunski, and J. Tommassen. 1992. Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp genes and processing of secretory apparatus components by prepilin peptidase. Mol. Microbiol. 6:1121-1131.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1121-1131
    • Bally, M.1    Filloux, A.2    Akrim, M.3    Ball, G.4    Lazdunski, A.5    Tommassen, J.6
  • 4
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion in Escherichia coli
    • Casadaban, M. C., and S. N. Cohen. 1980. Analysis of gene control signals by DNA fusion in Escherichia coli. J. Mol. Biol. 138:179-207.
    • (1980) J. Mol. Biol. , vol.138 , pp. 179-207
    • Casadaban, M.C.1    Cohen, S.N.2
  • 5
    • 0030048933 scopus 로고    scopus 로고
    • Porins of Vibrio cholerae: Purification and characterization of OmpU
    • Chakrabarti, S. R., K. Chaudhuri, K. Sen, and K. Das. 1996. Porins of Vibrio cholerae: purification and characterization of OmpU. J. Bacteriol. 178:524-530.
    • (1996) J. Bacteriol. , vol.178 , pp. 524-530
    • Chakrabarti, S.R.1    Chaudhuri, K.2    Sen, K.3    Das, K.4
  • 6
    • 0026574606 scopus 로고
    • Some of the out genes involved in the secretion of pectate lyases in Erwinia chrysanthemi are regulated by kdgR
    • Condemine, G., C. Dorel, N. Hugovieux-Cotte-Pattat, and J. Robert-Baudouy, 1992. Some of the out genes involved in the secretion of pectate lyases in Erwinia chrysanthemi are regulated by kdgR. Mol. Microbiol. 6:3199-3211.
    • (1992) Mol. Microbiol. , vol.6 , pp. 3199-3211
    • Condemine, G.1    Dorel, C.2    Hugovieux-Cotte-Pattat, N.3    Robert-Baudouy, J.4
  • 7
    • 0020539979 scopus 로고
    • Conformity between heat-labile toxin genes from human and porcine enterotoxigenic Escherichia coli
    • Dallas, W. S. 1983. Conformity between heat-labile toxin genes from human and porcine enterotoxigenic Escherichia coli. Infect. Immun. 40:647-652.
    • (1983) Infect. Immun. , vol.40 , pp. 647-652
    • Dallas, W.S.1
  • 8
    • 0018688158 scopus 로고
    • Cistrons encoding Escherichia coli heat-labile toxin
    • Dallas, W. S., D. M. Gill, and S. Falkow. 1979. Cistrons encoding Escherichia coli heat-labile toxin. J. Bacteriol. 139:850-858.
    • (1979) J. Bacteriol. , vol.139 , pp. 850-858
    • Dallas, W.S.1    Gill, D.M.2    Falkow, S.3
  • 9
    • 0023441713 scopus 로고
    • Cloning and expression in Escherichia coli of the Klebsiella pneumoniae genes for production, surface localization and secretion of the lipoprotein pullulanase
    • d'Enfert, C., A. Ryter, and A. P. Pugsley. 1987. Cloning and expression in Escherichia coli of the Klebsiella pneumoniae genes for production, surface localization and secretion of the lipoprotein pullulanase. EMBO J. 6:3531-3538.
    • (1987) EMBO J. , vol.6 , pp. 3531-3538
    • D'Enfert, C.1    Ryter, A.2    Pugsley, A.P.3
  • 10
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 11
    • 0025943752 scopus 로고
    • Structural characterization of protein secretion genes of the bacterial phytopathogen Xanthomonas campestris pathovar campestris: Relatedness to secretion systems of other gram-negative bacteria
    • Dums, F., G. M. Dow, and M. J. Daniels. 1991. Structural characterization of protein secretion genes of the bacterial phytopathogen Xanthomonas campestris pathovar campestris: relatedness to secretion systems of other gram-negative bacteria. Mol. Gen. Genet. 229:357-364.
