메뉴 건너뛰기




Volumn 54, Issue 3, 2004, Pages 647-664

Structure and assembly of the pseudopilin PulG

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; PILIN; PROTEIN PRECURSOR; PROTEIN SUBUNIT; PSEUDOPILIN PULG; PULLULANASE; UNCLASSIFIED DRUG;

EID: 7644237002     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2004.04307.x     Document Type: Article
Times cited : (94)

References (64)
  • 1
    • 0025778670 scopus 로고
    • Construction and properties of a family of pACYC184-derived cloning vectors compatible with pBR322 and its derivatives
    • Bartolomé, B., Jubete, Y., Martinez, E., and de la Cruz, F. (1991) Construction and properties of a family of pACYC184-derived cloning vectors compatible with pBR322 and its derivatives. Gene 102: 75-78.
    • (1991) Gene , vol.102 , pp. 75-78
    • Bartolomé, B.1    Jubete, Y.2    Martinez, E.3    De La Cruz, F.4
  • 2
    • 0025319892 scopus 로고
    • Morphogenic expression of Moraxella bovis fimbriae (pili) in Pseudomonas aeruginosa
    • Beard, M.K., Mattick, J.S., Moor, M.R., Marrs, C.F., and Egerton, J.R. (1990) Morphogenic expression of Moraxella bovis fimbriae (pili) in Pseudomonas aeruginosa. J Bacteriol 172: 2601-2607.
    • (1990) J Bacteriol , vol.172 , pp. 2601-2607
    • Beard, M.K.1    Mattick, J.S.2    Moor, M.R.3    Marrs, C.F.4    Egerton, J.R.5
  • 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., Koster, M., Latijnhouwers, M., de Cock, H., and Tommassen, J. (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
    • 0033579546 scopus 로고    scopus 로고
    • The C-terminal domain of the Pseudomonas secretin XcpQ forms oligomeric rings with pore activity
    • Brok, R., Van Gelder, P., Winterhalter, M., Ziese, U., Koster, A.J., de Cock, H., et al. (1999) The C-terminal domain of the Pseudomonas secretin XcpQ forms oligomeric rings with pore activity. J Mol Biol 294: 1169-1179.
    • (1999) J Mol Biol , vol.294 , pp. 1169-1179
    • Brok, R.1    Van Gelder, P.2    Winterhalter, M.3    Ziese, U.4    Koster, A.J.5    De Cock, H.6
  • 5
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project (1994) The CCP4 suite: programs for protein crystallography. Acta Cryst D50: 760-763.
    • (1994) Acta Cryst , vol.D50 , pp. 760-763
  • 6
    • 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., Davidsen, L., Derrick, J.P., Ford, R.C., and Tonjum, T. (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
  • 7
    • 0037389450 scopus 로고    scopus 로고
    • Three-dimensional structure of the Neisseria meningitidis secretin PilQ determined from negative-stain transmission electron microscopy
    • Collins, R.F., Ford, R.C., Kitmitto, A., Olsen, R.O., Tonjum, T., and Derrick, J.P. (2003) Three-dimensional structure of the Neisseria meningitidis secretin PilQ determined from negative-stain transmission electron microscopy. J Bacteriol 185: 2611-2617.
    • (2003) J Bacteriol , vol.185 , pp. 2611-2617
    • Collins, R.F.1    Ford, R.C.2    Kitmitto, A.3    Olsen, R.O.4    Tonjum, T.5    Derrick, J.P.6
  • 8
    • 12444272635 scopus 로고    scopus 로고
    • Type IV pilin structure and assembly. X-ray and EM analyses of Vibrio cholerae toxin-coregulated pilus and Pseudomonas aeruginosa PAK pilin
    • Craig, L., Taylor, R., Pique, M.E., Adair, B.D., Arvai, A.S., Singh, M., et al. (2003) Type IV pilin structure and assembly. X-ray and EM analyses of Vibrio cholerae toxin-coregulated pilus and Pseudomonas aeruginosa PAK pilin. Mol Cell 11: 1139-1150.
