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Volumn 52, Issue 1, 2004, Pages 67-79

The inner membrane subassembly of the enteropathogenic Escherichia coli bundle-forming pilus machine

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ESCHERICHIA COLI PROTEIN; NUCLEOTIDE BINDING PROTEIN; PROTEIN BFPC; PROTEIN BFPD; PROTEIN BFPE; PROTEIN BFPF; PROTEIN TFPS; UNCLASSIFIED DRUG;

EID: 1942424083     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2003.03963.x     Document Type: Article
Times cited : (59)

References (73)
  • 1
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: Preparing the next generation of molecular biologists
    • Alberts, B. (1998) The cell as a collection of protein machines: preparing the next generation of molecular biologists. Cell 92: 291-294.
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1
  • 2
    • 0033613811 scopus 로고    scopus 로고
    • Membrane topology of the Rickettsia prowazekii ATP/ADP translocase revealed by novel dual pho-lac reporters
    • Alexeyev, M.F., and Winkler, H.H. (1999) Membrane topology of the Rickettsia prowazekii ATP/ADP translocase revealed by novel dual pho-lac reporters. J Mol Biol 285: 1503-1513.
    • (1999) J Mol Biol , vol.285 , pp. 1503-1513
    • Alexeyev, M.F.1    Winkler, H.H.2
  • 3
    • 0029063497 scopus 로고
    • Identification of a gene, pilV, required for type 4 fimbrial biogenesis in Pseudomonas aeruginosa, whose product possesses a pre-pilin-like leader sequence
    • Alm, R.A., and Mattick, J.S. (1995) Identification of a gene, pilV, required for type 4 fimbrial biogenesis in Pseudomonas aeruginosa, whose product possesses a pre-pilin-like leader sequence. Mol Micro 16: 485-496.
    • (1995) Mol Micro , vol.16 , pp. 485-496
    • Alm, R.A.1    Mattick, J.S.2
  • 4
    • 0030042096 scopus 로고    scopus 로고
    • Identification of a novel gene, pilZ, essential for type 4 fimbrial biogenesis in Pseudomonas aeruginosa
    • Alm, R.A., Bodero, A.J., Free, P.D., and Mattick, U.S. (1996a) Identification of a novel gene, pilZ, essential for type 4 fimbrial biogenesis in Pseudomonas aeruginosa. J Bacteriol 178: 46-53.
    • (1996) J Bacteriol , vol.178 , pp. 46-53
    • Alm, R.A.1    Bodero, A.J.2    Free, P.D.3    Mattick, U.S.4
  • 5
    • 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 pilY1 encodes a gonococcal PilC homologue
    • Alm, R.A., Hallinan, J.P., Watson, A.A., and Mattick, U.S. (1996b) Fimbrial biogenesis genes of Pseudomonas aeruginosa: pilW and pilX increase the similarity of type 4 fimbriae to the GSP protein-secretion systems and pilY1 encodes a gonococcal PilC homologue. Mol Micro 22; 161-173.
    • (1996) Mol Micro , vol.22 , pp. 161-173
    • Alm, R.A.1    Hallinan, J.P.2    Watson, A.A.3    Mattick, U.S.4
  • 6
    • 0031985046 scopus 로고    scopus 로고
    • Role of BfpF, a member of the PilT family of putative nucleotide-binding proteins, in type IV pilus biogenesis and in interactions between enteropathogenic Escherichia coli and host cells
    • Anantha, R.P., Stone, K.D., and Donnenberg, M.S. (1998) Role of BfpF, a member of the PilT family of putative nucleotide-binding proteins, in type IV pilus biogenesis and in interactions between enteropathogenic Escherichia coli and host cells. Infect Immun 66: 122-131.
    • (1998) Infect Immun , vol.66 , pp. 122-131
    • Anantha, R.P.1    Stone, K.D.2    Donnenberg, M.S.3
  • 7
    • 0034005318 scopus 로고    scopus 로고
    • Effects of bfp mutations on biogenesis of functional enteropathogenic Escherichia coli type IV pili
    • Anantha, R.P., Stone, K.D., and Donnenberg, M.S. (2000) Effects of bfp mutations on biogenesis of functional enteropathogenic Escherichia coli type IV pili. J Bacteriol 182: 2498-2506.
    • (2000) J Bacteriol , vol.182 , pp. 2498-2506
    • Anantha, R.P.1    Stone, K.D.2    Donnenberg, M.S.3
  • 8
    • 0032948809 scopus 로고    scopus 로고
    • Assembly of XcpR in the cytoplasmic membrane is required for extracellular protein secretion in Pseudomonas aeruginosa
    • Ball, G., Chapon-Hervé, V., Bleves, S., Michel, G., and Bally, M. (1999) Assembly of XcpR in the cytoplasmic membrane is required for extracellular protein secretion in Pseudomonas aeruginosa. J Bacteriol 181: 382-388.