    • (1991) Mol. Gen. Genet. , vol.229 , pp. 357-364
    • Dums, F.1    Dow, G.M.2    Daniels, M.J.3
  • 12
    • 0028264802 scopus 로고
    • Type IV prepilin peptidase gene of Neisseria gonorrhoeae MS11: Presence of a related gene in other piliated and nonpiliated Neisseria strains
    • Dupuy B., and A. P. Pugsley. 1994. Type IV prepilin peptidase gene of Neisseria gonorrhoeae MS11: presence of a related gene in other piliated and nonpiliated Neisseria strains. J. Bacteriol. 176:1323-1331.
    • (1994) J. Bacteriol. , vol.176 , pp. 1323-1331
    • Dupuy, B.1    Pugsley, A.P.2
  • 13
    • 0027310249 scopus 로고
    • Analysis of enterotoxin synthesis in a Vibrio cholerae strain lacking DsbA, a periplasmic enzyme involved in disulphide bond formation
    • Findlay, G., J. Yu, and T. R. Hirst. 1993. Analysis of enterotoxin synthesis in a Vibrio cholerae strain lacking DsbA, a periplasmic enzyme involved in disulphide bond formation. Biochem. Soc. Trans. 21:212S.
    • (1993) Biochem. Soc. Trans. , vol.21
    • Findlay, G.1    Yu, J.2    Hirst, T.R.3
  • 14
    • 0026332855 scopus 로고
    • Vibrio cholerae hemagglutinin/protease, colonial variation, virulence, and detachment
    • Finkelstein, R. A., M. Boesman-Finkelstein, Y. Chang, and C. C. Häse. 1992. Vibrio cholerae hemagglutinin/protease, colonial variation, virulence, and detachment. Infect. Immun. 60:472-478.
    • (1992) Infect. Immun. , vol.60 , pp. 472-478
    • Finkelstein, R.A.1    Boesman-Finkelstein, M.2    Chang, Y.3    Häse, C.C.4
  • 15
    • 0025953682 scopus 로고
    • Distinguishing between the extracellular DNases of Vibrio cholerae and development of a transformation system
    • Focareta, T., and P. A. Manning. 1991. Distinguishing between the extracellular DNases of Vibrio cholerae and development of a transformation system. Mol. Microbiol. 5:2547-2555.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2547-2555
    • Focareta, T.1    Manning, P.A.2
  • 16
    • 0029924909 scopus 로고    scopus 로고
    • The cryptic general secretory pathway (gsp) operon of Escherichia coli K-12 encodes functional proteins
    • Francetic, O., and A. P. Pugsley. 1996. The cryptic general secretory pathway (gsp) operon of Escherichia coli K-12 encodes functional proteins. J. Bacteriol. 178:3544-3549.
    • (1996) J. Bacteriol. , vol.178 , pp. 3544-3549
    • Francetic, O.1    Pugsley, A.P.2
  • 17
    • 0022870839 scopus 로고
    • Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector
    • Fürste, J. P., W. Pansegrau, R. Frank, H. Blocker, P. Scholz, M. Bagdasarian, and E. Lanka. 1986. Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector. Gene 48:119-131.
    • (1986) Gene , vol.48 , pp. 119-131
    • Fürste, J.P.1    Pansegrau, W.2    Frank, R.3    Blocker, H.4    Scholz, P.5    Bagdasarian, M.6    Lanka, E.7
  • 18
    • 0019440931 scopus 로고
    • Subunit number and arrangement in Escherichia coli heat-labile enterotoxin
    • Gill, D. M., J. D. Clements, D. C. Robertson, and R. A. Finkelstein. 1981. Subunit number and arrangement in Escherichia coli heat-labile enterotoxin. Infect. Immun. 33:677-682.
    • (1981) Infect. Immun. , vol.33 , pp. 677-682
    • Gill, D.M.1    Clements, J.D.2    Robertson, D.C.3    Finkelstein, R.A.4
  • 19
    • 0029870545 scopus 로고    scopus 로고
    • Insertion of an outer membrane protein in Escherichia coli requires a chaperon-like protein
    • Hardie, K. R., S. Lory, and A. P. Pugsley. 1996. Insertion of an outer membrane protein in Escherichia coli requires a chaperon-like protein. EMBO J. 15:978-988.
