메뉴 건너뛰기




Volumn 185, Issue 11, 2003, Pages 3416-3428

Type IV-like pili formed by the type II secreton: Specificity, composition, bundling, polar localization, and surface presentation of peptides

Author keywords

[No Author keywords available]

Indexed keywords

GENE PRODUCT; PROTEIN GSPG; PROTEIN PULG; PROTEIN SECRETON; PULLULANASE; UNCLASSIFIED DRUG;

EID: 0037853309     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.11.3416-3428.2003     Document Type: Article
Times cited : (114)

References (55)
  • 1
    • 0036173113 scopus 로고    scopus 로고
    • A novel type II secretion system in Pseudomonas aeruginosa
    • Ball, G., E. Durand, A. Lazdunski, and A. Filloux. 2002. A novel type II secretion system in Pseudomonas aeruginosa. Mol. Microbiol. 43:475-485.
    • (2002) Mol. Microbiol. , vol.43 , pp. 475-485
    • Ball, G.1    Durand, E.2    Lazdunski, A.3    Filloux, A.4
  • 2
    • 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
  • 3
    • 0031983616 scopus 로고    scopus 로고
    • Formation of oligomeric rings by XcpQ and PilQ, which are involved in protein transport across the outer membrane of Pseudomonas aeruginosa
    • Bitter, W., M. Koster, M. Latijnhouwers, H. de Cock, and J. Tommassen. 1998. Formation of oligomeric rings by XcpQ and PilQ, which are involved in protein transport across the outer membrane of Pseudomonas aeruginosa. Mol. Microbiol. 27:209-219.
    • (1998) Mol. Microbiol. , vol.27 , pp. 209-219
    • Bitter, W.1    Koster, M.2    Latijnhouwers, M.3    De Cock, H.4    Tommassen, J.5
  • 4
    • 0031983197 scopus 로고    scopus 로고
    • The secretion apparatus of Pseudomonas aeruginosa: Identification of a fifth pseudopilin
    • Bleves, S., A. Lazdunski, J. Tommassen, and A. Filloux. 1998. The secretion apparatus of Pseudomonas aeruginosa: identification of a fifth pseudopilin, XcpX. Mol. Microbiol. 27:31-40.
    • (1998) XcpX. Mol. Microbiol. , vol.27 , pp. 31-40
    • Bleves, S.1    Lazdunski, A.2    Tommassen, J.3    Filloux, A.4
  • 5
    • 0035957511 scopus 로고    scopus 로고
    • The PDZ domain of OutC and the N-terminal region of OutD determine the secretion specificity of the type II out pathway of Erwinia chrysanthemi
    • Bouley, J., G. Condemine, and V. E. Shevchik. 2001. The PDZ domain of OutC and the N-terminal region of OutD determine the secretion specificity of the type II out pathway of Erwinia chrysanthemi. J. Mol. Biol. 27:205-219.
    • (2001) J. Mol. Biol. , vol.27 , pp. 205-219
    • Bouley, J.1    Condemine, G.2    Shevchik, V.E.3
  • 6
    • 0028094123 scopus 로고
    • Immunoaffinity purification of FLAG epitope-tagged bacterial alkaline phosphatase using a novel monoclonal antibody and a peptide elution
    • Brizzard, B. L., R. G. Chubert, and D. L. Vizard. 1994. Immunoaffinity purification of FLAG epitope-tagged bacterial alkaline phosphatase using a novel monoclonal antibody and a peptide elution. BioTechniques 16:730-735.
    • (1994) BioTechniques , vol.16 , pp. 730-735
    • Brizzard, B.L.1    Chubert, R.G.2    Vizard, D.L.3
  • 7
    • 0034973703 scopus 로고    scopus 로고
    • Analysis of the PilQ secretin from Neisseria meningitidis by transmission electron microscopy reveals a dodecameric quaternary structure
    • Collins, R. F., L. Davidsen, J. P. Derrick, R. C. Ford, and T. Tonjum. 2001. Analysis of the PilQ secretin from Neisseria meningitidis by transmission electron microscopy reveals a dodecameric quaternary structure. J. Bacteriol. 183:3825-3832.