    • (1999) J Bacteriol , vol.181 , pp. 382-388
    • Ball, G.1    Chapon-Hervé, V.2    Bleves, S.3    Michel, G.4    Bally, M.5
  • 9
    • 0032568984 scopus 로고    scopus 로고
    • Type IV pili, transient bacterial aggregates, and virulence of enteropathogenic Escherichia coli
    • Bieber, D., Ramer, S.W., Wu, C.-Y., Murray, W.J., Tobe, T., Fernandez, R., and Schoolnik, G.K. (1998) Type IV pili, transient bacterial aggregates, and virulence of enteropathogenic Escherichia coli. Science 280: 2114-2118.
    • (1998) Science , vol.280 , pp. 2114-2118
    • Bieber, D.1    Ramer, S.W.2    Wu, C.-Y.3    Murray, W.J.4    Tobe, T.5    Fernandez, R.6    Schoolnik, G.K.7
  • 10
    • 0034937029 scopus 로고    scopus 로고
    • Novel topology of BfpE, a cytoplasmic membrane protein required for type IV fimbrial biogenesis in enteropathogenic Escherichia coli
    • Blank, T.E., and Donnenberg, M.S. (2001) Novel topology of BfpE, a cytoplasmic membrane protein required for type IV fimbrial biogenesis in enteropathogenic Escherichia coli. J Bacteriol 183: 4435-4450.
    • (2001) J Bacteriol , vol.183 , pp. 4435-4450
    • Blank, T.E.1    Donnenberg, M.S.2
  • 11
    • 0015499038 scopus 로고
    • Stimulation of pilus formation in Pseudomonas aeruginosa by RNA bacteriophage adsorption
    • Bradley, D.E. (1972) Stimulation of pilus formation in Pseudomonas aeruginosa by RNA bacteriophage adsorption. Biochem Biophys Res Commun 47:1080-1087.
    • (1972) Biochem Biophys Res Commun , vol.47 , pp. 1080-1087
    • Bradley, D.E.1
  • 12
    • 0018821703 scopus 로고
    • A function of Pseudomonas aeruginosa PAO polar pili: Twitching motility
    • Bradley, D.E. (1980) A function of Pseudomonas aeruginosa PAO polar pili: Twitching motility. Can J Microbiol 26: 146-154.
    • (1980) Can J Microbiol , vol.26 , pp. 146-154
    • Bradley, D.E.1
  • 13
    • 0028940060 scopus 로고
    • ComC is required for the processing and translocation of ComGC, a pilin-like competence protein of Bacillus subtilis
    • Chung, Y.S., and Dubnau, D. (1995) ComC is required for the processing and translocation of ComGC, a pilin-like competence protein of Bacillus subtilis. Mol Microbiol 15: 543-551.
    • (1995) Mol Microbiol , vol.15 , pp. 543-551
    • Chung, Y.S.1    Dubnau, D.2
  • 14
    • 0031973221 scopus 로고    scopus 로고
    • All seven comG open reading frames are required for DNA binding during transformation of competent Bacillus subtilis
    • Chung, Y.S., and Dubnau, D. (1998) All seven comG open reading frames are required for DNA binding during transformation of competent Bacillus subtilis. J Bacteriol 180: 41-45.
    • (1998) J Bacteriol , vol.180 , pp. 41-45
    • Chung, Y.S.1    Dubnau, D.2
  • 15
    • 0031950535 scopus 로고    scopus 로고
    • Cell surface localization and processing of the ComG proteins, required for DNA binding during transformation of Bacillus subtilis
    • Chung, Y.S., Breidt, F., and Dubnau, D. (1998) Cell surface localization and processing of the ComG proteins, required for DNA binding during transformation of Bacillus subtilis. Mol Microbiol 29: 905-913.
    • (1998) Mol Microbiol , vol.29 , pp. 905-913
    • Chung, Y.S.1    Breidt, F.2    Dubnau, D.3
  • 16
    • 0018599718 scopus 로고
    • An adhesive factor found in strains of Escherichia coli belonging to the traditional infantile enteropathogenic serotypes
    • Cravioto, A., Gross, R.J., Scotland, S.M., and Rowe, B. (1979) An adhesive factor found In strains of Escherichia coli belonging to the traditional infantile enteropathogenic serotypes. Curr Microbiol 3: 95-99.
    • (1979) Curr Microbiol , vol.3 , pp. 95-99
    • Cravioto, A.1    Gross, R.J.2    Scotland, S.M.3    Rowe, B.4
  • 17
    • 0025836761 scopus 로고
    • Escherichia coli alkaline phosphatase fails to acquire disulfide bonds when retained in the cytoplasm
    • Derman, A.I., and Beckwith, J. (1991) Escherichia coli alkaline phosphatase fails to acquire disulfide bonds when retained in the cytoplasm. J Bacteriol 173: 7719-7722.