    • (1996) EMBO J. , vol.15 , pp. 978-988
    • Hardie, K.R.1    Lory, S.2    Pugsley, A.P.3
  • 20
    • 0027944329 scopus 로고
    • Genetic characterization of mannose-sensitive hemagglutinin (MSHA)-negative mutants of Vibrio cholerae derived by Tn5 mutagenesis
    • Häse, C. C., M. E. Bauer, and R. A. Finkelstein. 1994. Genetic characterization of mannose-sensitive hemagglutinin (MSHA)-negative mutants of Vibrio cholerae derived by Tn5 mutagenesis. Gene 150:17-25.
    • (1994) Gene , vol.150 , pp. 17-25
    • Häse, C.C.1    Bauer, M.E.2    Finkelstein, R.A.3
  • 21
    • 0025975352 scopus 로고
    • Cloned Erwinia chrysanthemi out genes enable Escherichia coli to selectively secrete a diverse family of heterologous proteins to its milieu
    • He, S. Y., M. Lindeberg, A. K. Chatterjee, and A. Collmer. 1991. Cloned Erwinia chrysanthemi out genes enable Escherichia coli to selectively secrete a diverse family of heterologous proteins to its milieu. Proc. Natl. Acad. Sci. USA 88:1079-1083.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1079-1083
    • He, S.Y.1    Lindeberg, M.2    Chatterjee, A.K.3    Collmer, A.4
  • 22
    • 0023736046 scopus 로고
    • Toxin, toxin-coregulated pili, and the ToxR regulon are essential for Vibrio cholerae pathogenesis in humans
    • Herrington, D. A., R. H. Hall, G. Losonsky, J. J. Mekalanos, R. K. Taylor, and M. M. Levine. 1988. Toxin, toxin-coregulated pili, and the ToxR regulon are essential for Vibrio cholerae pathogenesis in humans. J. Exp. Med. 168:1487-1492.
    • (1988) J. Exp. Med. , vol.168 , pp. 1487-1492
    • Herrington, D.A.1    Hall, R.H.2    Losonsky, G.3    Mekalanos, J.J.4    Taylor, R.K.5    Levine, M.M.6
  • 23
    • 0023449557 scopus 로고
    • Conformation of protein secreted across bacterial outer membranes: A study of enterotoxin translocation from Vibrio cholerae
    • Hirst, T. R., and J. Holmgren. 1987. Conformation of protein secreted across bacterial outer membranes: a study of enterotoxin translocation from Vibrio cholerae. Proc. Natl. Acad. Sci. USA 84:7418-7422.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7418-7422
    • Hirst, T.R.1    Holmgren, J.2
  • 24
    • 0021346267 scopus 로고
    • Cellular location of heat-labile enterotoxin in Escherichia coli
    • Hirst, T. R., L. L. Randall, and S. J. S. Hardy. 1984. Cellular location of heat-labile enterotoxin in Escherichia coli. J. Bacteriol. 157:637-642.
    • (1984) J. Bacteriol. , vol.157 , pp. 637-642
    • Hirst, T.R.1    Randall, L.L.2    Hardy, S.J.S.3
  • 25
    • 0021702380 scopus 로고
    • Kinetics of synthesis, processing, and membrane transport of heat-labile enterotoxin, a periplasmic protein in Escherichia coli
    • Hofstra, H., and B. Witholt. 1984. Kinetics of synthesis, processing, and membrane transport of heat-labile enterotoxin, a periplasmic protein in Escherichia coli. J. Biol. Chem. 259:15182-15187.
    • (1984) J. Biol. Chem. , vol.259 , pp. 15182-15187
    • Hofstra, H.1    Witholt, B.2
  • 26
    • 0027431108 scopus 로고
    • Isolation and analysis of eight exe genes and their involvement in extracellular protein secretion and outer membrane assembly in Aeromonas hydrophila
    • Howard, P. S., J. Critch, and A. Bedi. 1993. Isolation and analysis of eight exe genes and their involvement in extracellular protein secretion and outer membrane assembly in Aeromonas hydrophila. J. Bacteriol. 175:6695-6703.