    • (2001) J. Bacteriol. , vol.183 , pp. 3825-3832
    • Collins, R.F.1    Davidsen, L.2    Derrick, J.P.3    Ford, R.C.4    Tonjum, T.5
  • 8
    • 0023375651 scopus 로고
    • Export and secretion of the lipoprotein pullulanase by Klebsiella pneumoniae
    • d'Enfert, C., C. Chapon, and A. P. Pugsley. 1987. Export and secretion of the lipoprotein pullulanase by Klebsiella pneumoniae. Mol. Microbiol. 1:107-116.
    • (1987) Mol. Microbiol. , vol.1 , pp. 107-116
    • D'Enfert, C.1    Chapon, C.2    Pugsley, A.P.3
  • 9
    • 0024341985 scopus 로고
    • Protein secretion by gram-negative bacteria: Characterization of two membrane proteins required for pullulanase secretion by Escherichia coli K-12
    • d'Enfert, C., I. Reyss, C. Wandersman, and A. P. Pugsley. 1989. Protein secretion by gram-negative bacteria: characterization of two membrane proteins required for pullulanase secretion by Escherichia coli K-12. J. Biol. Chem. 264:17462-17468.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17462-17468
    • D'Enfert, C.1    Reyss, I.2    Wandersman, C.3    Pugsley, A.P.4
  • 10
    • 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
  • 11
    • 0028046269 scopus 로고
    • Permissible peptide insertions surrounding the signal peptide-mature protein junction of the ClpG prepilin: CS31A fimbriae of Escherichia coli as carriers of foreign sequences
    • Der Vartarian, M., M. C. Mechin, B. Jaffeux, Y. Bertin, I. Felix, and B. Gaillard-Martinie. 1994. Permissible peptide insertions surrounding the signal peptide-mature protein junction of the ClpG prepilin: CS31A fimbriae of Escherichia coli as carriers of foreign sequences. Gene 148:23-32.
    • (1994) Gene , vol.148 , pp. 23-32
    • Der Vartarian, M.1    Mechin, M.C.2    Jaffeux, B.3    Bertin, Y.4    Felix, I.5    Gaillard-Martinie, B.6
  • 12
    • 0031696843 scopus 로고    scopus 로고
    • Initial binding of Shiga toxin-producing Escherichia coli to host cells and subsequent induction of actin rearrangements depend on filamentous EspA-containing surface appendages
    • Ebel, F., T. Podzadel, M. Rohde, A. U. Kresse, S. Krämer, C. Deibel, C. A. Guzman, and T. Chakraborty. 1998. Initial binding of Shiga toxin-producing Escherichia coli to host cells and subsequent induction of actin rearrangements depend on filamentous EspA-containing surface appendages. Mol. Microbiol. 30:147-161.
    • (1998) Mol. Microbiol. , vol.30 , pp. 147-161
    • Ebel, F.1    Podzadel, T.2    Rohde, M.3    Kresse, A.U.4    Krämer, S.5    Deibel, C.6    Guzman, C.A.7    Chakraborty, T.8
  • 13
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product
    • Evans, G. I., G. K. Lewis, G. Ramsay, and J. M. Bishop. 1985. Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell. Biol. 5:3610-3616.
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3610-3616
    • Evans, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 14
    • 0034671617 scopus 로고    scopus 로고
    • Expression of the endogenous type II secretion pathway in Escherichia coli leads to chitinase secretion
    • Francetic, O., D. Belin, C. Badaut, and A. P. Pugsley. 2000. Expression of the endogenous type II secretion pathway in Escherichia coli leads to chitinase secretion. EMBO J. 19:6697-6703.
    • (2000) EMBO J. , vol.19 , pp. 6697-6703
    • Francetic, O.1    Belin, D.2    Badaut, C.3    Pugsley, A.P.4
  • 15
    • 0030586757 scopus 로고    scopus 로고
    • A rapid screening procedure to identify mini-Tn10 insertion mutants of Escherichia coli K-12 with altered adhesion properties
    • Genevaux, P., S. Muller, and P. Bauda. 1996. A rapid screening procedure to identify mini-Tn10 insertion mutants of Escherichia coli K-12 with altered adhesion properties. FEMS Microbiol. Lett. 142:27-30.