    • (1991) J Bacteriol , vol.173 , pp. 7719-7722
    • Derman, A.I.1    Beckwith, J.2
  • 18
    • 0001102041 scopus 로고
    • Enteropathogenic Escherichia coli
    • Blaser, M.J., Smith, P.D., Ravdin, J.I., Greenberg, H.B. and Guerrant, R.L., (eds). New York: Raven Press
    • Donnenberg, M.S. (1995) Enteropathogenic Escherichia coli. In Infections of the Gastrointestinal Tract. Blaser, M.J., Smith, P.D., Ravdin, J.I., Greenberg, H.B. and Guerrant, R.L., (eds). New York: Raven Press, pp. 709-726.
    • (1995) Infections of the Gastrointestinal Tract , pp. 709-726
    • Donnenberg, M.S.1
  • 19
    • 0026482190 scopus 로고
    • A plasmid-encoded type IV fimbrial gene of enteropathogenic Escherichia coli associated with localized adherence
    • Donnenberg, M.S., Girón, J.A., Nataro, J.P., and Kaper, J.B. (1992) A plasmid-encoded type IV fimbrial gene of enteropathogenic Escherichia coli associated with localized adherence. Mol Microbiol 6: 3427-3437.
    • (1992) Mol Microbiol , vol.6 , pp. 3427-3437
    • Donnenberg, M.S.1    Girón, J.A.2    Nataro, J.P.3    Kaper, J.B.4
  • 20
    • 0032697140 scopus 로고    scopus 로고
    • DNA uptake in bacteria
    • Dubnau, D. (1999) DNA uptake in bacteria. Annu Rev Microbiol 53: 217-244.
    • (1999) Annu Rev Microbiol , vol.53 , pp. 217-244
    • Dubnau, D.1
  • 21
    • 0242360953 scopus 로고    scopus 로고
    • DNA transport during transformation
    • Dubnau, D. (2003) DNA transport during transformation. Front Biosci 8: s544-s556.
    • (2003) Front Biosci , vol.8
    • Dubnau, D.1
  • 22
    • 0037406829 scopus 로고    scopus 로고
    • Type II protein secretion in Pseudomonas aeruginosa: The pseudopilus is a multifibrillar and adhesive structure
    • Durand, É., Bernadac, A., Ball, G., Lazdunski, A., Sturgis, J.N., and Filloux, A. (2003) Type II protein secretion in Pseudomonas aeruginosa: the pseudopilus is a multifibrillar and adhesive structure. J Bacteriol 185: 2749-2758.
    • (2003) J Bacteriol , vol.185 , pp. 2749-2758
    • Durand, É.1    Bernadac, A.2    Ball, G.3    Lazdunski, A.4    Sturgis, J.N.5    Filloux, A.6
  • 23
    • 0029008485 scopus 로고
    • Characterization of the pilF-pilD pilus-assembly locus of Neisseria gonorrhoeae
    • Freitag, N.E., Seifert, H.S., and Koomey, M. (1995) Characterization of the pilF-pilD pilus-assembly locus of Neisseria gonorrhoeae. Mol Microbiol 16: 575-586.
    • (1995) Mol Microbiol , vol.16 , pp. 575-586
    • Freitag, N.E.1    Seifert, H.S.2    Koomey, M.3
  • 25
    • 0024357799 scopus 로고
    • A simple method for site-directed mutagenesis using the polymerase chain reaction
    • Helmsley, A., Arnheim, N., Toney, M.D., Cortopassi, G., and Galas, D.J. (1989) A simple method for site-directed mutagenesis using the polymerase chain reaction. Nucleic Acids Res 17: 6545-6551.
    • (1989) Nucleic Acids Res , vol.17 , pp. 6545-6551
    • Helmsley, A.1    Arnheim, N.2    Toney, M.D.3    Cortopassi, G.4    Galas, D.J.5
  • 26
  • 27
    • 0023736046 scopus 로고
    • Toxin, toxin-coregulated pili, and the toxR regulon are essential for Vibrio cholerae pathogenesis in humans
    • Herrington, D.A., Hall, R.H., Losonsky, G., Mekalanos, J.J., Taylor, R.K., and Levin, M.M. (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    Levin, M.M.6
  • 28
    • 0027489247 scopus 로고
    • Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein-secretion apparatus: A general system for the formation of surface-associated protein complexes
    • Hobbs, M., and Mattick, U.S. (1993) Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein-secretion apparatus: a general system for the formation of surface-associated protein complexes. Mol Microbiol 10: 233-243.