    • (2003) Mol Cell , vol.11 , pp. 1139-1150
    • Craig, L.1    Taylor, R.2    Pique, M.E.3    Adair, B.D.4    Arvai, A.S.5    Singh, M.6
  • 9
    • 2442589577 scopus 로고    scopus 로고
    • Type IV pilus structure and bacterial pathogenicity
    • Craig, L., Pique, M.E., and Tainer, J.A. (2004) Type IV pilus structure and bacterial pathogenicity. Nature Rev Microbiol 2: 363-378.
    • (2004) Nature Rev Microbiol , vol.2 , pp. 363-378
    • Craig, L.1    Pique, M.E.2    Tainer, J.A.3
  • 10
    • 0000668797 scopus 로고
    • Reconstitution of three-dimensional structures from electron micrographs
    • DeRosier, D.J., and Klug, A. (1968) Reconstitution of three-dimensional structures from electron micrographs. Nature 217: 130-134.
    • (1968) Nature , vol.217 , pp. 130-134
    • DeRosier, D.J.1    Klug, A.2
  • 11
    • 0030915704 scopus 로고    scopus 로고
    • Improved R-factors for diffraction data analysis in macromolecular crystallography
    • Diederichs, K., and Karplus, P.A. (1997) Improved R-factors for diffraction data analysis in macromolecular crystallography. Nature Struct Biol 4: 269-275.
    • (1997) Nature Struct Biol , vol.4 , pp. 269-275
    • Diederichs, K.1    Karplus, P.A.2
  • 12
    • 0026634706 scopus 로고
    • PulO, a component of the pullulanase secretion pathway of Klebsiella oxytoca, correctly and efficiently processes gonococcal type IV prepilin in Escherichia coli
    • Dupuy, B., Taha, M.-K., Possot, O., Marchai, C., and Pugsley, A.P. (1992) PulO, a component of the pullulanase secretion pathway of Klebsiella oxytoca, correctly and efficiently processes gonococcal type IV prepilin in Escherichia coli. Mol Microbiol 6: 1887-1894.
    • (1992) Mol Microbiol , vol.6 , pp. 1887-1894
    • Dupuy, B.1    Taha, M.-K.2    Possot, O.3    Marchai, C.4    Pugsley, A.P.5
  • 13
    • 0037406829 scopus 로고    scopus 로고
    • Type II protein secretion in Pseudomlonas aeruginosa: The pseudopilus is a multifibrillar and adhesive structure
    • Durand, E., Bernadac, A., Ball, G., Lazdunski, A., Sturgis, J.N., and Filloux, A. (2003) Type II protein secretion in Pseudomlonas aeruginosa: the pseudopilus is a multifibrillar and adhesive structure. J Bacteriol 185: 2749-2758.
    • (2003) J Bacteriol , vol.185 , pp. 2749-2758
    • Durand, E.1    Bernadac, A.2    Ball, G.3    Lazdunski, A.4    Sturgis, J.N.5    Filloux, A.6
  • 14
    • 0023446388 scopus 로고
    • Expression of multiple types of N-methyl Phe pili in Pseudomonas aeruginosa
    • Elleman, T.C., and Peterson, J.E. (1987) Expression of multiple types of N-methyl Phe pili in Pseudomonas aeruginosa. Mol Microbiol 1: 377-380.
    • (1987) Mol Microbiol , vol.1 , pp. 377-380
    • Elleman, T.C.1    Peterson, J.E.2
  • 15
  • 16
    • 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., Ryter, A., and Pugsley, A.P. (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
  • 17
    • 0021836574 scopus 로고
    • Intragenic recombination leads to pilus antigenic variation in Neisseria gonorrhoeae
    • Hagblom, P., Segal, E., Billyard, E., and So, M. (1985) Intragenic recombination leads to pilus antigenic variation in Neisseria gonorrhoeae. Nature 315: 156-158.
    • (1985) Nature , vol.315 , pp. 156-158
    • Hagblom, P.1    Segal, E.2    Billyard, E.3    So, M.4
  • 19
    • 0036428752 scopus 로고    scopus 로고
    • Exploring the 3D molecular architecture of Escherichia coli type 1 pili
    • Hahn, E., Wild, P., Hermanns, U., Sebbel, P., Glockshuber, R., Häner, M., et al. (2002) Exploring the 3D molecular architecture of Escherichia coli type 1 pili. J Mol Biol 323: 845-857.