    • (1996) FEMS Microbiol. Lett. , vol.142 , pp. 27-30
    • Genevaux, P.1    Muller, S.2    Bauda, P.3
  • 16
    • 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 J. S. Mattick. 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, J.S.2
  • 17
    • 0029927929 scopus 로고    scopus 로고
    • Complementation of deletion mutations in a cloned functional cluster of Erwinia chrysanthemi out genes with Erwinia carotovora out homologs reveals OutC and OutD as candidate gatekeepers of species-specific secretion of proteins via the type II pathway
    • Lindeberg, M., G. P. C. Salmond, and A. Collmer. 1996. Complementation of deletion mutations in a cloned functional cluster of Erwinia chrysanthemi out genes with Erwinia carotovora out homologs reveals OutC and OutD as candidate gatekeepers of species-specific secretion of proteins via the type II pathway. Mol. Microbiol. 20:175-190.
    • (1996) Mol. Microbiol. , vol.20 , pp. 175-190
    • Lindeberg, M.1    Salmond, G.P.C.2    Collmer, A.3
  • 18
    • 0022921901 scopus 로고
    • Mutations in a new chromosomal gene of Escherichia coli K-12, pcnB, reduce plasmid copy number of pBR322 and its derivatives
    • Lopilato, J., S. Bortner, and J. Beckwith. 1986. Mutations in a new chromosomal gene of Escherichia coli K-12, pcnB, reduce plasmid copy number of pBR322 and its derivatives. Mol. Gen. Genet. 205:285-290.
    • (1986) Mol. Gen. Genet. , vol.205 , pp. 285-290
    • Lopilato, J.1    Bortner, S.2    Beckwith, J.3
  • 19
    • 0034618643 scopus 로고    scopus 로고
    • Pilus retraction powers bacterial twitching motility
    • Merz, A. J., M. So, and M. P. Sheetz. 2000. Pilus retraction powers bacterial twitching motility. Nature 407:98-101.
    • (2000) Nature , vol.407 , pp. 98-101
    • Merz, A.J.1    So, M.2    Sheetz, M.P.3
  • 20
    • 0022365856 scopus 로고
    • Characterization and expression of the structural gene for pullulanase, a maltose-inducible secreted protein of Klebsiella pneumoniae
    • Michaelis, S., C. Chapon, C. d'Enfert, A. P. Pugsley, and M. Schwartz. 1985. Characterization and expression of the structural gene for pullulanase, a maltose-inducible secreted protein of Klebsiella pneumoniae. J. Bacteriol. 164:633-638.
    • (1985) J. Bacteriol. , vol.164 , pp. 633-638
    • Michaelis, S.1    Chapon, C.2    D'Enfert, C.3    Pugsley, A.P.4    Schwartz, M.5
  • 21
  • 23
    • 0034657105 scopus 로고    scopus 로고
    • Domain structure of secretin PulD revealed by limited proteolysis and electron microscopy
    • Nouwen, N., H. Stahlberg, A. P. Pugsley, and A. Engel. 2000. Domain structure of secretin PulD revealed by limited proteolysis and electron microscopy. EMBO J. 19:2229-2236.
    • (2000) EMBO J. , vol.19 , pp. 2229-2236
    • Nouwen, N.1    Stahlberg, H.2    Pugsley, A.P.3    Engel, A.4
  • 24
    • 0033214349 scopus 로고    scopus 로고
    • Bacterial type II protein export and pilus biogenesis: More than just homologies?
    • Nunn, D. 1999. Bacterial type II protein export and pilus biogenesis: more than just homologies? Trends Cell Biol. 9:402-408.
    • (1999) Trends Cell Biol. , vol.9 , pp. 402-408
    • Nunn, D.1
  • 25
    • 0027273016 scopus 로고
    • Cleavage, methylation, and localization of the Pseudomonas aeruginosa export proteins XcpT, -U, -V, and -W
    • Nunn, D. N., and S. Lory. 1993. Cleavage, methylation, and localization of the Pseudomonas aeruginosa export proteins XcpT, -U, -V, and -W. J. Bacteriol. 4375-4382.
    • (1993) J. Bacteriol. , pp. 4375-4382
    • Nunn, D.N.1    Lory, S.2
  • 26
    • 0031724115 scopus 로고    scopus 로고
    • Flagellar and twitching motility are necessary for Pseudomonas aeruginosa biofilm development
    • O'Toole, G. A., and R. Kolter. 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
  • 27
    • 0024041477 scopus 로고
    • The expression of mutant pilins in Pseudomonas aeruginosa: Fifth position glutamate affects pilin methylation
    • Pasloske, B. L., and W. Paranchych. 1988. The expression of mutant pilins in Pseudomonas aeruginosa: fifth position glutamate affects pilin methylation. Mol. Microbiol. 2:489-495.