    • (1993) Mol Microbiol , vol.10 , pp. 233-243
    • Hobbs, M.1    Mattick, U.S.2
  • 29
    • 0036646537 scopus 로고    scopus 로고
    • XpsG, the major pseudopilin in Xanthomonas campestris pv. Campestris, forms a pilus-like structure between cytoplasmic and outer membranes
    • Hu, N.T., Leu, W.M., Lee, M.S., Chen, A., Cheng, S.C., Song, Y.L., and Chen, L.Y. (2002) XpsG, the major pseudopilin in Xanthomonas campestris pv. Campestris, forms a pilus-like structure between cytoplasmic and outer membranes. Biochem J 365: 205-211.
    • (2002) Biochem J , vol.365 , pp. 205-211
    • Hu, N.T.1    Leu, W.M.2    Lee, M.S.3    Chen, A.4    Cheng, S.C.5    Song, Y.L.6    Chen, L.Y.7
  • 30
    • 0242575007 scopus 로고    scopus 로고
    • Structural and topographical studies of the type IV bundle-forming pilus assembly complex of enteropathogenic Escherichia coli
    • Hwang, J., Bieber, D., Ramer, S.W., Wu, C.-Y., and Schoolnik, G.K. (2003) Structural and topographical studies of the type IV bundle-forming pilus assembly complex of enteropathogenic Escherichia coli. J Bacteriol 185: 6695-6701.
    • (2003) J Bacteriol , vol.185 , pp. 6695-6701
    • Hwang, J.1    Bieber, D.2    Ramer, S.W.3    Wu, C.-Y.4    Schoolnik, G.K.5
  • 31
    • 0034724415 scopus 로고    scopus 로고
    • Sequence-related protein export NTPases encoded by the conjugative transfer region of RP4 and by the cag pathogenicity island of Helicobacter pylori share similar hexameric ring structures
    • Krause, S., Bárcena, M., Pansegrau, W., Lurz, R., Carazo, J.M., and Lanka, E. (2000) Sequence-related protein export NTPases encoded by the conjugative transfer region of RP4 and by the cag pathogenicity island of Helicobacter pylori share similar hexameric ring structures. Proc Natl Acad Sci USA 97: 3067-3072.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3067-3072
    • Krause, S.1    Bárcena, M.2    Pansegrau, W.3    Lurz, R.4    Carazo, J.M.5    Lanka, E.6
  • 32
    • 0035157710 scopus 로고    scopus 로고
    • Involvement of the XpsN protein in formation of the XpsL-XpsM complex in Xanthomonas campestris pv. Campestris type II secretion apparatus
    • Lee, H.-M., Tyan, S.-W., Leu, W.-M., Chen, L-Y., Chen, D.C., and Hu, N.-T. (2001) Involvement of the XpsN protein in formation of the XpsL-XpsM complex in Xanthomonas campestris pv. Campestris type II secretion apparatus. J Bacteriol 183: 528-535.
    • (2001) J Bacteriol , vol.183 , pp. 528-535
    • Lee, H.-M.1    Tyan, S.-W.2    Leu, W.-M.3    Chen, L.-Y.4    Chen, D.C.5    Hu, N.-T.6
  • 33
    • 0028136885 scopus 로고
    • Bacterial gene transfer by natural genetic transformation in the environment
    • Lorenz, M.G., and Wackernagel, W. (1994) Bacterial gene transfer by natural genetic transformation in the environment. Microbiol Rev 58: 563-602.
    • (1994) Microbiol Rev , vol.58 , pp. 563-602
    • Lorenz, M.G.1    Wackernagel, W.2
  • 34
    • 0036188456 scopus 로고    scopus 로고
    • TrwD, the hexameric traffic ATPase encoded by plasmid R388, induces membrane destabilization and hemifusion of lipid vesicles
    • Machón, C., Rivas, S., Albert, A., Goñi, F.M., and de la Cruz, F. (2002) TrwD, the hexameric traffic ATPase encoded by plasmid R388, induces membrane destabilization and hemifusion of lipid vesicles. J Bacteriol 184: 1661-1668.
    • (2002) J Bacteriol , vol.184 , pp. 1661-1668
    • Machón, C.1    Rivas, S.2    Albert, A.3    Goñi, F.M.4    De La Cruz, F.5
  • 35
    • 0035095037 scopus 로고    scopus 로고
    • Translocated EspF protein from enteropathogenic Escherichia coli disrupts host intestinal barrier function
    • McNamara, B.P., Koutsouris, A., O'Connell, C.B., Nougayrède, J.P., Donnenberg, M.S., and Hecht, G. (2001) Translocated EspF protein from enteropathogenic Escherichia coli disrupts host intestinal barrier function. J Clin Invest 107: 621-629.