    • (1993) J. Bacteriol. , vol.175 , pp. 6695-6703
    • Howard, P.S.1    Critch, J.2    Bedi, A.3
  • 27
    • 0026681629 scopus 로고
    • Cloning and characterization of a gene required for the secretion of extracellular enzymes across the outer membrane by Xanthomonas campestris pv. campestris
    • Hu, N.-T., M.-N. Hung, S.-J. Chiou, F. Tang, D.-C. Chiang, H.-Y. Huang, and C.-Y. Wu. 1992. Cloning and characterization of a gene required for the secretion of extracellular enzymes across the outer membrane by Xanthomonas campestris pv. campestris. J. Bacteriol. 174:2679-2687.
    • (1992) J. Bacteriol. , vol.174 , pp. 2679-2687
    • Hu, N.-T.1    Hung, M.-N.2    Chiou, S.-J.3    Tang, F.4    Chiang, D.-C.5    Huang, H.-Y.6    Wu, C.-Y.7
  • 28
    • 0026600442 scopus 로고
    • The Aeromonas hydrophila exeE gene, required both for protein secretion and normal outer membrane biogenesis, is a member of a general secretion pathway
    • Jiang, B., and S. P. Howard. 1992. The Aeromonas hydrophila exeE gene, required both for protein secretion and normal outer membrane biogenesis, is a member of a general secretion pathway. Mol. Microbiol. 6:1351-1361.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1351-1361
    • Jiang, B.1    Howard, S.P.2
  • 29
    • 0021713896 scopus 로고
    • Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-α-factor
    • Julius, D., A. Brake, L. Blair, R. Kunisawa, and J. Thorner. 1984. Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-α-factor. Cell 37:1075-1089.
    • (1984) Cell , vol.37 , pp. 1075-1089
    • Julius, D.1    Brake, A.2    Blair, L.3    Kunisawa, R.4    Thorner, J.5
  • 31
    • 0025944413 scopus 로고
    • Processing of TCP pilin by TcpJ typifies a common step intrinsic to a newly recognized pathway of extracellular protein secretion by Gram-negative bacteria
    • Kaufman, M. R., J. M. Seyer, and R. K. Taylor. 1991. Processing of TCP pilin by TcpJ typifies a common step intrinsic to a newly recognized pathway of extracellular protein secretion by Gram-negative bacteria. Genes Dev. 5:1834-1846.
    • (1991) Genes Dev. , vol.5 , pp. 1834-1846
    • Kaufman, M.R.1    Seyer, J.M.2    Taylor, R.K.3
  • 32
    • 0027467127 scopus 로고
    • Biogenesis and regulation of the Vibrio cholerae toxin-coregulated pilus: Analogies to other virulence factor secretory systems
    • Kaufman, M. R., C. E. Shaw, I. D. Jones, and R. K. Taylor. 1993. Biogenesis and regulation of the Vibrio cholerae toxin-coregulated pilus: analogies to other virulence factor secretory systems. Gene 126:43-49.
    • (1993) Gene , vol.126 , pp. 43-49
    • Kaufman, M.R.1    Shaw, C.E.2    Jones, I.D.3    Taylor, R.K.4
  • 33
    • 0026021803 scopus 로고
    • Pilin expression and processing in pilus mutants of Neisseria gonorrhoeae: Critical role of Gly-1 in assembly
    • Koomey, M., S. Bergstrom, M. Blake, and J. Swanson. 1991. Pilin expression and processing in pilus mutants of Neisseria gonorrhoeae: critical role of Gly-1 in assembly. Mol. Microbiol. 5:279-287.