    • (1988) Mol. Microbiol. , vol.2 , pp. 489-495
    • Pasloske, B.L.1    Paranchych, W.2
  • 28
    • 0024598452 scopus 로고
    • Assembly of mutant pilins in Pseudomonas aeruginosa: Formation of pili composed of heterologous subunits
    • Pasloske, B. L., D. G. Scraba, and W. Paranchych. 1989. Assembly of mutant pilins in Pseudomonas aeruginosa: formation of pili composed of heterologous subunits. J. Bacteriol. 171:2142-2147.
    • (1989) J. Bacteriol. , vol.171 , pp. 2142-2147
    • Pasloske, B.L.1    Scraba, D.G.2    Paranchych, W.3
  • 29
    • 0032563102 scopus 로고    scopus 로고
    • Amino acid substitutions in PilD, a bifunctional enzyme of Pseudomonas aeruginosa: Effect on leader peptidase and N-methyltransferase activities in vitro and in vivo
    • Pepe, J. C., and S. Lory. 1998. Amino acid substitutions in PilD, a bifunctional enzyme of Pseudomonas aeruginosa: effect on leader peptidase and N-methyltransferase activities in vitro and in vivo. J. Biol. Chem. 273:19120-19129.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19120-19129
    • Pepe, J.C.1    Lory, S.2
  • 30
    • 0031005016 scopus 로고    scopus 로고
    • Energy requirement for pullulanase secretion by the main terminal branch of the general secretory pathway
    • Possot, O., L. Letellier, and A. P. Pugsley. 1997. Energy requirement for pullulanase secretion by the main terminal branch of the general secretory pathway. Mol. Microbiol. 24:457-464.
    • (1997) Mol. Microbiol. , vol.24 , pp. 457-464
    • Possot, O.1    Letellier, L.2    Pugsley, A.P.3
  • 31
    • 0034034763 scopus 로고    scopus 로고
    • Multiple interactions between pullulanase secreton components involved in stabilization and cytoplasmic membrane association of PulE
    • Possot, O., G. Vignon, N. Bomchil, F. Ebel, and A. P. Pugsley. 2000. Multiple interactions between pullulanase secreton components involved in stabilization and cytoplasmic membrane association of PulE. J. Bacteriol. 182:2142-2152.
    • (2000) J. Bacteriol. , vol.182 , pp. 2142-2152
    • Possot, O.1    Vignon, G.2    Bomchil, N.3    Ebel, F.4    Pugsley, A.P.5
  • 32
    • 0031754332 scopus 로고    scopus 로고
    • Genetic analysis of Escherichia coli biofilm formation: Roles of flagella motility, chemotaxis and type I pili
    • Pratt, L. A., and K. Kolter. 1998. Genetic analysis of Escherichia coli biofilm formation: roles of flagella motility, chemotaxis and type I pili. Mol. Microbiol. 30:285-293.
    • (1998) Mol. Microbiol. , vol.30 , pp. 285-293
    • Pratt, L.A.1    Kolter, K.2
  • 33
    • 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
  • 34
    • 0029899207 scopus 로고    scopus 로고
    • Multimers of the precursor of a type IV pilin-like component of the general secretory pathway are unrelated to pili
    • Pugsley, A. P. 1996. Multimers of the precursor of a type IV pilin-like component of the general secretory pathway are unrelated to pili. Mol. Microbiol. 20:1235-1245.
    • (1996) Mol. Microbiol. , vol.20 , pp. 1235-1245
    • Pugsley, A.P.1
  • 35
    • 0027337742 scopus 로고
    • Processing and methylation of PulG, a pilin-like component of the general secretory pathway of Klebsiella oxytoca
    • Pugsley, A. P. 1993. Processing and methylation of PulG, a 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
  • 36
    • 0035143586 scopus 로고    scopus 로고
    • Disulphide bond formation in secreton component PulK provides a possible explanation for the role of DsbA in pullulanase secretion
    • Pugsley, A. P., N. Bayan, and N. Sauvonnet. 2001. Disulphide bond formation in secreton component PulK provides a possible explanation for the role of DsbA in pullulanase secretion. J. Bacteriol. 183:1312-1319.