    • (2001) J Clin Invest , vol.107 , pp. 621-629
    • McNamara, B.P.1    Koutsouris, A.2    O'Connell, C.B.3    Nougayrède, J.P.4    Donnenberg, M.S.5    Hecht, G.6
  • 37
    • 0000324271 scopus 로고
    • Common architecture of type IV fimbriae and complexes involved in macromolecular traffic
    • Mattick, J.S., and Aim, R.A. (1995) Common architecture of type IV fimbriae and complexes involved in macromolecular traffic. Trends Microbiol 3: 411-413.
    • (1995) Trends Microbiol , vol.3 , pp. 411-413
    • Mattick, J.S.1    Aim, R.A.2
  • 38
    • 0034618643 scopus 로고    scopus 로고
    • Pilus retraction powers bacterial twitching motility
    • Merz, A.J., So, M., and Sheetz, M.P. (2000) Pilus retraction powers bacterial twitching motility. Nature 407: 98-102.
    • (2000) Nature , vol.407 , pp. 98-102
    • Merz, A.J.1    So, M.2    Sheetz, M.P.3
  • 39
    • 0032434689 scopus 로고    scopus 로고
    • Mutual stabilization of the XcpZ and XcpY components of the secretory apparatus in Pseudomonas aeruginosa
    • Michel, G., Bleves, S., Ball, G., Lazdunski, A., and Filloux, A. (1998) Mutual stabilization of the XcpZ and XcpY components of the secretory apparatus in Pseudomonas aeruginosa. Microbiology 144: 3379-3386.
    • (1998) Microbiology , vol.144 , pp. 3379-3386
    • Michel, G.1    Bleves, S.2    Ball, G.3    Lazdunski, A.4    Filloux, A.5
  • 40
    • 0025292817 scopus 로고
    • Products of three accessory genes, pilB, pilC, and pilD, are required for biogenesis of Pseudomonas aeruginosa pili
    • Nunn, D., Bergman, S., and Lory, S. (1990) Products of three accessory genes, pilB, pilC, and pilD, are required for biogenesis of Pseudomonas aeruginosa pili. J Bacteriol 172: 2911-2919.
    • (1990) J Bacteriol , vol.172 , pp. 2911-2919
    • Nunn, D.1    Bergman, S.2    Lory, S.3
  • 41
    • 0031724115 scopus 로고    scopus 로고
    • Flagellar and twitching motility are necessary for Pseudomonas aeruginosa biofilm development
    • O'Toole, G.A., and Kolter, R. (1998) Flagellar and twitching motility are necessary for Pseudomonas aeruginosa biofilm development. Mol Microbiol 30: 295-304.
    • (1998) Mol Microbiol , vol.30 , pp. 295-304
    • O'Toole, G.A.1    Kolter, R.2
  • 42
    • 0015523228 scopus 로고
    • Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane
    • Osborn, M.J., Gander, J.E., Parisi, E., and Carson, J. (1972) Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane. J Biol Chem 247: 3962-3972.
    • (1972) J Biol Chem , vol.247 , pp. 3962-3972
    • Osborn, M.J.1    Gander, J.E.2    Parisi, E.3    Carson, J.4
  • 43
    • 0028242862 scopus 로고
    • Molecular characterization of PulE, a protein required for pullulanase secretion
    • Possot, O., and Pugsley, A.P. (1994) Molecular characterization of PulE, a protein required for pullulanase secretion. Mol Microbiol 12: 287-299.
    • (1994) Mol Microbiol , vol.12 , pp. 287-299
    • Possot, O.1    Pugsley, A.P.2
  • 44
    • 0034034763 scopus 로고    scopus 로고
    • Multiple interactions between pullulanase secreton components involved in stabilization and cytoplasmic membrane association of PuIE
    • Possot, O.M., Vignon, G., Bomchil, N., Ebel, F., and Pugsley, A.P. (2000) Multiple interactions between pullulanase secreton components involved in stabilization and cytoplasmic membrane association of PuIE. J Bacteriol 182: 2142-2152.
    • (2000) J Bacteriol , vol.182 , pp. 2142-2152
    • Possot, O.M.1    Vignon, G.2    Bomchil, N.3    Ebel, F.4    Pugsley, A.P.5
  • 45
    • 0027450561 scopus 로고
    • The complete general secretory pathway in Gram-negative bacteria
    • Pugsley, A.P. (1993) The complete general secretory pathway in Gram-negative bacteria. Microbiol Rev 57: 50-108.
    • (1993) Microbiol Rev , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 46
    • 0033546401 scopus 로고    scopus 로고
    • Assembly of the type II secretion machinery of Erwinia chrysanthemi: Direct interaction and associated conformational change between OutE, the putative ATP-binding component and the membrane protein OutL
    • Py, B., Loiseau, L., and Barras, F. (1999) Assembly of the type II secretion machinery of Erwinia chrysanthemi: Direct interaction and associated conformational change between OutE, the putative ATP-binding component and the membrane protein OutL. J Mol Biol 289: 659-670.