    • (1991) Mol. Microbiol. , vol.5 , pp. 279-287
    • Koomey, M.1    Bergstrom, S.2    Blake, M.3    Swanson, J.4
  • 34
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and R. F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 35
    • 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 (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 36
    • 0027370018 scopus 로고
    • The ompS gene of Vibrio cholerae encodes a growth-phase dependent maltoporin
    • Lång, H., and E. T. Palva. 1993. The ompS gene of Vibrio cholerae encodes a growth-phase dependent maltoporin. Mol. Microbiol. 10:891-901.
    • (1993) Mol. Microbiol. , vol.10 , pp. 891-901
    • Lång, H.1    Palva, E.T.2
  • 37
    • 0027204807 scopus 로고
    • Conservation of genes encoding components of a type IV pilus assembly/two-step protein export pathway in Neisseria gonorrhoeae
    • Lauer, P., N. H. Albertson, and M. Koomey. 1993. Conservation of genes encoding components of a type IV pilus assembly/two-step protein export pathway in Neisseria gonorrhoeae. Mol. Microbiol. 8:357-368.
    • (1993) Mol. Microbiol. , vol.8 , pp. 357-368
    • Lauer, P.1    Albertson, N.H.2    Koomey, M.3
  • 38
    • 0026564086 scopus 로고
    • Analysis of eight out genes in a cluster required for pectic enzyme secretion by Erwinia chrysanthemi: Sequence comparison with secretion genes from other gram-negative bacteria
    • Lindeberg, M., and A. Collmer. 1992. Analysis of eight out genes in a cluster required for pectic enzyme secretion by Erwinia chrysanthemi: sequence comparison with secretion genes from other gram-negative bacteria. J. Bacteriol. 174:7385-7397.
    • (1992) J. Bacteriol. , vol.174 , pp. 7385-7397
    • Lindeberg, M.1    Collmer, A.2
  • 39
    • 0029927929 scopus 로고    scopus 로고
    • Complementation of deletion mutations in a cloned functional cluster of Erwinia chrysanthemi out genes with Erwinia carotovora out homologues revealed OutC and OutD as candidate gatekeepers of species-specific secretion of proteins via type II pathway
    • Lindeberg, M., G. Salmond, and A. Collmer. 1996. Complementation of deletion mutations in a cloned functional cluster of Erwinia chrysanthemi out genes with Erwinia carotovora out homologues revealed OutC and OutD as candidate gatekeepers of species-specific secretion of proteins via type II pathway. Mol. Microbiol. 20:175-190.
    • (1996) Mol. Microbiol. , vol.20 , pp. 175-190
    • Lindeberg, M.1    Salmond, G.2    Collmer, A.3
  • 40
    • 0029875905 scopus 로고    scopus 로고
    • Essential role of a sodium dodecyl sulfate-resistant protein IV multimer in assembly-export of filamentous phage
    • Linderoth, N. A., P. Model, and M. Russel. 1996. Essential role of a sodium dodecyl sulfate-resistant protein IV multimer in assembly-export of filamentous phage. J. Bacteriol. 178:1962-1970.
    • (1996) J. Bacteriol. , vol.178 , pp. 1962-1970
    • Linderoth, N.A.1    Model, P.2    Russel, M.3
  • 41
    • 0030071927 scopus 로고    scopus 로고
    • Physical linkage of the Vibrio cholerae mannose-sensitive hemagglutinin secretory and structural subunit gene loci: Identification of the mshG coding sequence
    • Marsh, J. W., D. Sun, and R. K. Taylor. 1996. Physical linkage of the Vibrio cholerae mannose-sensitive hemagglutinin secretory and structural subunit gene loci: identification of the mshG coding sequence. Infect. Immun. 64:460-465.
    • (1996) Infect. Immun. , vol.64 , pp. 460-465
    • Marsh, J.W.1    Sun, D.2    Taylor, R.K.3
  • 43
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 44
    • 0023892552 scopus 로고
    • A novel suicide vector and its use in construction of insertion mutations: Osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR
    • Miller, V. L., and J. J. Mekalanos. 1988. A novel suicide vector and its use in construction of insertion mutations: osmoregulation of outer membrane proteins and virulence determinants in Vibrio cholerae requires toxR. J. Bacteriol. 170:2575-2583.