    • (2001) J. Bacteriol. , vol.183 , pp. 1312-1319
    • Pugsley, A.P.1    Bayan, N.2    Sauvonnet, N.3
  • 37
    • 0026605350 scopus 로고
    • An enzyme with type IV prepilin peptidase activity is required to process a component 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 a component 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
  • 38
    • 0027358573 scopus 로고
    • The general secretory pathway of Klebsiella oxytoca: No evidence for relocalization or assembly of pilin-like PulG protein into a multiprotein complex
    • Pugsley, A. P., and O. Possot. 1993. The general secretory pathway of Klebsiella oxytoca: no evidence for relocalization or assembly of pilin-like PulG protein into a multiprotein complex. Mol. Microbiol. 10:665-674.
    • (1993) Mol. Microbiol. , vol.10 , pp. 665-674
    • Pugsley, A.P.1    Possot, O.2
  • 39
    • 0032946345 scopus 로고    scopus 로고
    • Polymeric display of immunogenic epitopes from herpes simplex virus and transmissible gastroenteritis virus surface proteins on an enteroadherent fimbria
    • Rani, D., M. Bayer, and D. Schifferli. 1999. Polymeric display of immunogenic epitopes from herpes simplex virus and transmissible gastroenteritis virus surface proteins on an enteroadherent fimbria. Clin. Diagn. Lab. Immunol. 6:30-40.
    • (1999) Clin. Diagn. Lab. Immunol. , vol.6 , pp. 30-40
    • Rani, D.1    Bayer, M.2    Schifferli, D.3
  • 40
    • 0025293866 scopus 로고
    • Five additional genes in the pulC-O operon of the gram-negative bacterium Klebsiella oxytoca UNF5023 that are required for pullulanase secretion
    • Reyss, I., and A. P. Pugsley. 1990. Five additional genes in the pulC-O operon of the gram-negative bacterium Klebsiella oxytoca UNF5023 that are required for pullulanase secretion. Mol. Gen. Genet. 222:176-184.
    • (1990) Mol. Gen. Genet. , vol.222 , pp. 176-184
    • Reyss, I.1    Pugsley, A.P.2
  • 42
    • 0035077415 scopus 로고    scopus 로고
    • Type II secretion is a subset of the PilD-dependent processes that facilitate intracellular infection by Legionella pneumophila
    • Rossier, O., and N. P. Cianciotto. 2001. Type II secretion is a subset of the PilD-dependent processes that facilitate intracellular infection by Legionella pneumophila. Infect. Immun. 69:2092-2098.
    • (2001) Infect. Immun. , vol.69 , pp. 2092-2098
    • Rossier, O.1    Cianciotto, N.P.2
  • 43
    • 0034657719 scopus 로고    scopus 로고
    • Pilus formation and protein secretion by the same machinery in Escherichia coli
    • Sauvonnet, N., G. Vignon, A. P. Pugsley, and P. Gounon. 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
  • 44
    • 0030993971 scopus 로고    scopus 로고
    • A gene cluster related to type II secretion pathway operons of gram-negative bacteria is located on the large plasmid of enterohemorrhagic Escherichia coli O157 strains
    • Schmidt, H., B. Henkel, and H. Karch. 1997. A gene cluster related to type II secretion pathway operons of gram-negative bacteria is located on the large plasmid of enterohemorrhagic Escherichia coli O157 strains. FEMS Microbiol. Lett. 148:265-272.
    • (1997) FEMS Microbiol. Lett. , vol.148 , pp. 265-272
    • Schmidt, H.1    Henkel, B.2    Karch, H.3
  • 45
    • 0029865819 scopus 로고    scopus 로고
    • Molecular interactions between the Strep-tag affinity peptide and its cognate target, streptavidin
    • Schmidt, T. G., J. Koepke, R. Frank, and A. Skerra. 1996. Molecular interactions between the Strep-tag affinity peptide and its cognate target, streptavidin. J. Mol. Biol. 255:753-766.