    • (1999) J Mol Biol , vol.289 , pp. 659-670
    • Py, B.1    Loiseau, L.2    Barras, F.3
  • 47
    • 0035065972 scopus 로고    scopus 로고
    • An inner membrane platform in the type II secretion machinery of Gram-negative bacteria
    • Py, B., Loiseau, L., and Barras, F. (2001) An inner membrane platform in the type II secretion machinery of Gram-negative bacteria. EMBO Rep 2: 244-248.
    • (2001) EMBO Rep , vol.2 , pp. 244-248
    • Py, B.1    Loiseau, L.2    Barras, F.3
  • 48
    • 0029904580 scopus 로고    scopus 로고
    • BfpB, an outer membrane lipoprotein required for the biogenesis of bundle-forming pili in enteropathogenic Escherichia coli
    • Ramer, S.W., Bieber, D., and Schoolnik, G.K. (1996) BfpB, an outer membrane lipoprotein required for the biogenesis of bundle-forming pili in enteropathogenic Escherichia coli. J Bacteriol 178: 6555-6563.
    • (1996) J Bacteriol , vol.178 , pp. 6555-6563
    • Ramer, S.W.1    Bieber, D.2    Schoolnik, G.K.3
  • 49
    • 0036279961 scopus 로고    scopus 로고
    • The type IV pilus assembly complex: Biogenic interactions among the bundle-forming pilus proteins of enteropathogenic Escherichia coli
    • Ramer, S.W., Schoolnik, G.K., Wu, C.-Y., Hwang, J., Schmidt, S.A., and Bieber, D. (2002) The type IV pilus assembly complex: biogenic interactions among the bundle-forming pilus proteins of enteropathogenic Escherichia coli. J Bacteriol 184: 3457-3465.
    • (2002) J Bacteriol , vol.184 , pp. 3457-3465
    • Ramer, S.W.1    Schoolnik, G.K.2    Wu, C.-Y.3    Hwang, J.4    Schmidt, S.A.5    Bieber, D.6
  • 50
    • 0028979820 scopus 로고
    • Role of pili and the phase-variable PilC protein in natural competence for transformation of Neisseria gonorrhoeae
    • Rudel, T., Facius, D., Barten, R., Scheuerpflug, I., Nonnenmacher, E., and Meyer, T.F. (1995) Role of pili and the phase-variable PilC protein in natural competence for transformation of Neisseria gonorrhoeae. Proc Natl Acad Sci USA 92: 7986-7990.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7986-7990
    • Rudel, T.1    Facius, D.2    Barten, R.3    Scheuerpflug, I.4    Nonnenmacher, E.5    Meyer, T.F.6
  • 51
    • 0035029580 scopus 로고    scopus 로고
    • Biology of type II secretion
    • Sandkvist, M. (2001) Biology of type II secretion. Mol Micro 40: 271-283.
    • (2001) Mol Micro , vol.40 , pp. 271-283
    • Sandkvist, M.1
  • 52
    • 0029060583 scopus 로고
    • Interaction between the autokinase EpsE and EpsL in the cytoplasmic membrane is required for extracellular secretion in Vibrio cholerae
    • Sandkvist, M., Bagdasarian, M., Howard, S.P., and DiRita, V.J. (1995) Interaction 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
  • 53
    • 0032909439 scopus 로고    scopus 로고
    • Direct interaction of the EpsL and EpsM proteins of the general secretion apparatus in Vibrio cholerae
    • Sandkvist, M., Hough, L.P., Bagdasarian, M.M., and Bagdasarian, M. (1999) Direct interaction of the EpsL and EpsM proteins of the general secretion apparatus in Vibrio cholerae. J Bacteriol 181: 3129-3135.
    • (1999) J Bacteriol , vol.181 , pp. 3129-3135
    • Sandkvist, M.1    Hough, L.P.2    Bagdasarian, M.M.3    Bagdasarian, M.4
  • 54
    • 0033968224 scopus 로고    scopus 로고
    • Two regions of EpsL involved in species-specific protein-protein interactions with EpsE and EpsM of the general secretion pathway in Vibrio cholerae
    • Sandkvist, M., Keith, J.M., Bagdasarian, M., and Howard, S.P. (2000) Two regions of EpsL involved in species-specific protein-protein interactions with EpsE and EpsM of the general secretion pathway in Vibrio cholerae. J Bacteriol 182: 742-748.
    • (2000) J Bacteriol , vol.182 , pp. 742-748
    • Sandkvist, M.1    Keith, J.M.2    Bagdasarian, M.3    Howard, S.P.4
  • 55
    • 0034657719 scopus 로고    scopus 로고
    • Pilus formation and protein secretion by the same machinery in Escherichia coli
    • Sauvonnet, N., Vignon, G., Pugsley, A.P., and Gounon, P. (2000) Pilus formation and protein secretion by the same machinery in Escherichia coli. EMBO J 19: 2221-2228.