    • (1988) J. Bacteriol. , vol.170 , pp. 2575-2583
    • Miller, V.L.1    Mekalanos, J.J.2
  • 45
    • 0026019764 scopus 로고
    • A series of wide-host-range low-copy-number vectors that allow direct screening for recombinants
    • Morales, V. M., A. Backman, and M. Bagdasarian. 1991. A series of wide-host-range low-copy-number vectors that allow direct screening for recombinants. Gene 97:39-47.
    • (1991) Gene , vol.97 , pp. 39-47
    • Morales, V.M.1    Backman, A.2    Bagdasarian, M.3
  • 47
    • 0021811609 scopus 로고
    • Cloning of extracellular DNase and construction of a DNase-negative strain of Vibrio cholerae
    • Newland, J. W., B. A. Green, J. Foulds, and R. K. Holmes. 1985. Cloning of extracellular DNase and construction of a DNase-negative strain of Vibrio cholerae. Infect. Immun. 47:691-696.
    • (1985) Infect. Immun. , vol.47 , pp. 691-696
    • Newland, J.W.1    Green, B.A.2    Foulds, J.3    Holmes, R.K.4
  • 48
    • 0026345424 scopus 로고
    • Product of the Pseudomonas aeruginosa gene pilD is a prepilin leader peptidase
    • Nunn, D., and S. Lory. 1991. Product of the Pseudomonas aeruginosa gene pilD is a prepilin leader peptidase. Proc. Natl. Acad. Sci. USA 88:3281-3285.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3281-3285
    • Nunn, D.1    Lory, S.2
  • 49
    • 0027273016 scopus 로고
    • Cleavage, methylation, and localization of the Pseudomonas aeruginosa export proteins XcpT, -U, -V, and -W
    • Nunn, D., and S. Lory. 1993. Cleavage, methylation, and localization of the Pseudomonas aeruginosa export proteins XcpT, -U, -V, and -W. J. Bacteriol. 175:4375-4382.
    • (1993) J. Bacteriol. , vol.175 , pp. 4375-4382
    • Nunn, D.1    Lory, S.2
  • 50
    • 0027520986 scopus 로고
    • Genetic organization and sequence of the promoter-distal region of the tcp gene cluster of Vibrio cholerae
    • Ogierman, M. A., S. Zabihi, L. Mourtzios, and P. A. Manning. 1993. Genetic organization and sequence of the promoter-distal region of the tcp gene cluster of Vibrio cholerae. Gene 126:51-60.
    • (1993) Gene , vol.126 , pp. 51-60
    • Ogierman, M.A.1    Zabihi, S.2    Mourtzios, L.3    Manning, P.A.4
  • 51
    • 0027422306 scopus 로고
    • Genes required for extracellular secretion of enterotoxin are clustered in Vibrio cholerae
    • Overbye, L. J., M. Sandkvist, and M. Bagdasarian. 1993. Genes required for extracellular secretion of enterotoxin are clustered in Vibrio cholerae. Gene 132:101-106.
    • (1993) Gene , vol.132 , pp. 101-106
    • Overbye, L.J.1    Sandkvist, M.2    Bagdasarian, M.3
  • 52
    • 0019435491 scopus 로고
    • Synthesis of a precursor to the B subunit of heat-labile enterotoxin in Escherichia coli
    • Palva, E. T., T. R. Hirst, S. J. S. Hardy, J. Holmgren, and L. L. Randall. 1981. Synthesis of a precursor to the B subunit of heat-labile enterotoxin in Escherichia coli. J. Bacteriol. 146:325-330.
    • (1981) J. Bacteriol. , vol.146 , pp. 325-330
    • Palva, E.T.1    Hirst, T.R.2    Hardy, S.J.S.3    Holmgren, J.4    Randall, L.L.5
  • 53
    • 0026501599 scopus 로고
    • Pullulanase secretion in Escherichia coli K-12 requires a cytoplasmic protein and a putative polytopic cytoplasmic membrane protein
    • Possot, O., C. d'Enfert, I. Reyss, and A. P. Pugsley. 1992. Pullulanase secretion in Escherichia coli K-12 requires a cytoplasmic protein and a putative polytopic cytoplasmic membrane protein. Mol. Microbiol. 6:95-105.