    • (2002) J Mol Biol , vol.323 , pp. 845-857
    • Hahn, E.1    Wild, P.2    Hermanns, U.3    Sebbel, P.4    Glockshuber, R.5    Häner, M.6
  • 20
    • 0034674160 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas aeruginosa PAK pilin suggests a main-chain-dominated mode of receptor binding
    • Hazes, B., Sastry, P., Hayakawa, K., Read, R., and Irvin, R. (2000) Crystal structure of Pseudomonas aeruginosa PAK pilin suggests a main-chain-dominated mode of receptor binding. J Mol Biol 299: 1005-1017.
    • (2000) J Mol Biol , vol.299 , pp. 1005-1017
    • Hazes, B.1    Sastry, P.2    Hayakawa, K.3    Read, R.4    Irvin, R.5
  • 21
    • 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
  • 22
    • 0026574756 scopus 로고
    • Production of Neisseria gonorrhoeae pili (fimbriae) in Pseudomonas aeruginosa
    • Hoyne, P.A., Haas, R., Meyer, T.F., Davies, U.K., and Elleman, T.C. (1993) Production of Neisseria gonorrhoeae pili (fimbriae) in Pseudomonas aeruginosa. J Bacteriol 174: 7321-7327.
    • (1993) J Bacteriol , vol.174 , pp. 7321-7327
    • Hoyne, P.A.1    Haas, R.2    Meyer, T.F.3    Davies, U.K.4    Elleman, T.C.5
  • 23
    • 0036646537 scopus 로고    scopus 로고
    • XpsG, the major pseudopilin in Xanthomonas camplestric pv. campestris forms a pilus-like structure between cytoplasmic and outer membranes
    • Hu, N.-T., Leu, W.-M., Lee, M.-S., Chen, A., Chen, S.-C., Song, Y.-L., and Chen, L.-Y. (2002) XpsG, the major pseudopilin in Xanthomonas camplestric 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    Chen, S.-C.5    Song, Y.-L.6    Chen, L.-Y.7
  • 24
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., and Kjeldgard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst A47: 110-119.
    • (1991) Acta Cryst A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Kjeldgard, M.3
  • 25
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Cryst 26: 795-800.
    • (1993) J Appl Cryst , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 26
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and Sander, C. (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 27
    • 0035968237 scopus 로고    scopus 로고
    • Structure of a pilin monomer from Pseudomonas aeruginosa: Implications for the assembly of pili
    • Keizer, D., Slupsky, C., Kalisiak, M., Campbel, A., Crump, M., Sastry, P., et al. (2001) Structure of a pilin monomer from Pseudomonas aeruginosa: implications for the assembly of pili. J Biol Chem 276: 24186-24193.
    • (2001) J Biol Chem , vol.276 , pp. 24186-24193
    • Keizer, D.1    Slupsky, C.2    Kalisiak, M.3    Campbel, A.4    Crump, M.5    Sastry, P.6
  • 28
    • 0033951396 scopus 로고    scopus 로고
    • Delineation of pilin domains required for bacterial association into microcolonies and intestinal colonization by Vibrio cholerae
    • Kirn, T.J., Lafferty, M.J., Sandoe, C.M.P., and Taylor, R.K. (2000) Delineation of pilin domains required for bacterial association into microcolonies and intestinal colonization by Vibrio cholerae. Mol Microbiol 35: 896-910.
    • (2000) Mol Microbiol , vol.35 , pp. 896-910
    • Kirn, T.J.1    Lafferty, M.J.2    Sandoe, C.M.P.3    Taylor, R.K.4
  • 29
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin, V.S., and Wilson, K.S. (1993) Automated refinement of protein models. Acta Cryst D49: 129-149.
    • (1993) Acta Cryst , vol.D49 , pp. 129-149
    • Lamzin, V.S.1    Wilson, K.S.2
  • 30
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J App Chryst 26: 383-391.