    • (2000) EMBO J , vol.19 , pp. 2221-2228
    • Sauvonnet, N.1    Vignon, G.2    Pugsley, A.P.3    Gounon, P.4
  • 56
    • 0021274267 scopus 로고
    • Distinctive patterns of adherence of enteropathogenic Escherichia coli to HeLa cells
    • Scaletsky, I.C.A., Silva, M.L.M., and Trabulsi, L.R. (1984) Distinctive patterns of adherence of enteropathogenic Escherichia coli to HeLa cells. Infect Immun 45: 534-536.
    • (1984) Infect Immun , vol.45 , pp. 534-536
    • Scaletsky, I.C.A.1    Silva, M.L.M.2    Trabulsi, L.R.3
  • 57
    • 0023780725 scopus 로고
    • DNA transformation leads to pilin antigenic variation in Neisseria gonorrhoeae
    • Seifert, H.S., Ajioka, R.S., Marchal, C., Sparling, P.F., and So, M. (1988) DNA transformation leads to pilin antigenic variation in Neisseria gonorrhoeae. Nature 336: 392-395.
    • (1988) Nature , vol.336 , pp. 392-395
    • Seifert, H.S.1    Ajioka, R.S.2    Marchal, C.3    Sparling, P.F.4    So, M.5
  • 58
    • 0027535139 scopus 로고
    • Cloning and characterization of the bundle-forming pilin gene of enteropathogenic Escherichia coli and its distribution in Salmonella serotypes
    • Sohel, I., Puente, J.L., Murray, W.J., Vuopio-Varkila, J., and Schoolnik, G.K. (1993) Cloning and characterization of the bundle-forming pilin gene of enteropathogenic Escherichia coli and its distribution in Salmonella serotypes. Mol Micro 7: 563-575.
    • (1993) Mol Micro , vol.7 , pp. 563-575
    • Sohel, I.1    Puente, J.L.2    Murray, W.J.3    Vuopio-Varkila, J.4    Schoolnik, G.K.5
  • 59
    • 0029975939 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli: Identification of a gene cluster coding for bundle-forming pilus morphogenesis
    • Sohel, I., Puente, J.L., Ramer, S.W., Bieber, D., Wu, C.-Y., and Schoolnik, G.K. (1996) Enteropathogenic Escherichia coli: identification of a gene cluster coding for bundle-forming pilus morphogenesis. J Bacteriol 178: 2613-2628.
    • (1996) J Bacteriol , vol.178 , pp. 2613-2628
    • Sohel, I.1    Puente, J.L.2    Ramer, S.W.3    Bieber, D.4    Wu, C.-Y.5    Schoolnik, G.K.6
  • 60
    • 0022526190 scopus 로고
    • The biology of natural transformation
    • Stewart, G.J., and Carlson, C.A. (1986) The biology of natural transformation. Annu Rev Microbiol 40: 211-235.
    • (1986) Annu Rev Microbiol , vol.40 , pp. 211-235
    • Stewart, G.J.1    Carlson, C.A.2
  • 61
    • 0029879021 scopus 로고    scopus 로고
    • A cluster of fourteen genes from enteropathogenic Escherichia coli is sufficient for biogenesis of a type IV pilus
    • Stone, K.D., Zhang, H.-Z., Carlson, L.K., and Donnenberg, M.S. (1996) A cluster of fourteen genes from enteropathogenic Escherichia coli is sufficient for biogenesis of a type IV pilus. Mol Microbiol 20: 325-337.
    • (1996) Mol Microbiol , vol.20 , pp. 325-337
    • Stone, K.D.1    Zhang, H.-Z.2    Carlson, L.K.3    Donnenberg, M.S.4
  • 62
    • 0027385590 scopus 로고
    • Structure-function and biogenesis of the type IV pili
    • Strom, M.S., and Lory, S. (1993) Structure-function and biogenesis of the type IV pili. Annu Rev Microbiol 47: 565-596.
    • (1993) Annu Rev Microbiol , vol.47 , pp. 565-596
    • Strom, M.S.1    Lory, S.2
  • 63
    • 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., Nunn, D.N., and Lory, S. (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
  • 64
    • 0029030966 scopus 로고
    • Identification and characterization of pilG, a highly conserved pilus-assembly gene in pathogenic Neisseria
    • Tønjum, T., Freitag, N.E., Namork, E., and Koomey, M. (1995) Identification and characterization of pilG, a highly conserved pilus-assembly gene in pathogenic Neisseria. Mol Microbiol 16: 451-464.