    • (1992) Mol. Microbiol. , vol.6 , pp. 95-105
    • Possot, O.1    D'Enfert, C.2    Reyss, I.3    Pugsley, A.P.4
  • 54
    • 0027337742 scopus 로고
    • Processing and methylation of PulG, pilin-like component of the general secretory pathway of Klebsiella oxytoca
    • Pugsley, A. P. 1993. Processing and methylation of PulG, pilin-like component of the general secretory pathway of Klebsiella oxytoca. Mol. Microbiol. 9:295-308.
    • (1993) Mol. Microbiol. , vol.9 , pp. 295-308
    • Pugsley, A.P.1
  • 55
    • 0026605350 scopus 로고
    • An enzyme with type IV prepilin peptidase activity is required to process components of the general extracellular protein secretion pathway of Klebsiella oxytoca
    • Pugsley, A. P., and B. Dupuy. 1992. An enzyme with type IV prepilin peptidase activity is required to process components of the general extracellular protein secretion pathway of Klebsiella oxytoca. Mol. Microbiol. 6:751-760.
    • (1992) Mol. Microbiol. , vol.6 , pp. 751-760
    • Pugsley, A.P.1    Dupuy, B.2
  • 56
    • 0028306098 scopus 로고
    • Beta-lactam topology probe analysis of the OutO NMePhe peptidase, and six other Out protein components of the Erwinia carotovora general secretion pathway apparatus
    • Reeves, P. J., P. Douglas, and G. P. C. Salmond. 1994. Beta-lactam topology probe analysis of the OutO NMePhe peptidase, and six other Out protein components of the Erwinia carotovora general secretion pathway apparatus. Mol. Microbiol. 12:445-457.
    • (1994) Mol. Microbiol. , vol.12 , pp. 445-457
    • Reeves, P.J.1    Douglas, P.2    Salmond, G.P.C.3
  • 57
    • 0027230857 scopus 로고
    • Molecular cloning and characterization of 13 out genes from Erwinia carotovora subspecies carotovora: Genes encoding members of a general secretion pathway (GSP) widespread in Gram-negative bacteria
    • Reeves, P. J., D. Whitcombe, S. Wharam, M. Gibson, G. Allison, N. Bunce, R. Barallon, P. Douglas, V. Mulholland, S. Stevens, D. Walker, and G. P. C. Salmond. 1993. Molecular cloning and characterization of 13 out genes from Erwinia carotovora subspecies carotovora: genes encoding members of a general secretion pathway (GSP) widespread in Gram-negative bacteria. Mol. Microbiol. 8:443-456.
    • (1993) Mol. Microbiol. , vol.8 , pp. 443-456
    • Reeves, P.J.1    Whitcombe, D.2    Wharam, S.3    Gibson, M.4    Allison, G.5    Bunce, N.6    Barallon, R.7    Douglas, P.8    Mulholland, V.9    Stevens, S.10    Walker, D.11    Salmond, G.P.C.12
  • 58
    • 0029060583 scopus 로고
    • Interactions between the autokinase EpsE and EpsL in the cytoplasmic membrane is required for extracellular secretion in Vibrio cholerae
    • Sandkvist, M., M. Bagdasarian, S. P. Howard, and V. J. DiRita. 1995. Interactions between the autokinase EpsE and EpsL in the cytoplasmic membrane is required for extracellular secretion in Vibrio cholerae. EMBO J. 14:1664-1673.
    • (1995) EMBO J. , vol.14 , pp. 1664-1673
    • Sandkvist, M.1    Bagdasarian, M.2    Howard, S.P.3    DiRita, V.J.4
  • 59
    • 0023631374 scopus 로고
    • Alterations at the carboxyl terminus change assembly and secretion properties of the B subunit of Escherichia coli heat-labile enterotoxin
    • Sandkvist, M., T. R. Hirst, and M. Bagdasarian. 1987. Alterations at the carboxyl terminus change assembly and secretion properties of the B subunit of Escherichia coli heat-labile enterotoxin. J. Bacteriol. 169:4570-4576.