    • (1996) J. Mol. Biol. , vol.255 , pp. 753-766
    • Schmidt, T.G.1    Koepke, J.2    Frank, R.3    Skerra, A.4
  • 46
    • 0035923586 scopus 로고    scopus 로고
    • Directed polar secretion of protease from single cells of Vibrio cholerae via the type II secretion pathway
    • Scott, M., Z. Dossani, and M. Sandkvist. 2001. Directed polar secretion of protease from single cells of Vibrio cholerae via the type II secretion pathway. Proc. Natl. Acad. Sci. USA 94:13978-13983.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13978-13983
    • Scott, M.1    Dossani, Z.2    Sandkvist, M.3
  • 48
    • 0030911423 scopus 로고    scopus 로고
    • Specific interaction between OutD, an Erwinia chrysanthemi outer membrane protein of the general secretory pathway, and secreted proteins
    • Shevchik, V. E., J. Robert-Badouy, and G. Condemine. 1997. Specific interaction between OutD, an Erwinia chrysanthemi outer membrane protein of the general secretory pathway, and secreted proteins. EMBO J 16:3007-3016.
    • (1997) EMBO J. , vol.16 , pp. 3007-3016
    • Shevchik, V.E.1    Robert-Badouy, J.2    Condemine, G.3
  • 49
    • 0035810950 scopus 로고    scopus 로고
    • Direct observation of extension and retraction of type IV pili
    • Skerker, J. M., and H. C. Berg. 2001. Direct observation of extension and retraction of type IV pili. Proc. Natl. Acad. Sci. USA 98:6901-6904.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6901-6904
    • Skerker, J.M.1    Berg, H.C.2
  • 50
    • 0025978598 scopus 로고
    • Amino acid substitutions in pilin of Pseudomonas aeruginosa: Effect on leader peptide cleavage, amino-terminal methylation, and pilus assembly
    • Strom, M. S., and S. Lory. 1991. Amino acid substitutions in pilin of Pseudomonas aeruginosa: effect on leader peptide cleavage, amino-terminal methylation, and pilus assembly. J. Biol. Chem. 266:1656-1664.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1656-1664
    • Strom, M.S.1    Lory, S.2
  • 51
    • 0024516176 scopus 로고
    • Cloning of DNA sequences encoding foreign peptides and their expression in the K88 pili
    • Thiry, G., A. Clippe, T. Scarcez, and J. Petre. 1989. Cloning of DNA sequences encoding foreign peptides and their expression in the K88 pili. Appl. Environ. Microbiol. 55:984-993.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 984-993
    • Thiry, G.1    Clippe, A.2    Scarcez, T.3    Petre, J.4
  • 52
    • 0032723826 scopus 로고    scopus 로고
    • Steps in the development of a Vibrio cholerae E1 Tor biofilm
    • Watnick, P. I., and R. Kolter. 1999. Steps in the development of a Vibrio cholerae E1 Tor biofilm. Mol. Microbiol. 34:586-595.
    • (1999) Mol. Microbiol. , vol.34 , pp. 586-595
    • Watnick, P.I.1    Kolter, R.2
  • 53
    • 0025878130 scopus 로고
    • Characterization of a Pseudomonas aeruginosa twitching motility gene and evidence for a specialized protein export system widespread in bacteria
    • Whitchurch, C. B., M. Hobbs, S. P. Livingstone, V. Krishnapillai, and J. S. Mattick. 1991. Characterization of a Pseudomonas aeruginosa twitching motility gene and evidence for a specialized protein export system widespread in bacteria. Gene 101:33-44.
    • (1991) Gene , vol.101 , pp. 33-44
    • Whitchurch, C.B.1    Hobbs, M.2    Livingstone, S.P.3    Krishnapillai, V.4    Mattick, J.S.5
  • 54
    • 0032409987 scopus 로고    scopus 로고
    • Suppression of an absolute defect in type IV pilus biogenesis by loss-of-function mutations in pilT, a twitching motility gene in Neisseria gonorrhoeae
    • Wolfgang, M., H.-S. Park, S. F. Hayes, J. P. M. van Putten, and M. Koomey. 1998. Suppression of an absolute defect in type IV pilus biogenesis by loss-of-function mutations in pilT, a twitching motility gene in Neisseria gonorrhoeae. Proc. Natl. Acad. Sci. USA 95:14973-14978.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14973-14978
    • Wolfgang, M.1    Park, H.-S.2    Hayes, S.F.3    Van Putten, J.P.M.4    Koomey, M.5
  • 55
    • 0034406525 scopus 로고    scopus 로고
    • Components and dynamics of fiber formation define a ubiquitous biogenesis pathway for bacterial pili
    • Wolfgang, M., J. P. M. van Putten, S. F. Hayes, D. Dorward, and M. Koomey. 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.M.2    Hayes, S.F.3    Dorward, D.4    Koomey, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.