    • (1995) Mol Microbiol , vol.16 , pp. 451-464
    • Tønjum, T.1    Freitag, N.E.2    Namork, E.3    Koomey, M.4
  • 65
    • 0030669210 scopus 로고    scopus 로고
    • The XcpR protein of Pseudomonas aeruginosa dimerizes via its N-terminus
    • Turner, L.R., Olson, J.W., and Lory, S. (1997) The XcpR protein of Pseudomonas aeruginosa dimerizes via its N-terminus. Mol Microbiol 26: 877-887.
    • (1997) Mol Microbiol , vol.26 , pp. 877-887
    • Turner, L.R.1    Olson, J.W.2    Lory, S.3
  • 66
    • 0025954297 scopus 로고
    • Localized adherence by enteropathogenic Escherichia coli is an inducible phenotype associated with the expression of new outer membrane proteins
    • Vuopio-Varkila, J., and Schoolnik, G.K. (1991) Localized adherence by enteropathogenic Escherichia coli is an inducible phenotype associated with the expression of new outer membrane proteins. J Exp Med 174: 1167-1177.
    • (1991) J Exp Med , vol.174 , pp. 1167-1177
    • Vuopio-Varkila, J.1    Schoolnik, G.K.2
  • 67
    • 0032949378 scopus 로고    scopus 로고
    • Type IV pili and cell motility
    • Wall, D., and Kaiser, D. (1999) Type IV pili and cell motility. Mol Microbiol 32: 1-10.
    • (1999) Mol Microbiol , vol.32 , pp. 1-10
    • Wall, D.1    Kaiser, D.2
  • 68
    • 0025878130 scopus 로고
    • Characterisation of a Pseudomonas aeruginosa twitching motility gene and evidence for a specialized protein export system widespread in eubacteria
    • Whitchurch, C.B., Hobbs, M., Livingston, S.P., Krishnapillai, V., and Mattick, J.S. (1991) Characterisation of a Pseudomonas aeruginosa twitching motility gene and evidence for a specialized protein export system widespread in eubacteria. Gene 101: 33-44.
    • (1991) Gene , vol.101 , pp. 33-44
    • Whitchurch, C.B.1    Hobbs, M.2    Livingston, S.P.3    Krishnapillai, V.4    Mattick, J.S.5
  • 69
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman, T., Williston, S., Brandts, J.F., and Lin, L.N. (1989) Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal Biochem 179: 131-137.
    • (1989) Anal Biochem , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 70
    • 0031824719 scopus 로고    scopus 로고
    • PilT mutations lead to simultaneous defects in competence for natural transformation and twitching motility in piliated Neisseria gonorrhoeae
    • Wolfgang, M., Lauer, P., Park, H.S., Brossay, L., Hébert, J., and Koomey, M. (1998) PilT mutations lead to simultaneous defects in competence for natural transformation and twitching motility in piliated Neisseria gonorrhoeae. Mol Microbiol 29: 321-330.
    • (1998) Mol Microbiol , vol.29 , pp. 321-330
    • Wolfgang, M.1    Lauer, P.2    Park, H.S.3    Brossay, L.4    Hébert, J.5    Koomey, M.6
  • 71
    • 0034406525 scopus 로고    scopus 로고
    • Components and dynamics of fiber formation define a ubiquitous biogenesis pathway for bacterial pili
    • Wolfgang, M., van Putten, J.P., Hayes, S.F., Dorward, D., and Koomey, M. (2000) Components and dynamics of fiber formation define a ubiquitous biogenesis pathway for bacterial pili. EMBO J 19: 6408-6418.
    • (2000) EMBO J , vol.19 , pp. 6408-6418
    • Wolfgang, M.1    Van Putten, J.P.2    Hayes, S.F.3    Dorward, D.4    Koomey, M.5
  • 72
    • 0032963612 scopus 로고    scopus 로고
    • Twelve pil genes are required for biogenesis of the R64 thin pilus
    • Yoshida, T., Kim, S.R., and Komano, T. (1999) Twelve pil genes are required for biogenesis of the R64 thin pilus. J Bacteriol 181: 2038-2043.
    • (1999) J Bacteriol , vol.181 , pp. 2038-2043
    • Yoshida, T.1    Kim, S.R.2    Komano, T.3
  • 73
    • 0028117722 scopus 로고
    • A plasmid-encoded prepilin peptidase gene from enteropathogenic Escherichia coli
    • Zhang, H.-Z., Lory, S., and Donnenberg, M.S. (1994) A plasmid-encoded prepilin peptidase gene from enteropathogenic Escherichia coli. J Bacteriol 176: 6885-6891.
    • (1994) J Bacteriol , vol.176 , pp. 6885-6891
    • Zhang, H.-Z.1    Lory, S.2    Donnenberg, M.S.3


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