    • (1987) J. Bacteriol. , vol.169 , pp. 4570-4576
    • Sandkvist, M.1    Hirst, T.R.2    Bagdasarian, M.3
  • 60
    • 0027506049 scopus 로고
    • A protein required for secretion of cholera toxin through the outer membrane of Vibrio cholerae
    • Sandkvist, M., V. Morales, and M. Bagdasarian. 1993. A protein required for secretion of cholera toxin through the outer membrane of Vibrio cholerae. Gene 123:81-86.
    • (1993) Gene , vol.123 , pp. 81-86
    • Sandkvist, M.1    Morales, V.2    Bagdasarian, M.3
  • 61
    • 0343846702 scopus 로고
    • Assembly of Escherichia coli heat-labile enterotoxin and its secretion from Vibrio cholerae
    • C. Kado, J. Crossa, and L. Sequeira (ed.), Academic Publishers, Dordrecht, The Netherlands
    • Sandkvist, M., L. J. Overbye, T. K. Sixma, W. G. J. Hol, and M. Bagdasarian. 1993. Assembly of Escherichia coli heat-labile enterotoxin and its secretion from Vibrio cholerae, p. 293-309. In C. Kado, J. Crossa, and L. Sequeira (ed.), Molecular mechanisms of bacterial virulence. Academic Publishers, Dordrecht, The Netherlands.
    • (1993) Molecular Mechanisms of Bacterial Virulence , pp. 293-309
    • Sandkvist, M.1    Overbye, L.J.2    Sixma, T.K.3    Hol, W.G.J.4    Bagdasarian, M.5
  • 63
    • 0025694884 scopus 로고
    • Genetic analysis of protein export in Escherichia coli
    • Schatz, P. J., and J. Beckwith. 1990. Genetic analysis of protein export in Escherichia coli. Annu. Rev. Genet. 24:215-248.
    • (1990) Annu. Rev. Genet. , vol.24 , pp. 215-248
    • Schatz, P.J.1    Beckwith, J.2
  • 64
  • 66
    • 0026458260 scopus 로고
    • Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin
    • Spangler, B. D. 1992. Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin. Microbiol. Rev. 56:622-647.
    • (1992) Microbiol. Rev. , vol.56 , pp. 622-647
    • Spangler, B.D.1
  • 67
    • 0027528605 scopus 로고
    • A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type IV pilin family
    • Strom, M. S., D. N. Nunn, and S. Lory. 1993. A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type IV pilin family. Proc. Natl. Acad. Sci. USA 90:2404-2408.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2404-2408
    • Strom, M.S.1    Nunn, D.N.2    Lory, S.3
  • 70
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor, S., and C. C. Richardson. 1985. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. USA 82:1074-1078.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 71
    • 0025296833 scopus 로고
    • Attachment of Vibrio cholerae serogroup O1 to zooplankton and phytoplankton of Bangladesh waters
    • Tamplin, M. L., A. L. Gauzens, A. Huq, D. A. Sack, and R. R. Colwell. 1990. Attachment of Vibrio cholerae serogroup O1 to zooplankton and phytoplankton of Bangladesh waters. Appl. Environ. Microbiol. 56:1977-1980.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 1977-1980
    • Tamplin, M.L.1    Gauzens, A.L.2    Huq, A.3    Sack, D.A.4    Colwell, R.R.5
  • 72
    • 0342556516 scopus 로고
    • A simplified method of direct sequencing of PCR amplified DNA with Sequenase T7 DNA polymerase
    • Thien, S. L. 1989. A simplified method of direct sequencing of PCR amplified DNA with Sequenase T7 DNA polymerase. USB Editorial Comments 16:8,18.
    • (1989) USB Editorial Comments , vol.16 , pp. 8
    • Thien, S.L.1
  • 74
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne, G. 1986. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14:4683-4690.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1


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