    • (1993) J App Chryst , vol.26 , pp. 383-391
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 31
    • 0022365856 scopus 로고
    • Characterization and expression of the structural gene for pullulanase, a maltose-inducible secreted protein of Klebsiella pneumoniae
    • Michaelis, S., Chapon, C., d'Enfert, C., Pugsley, A.P., and Schwartz, M. (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
  • 33
    • 0026499526 scopus 로고
    • Factors influencing the precision of quantitative scanning transmission electron microscopy
    • Müller, S.A., Goldie, K.N., Bürki, R., Häring, R., and Engel, A. (1992) Factors influencing the precision of quantitative scanning transmission electron microscopy. Ultramicroscopy 46: 317-334.
    • (1992) Ultramicroscopy , vol.46 , pp. 317-334
    • Müller, S.A.1    Goldie, K.N.2    Bürki, R.3    Häring, R.4    Engel, A.5
  • 34
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G.N., Vagin, A.A., and Dodson, E.J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst D53: 240-245.
    • (1997) Acta Cryst D , vol.53 , pp. 240-245
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 35
    • 0032897075 scopus 로고    scopus 로고
    • Efficient anisotropic refinement of macromolecular structures using FFT
    • Murshudov, G.N., Lebedev, A., Vagin, A.A., Wilson, K.S., and Dodson, E.J. (1999) Efficient anisotropic refinement of macromolecular structures using FFT. Acta Cryst D55: 247-255.
    • (1999) Acta Cryst , vol.D55 , pp. 247-255
    • Murshudov, G.N.1    Lebedev, A.2    Vagin, A.A.3    Wilson, K.S.4    Dodson, E.J.5
  • 36
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A., and Honig, B. (1991) Protein folding and association: insights from the interfacial thermodynamic properties of hydrocarbons. Proteins 11: 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 38
    • 0034657105 scopus 로고    scopus 로고
    • Domain structure of secretin PulD revealed by limited proteolysis and electron microscopy
    • Nouwen, N., Stahlberg, H., Pugsley, A.P., and Engel, A. (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
  • 39
    • 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
  • 41
    • 0024041477 scopus 로고
    • The expression of mutant pilins in Pseudomonas aeruginosa: Fifth position glutamate affects pilin methylation
    • Pasloske, B.L., and Paranchych, W. (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
  • 42
    • 0024598452 scopus 로고
    • Assembly of mutant pilins in Pseudomonas aeruginosa: Formation of pili composed of heterologous subunits
    • Pasloske, B.L., Scraba, D.G., and Paranchych, W. (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
  • 43
  • 44
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., Morris, R., and Lamzin, V.S. (1999) Automated protein model building combined with iterative structure refinement. Nature Struct Biol 6: 458-463.
    • (1999) Nature Struct Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 45
    • 0034034763 scopus 로고    scopus 로고
    • Multiple interactions between pullulanase secreton components involved in stabilization and cytoplasmic membrane association of PulE
    • Possot, O., 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 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
  • 46
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley, A.P. (1993a) 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
  • 47
    • 0027337742 scopus 로고
    • Processing and methylation of PulG, a pilin-like component of the general secretory pathway of Klebsiella oxytoca
    • Pugsley, A.P. (1993b) 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
  • 48
    • 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
  • 49
    • 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 Possot, O. (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
  • 50
    • 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., Bayan, N., and Sauvonnet, N. (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
  • 51
    • 0035029580 scopus 로고    scopus 로고
    • Biology of type II secretion
    • Sandkvist, M. (2001) Biology of type II secretion. Mol Microbiol 40: 271-283.
    • (2001) Mol Microbiol , vol.40 , pp. 271-283
    • Sandkvist, M.1
  • 52
    • 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. (2000a) 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
  • 53
    • 0033985118 scopus 로고    scopus 로고
    • PpdD type IV pilin of Escherichia coli K-12 can be assembled into pili in Pseudomonas aeruginosa
    • Sauvonnet, N., Gounon, P., and Pugsley, A.P. (2000b) PpdD type IV pilin of Escherichia coli K-12 can be assembled into pili in Pseudomonas aeruginosa. J Bacteriol 182: 848-854.
    • (2000) J Bacteriol , vol.182 , pp. 848-854
    • Sauvonnet, N.1    Gounon, P.2    Pugsley, A.P.3
  • 54
    • 0018650401 scopus 로고
    • Digital image processing: The Semper system
    • Saxton, W.O., Pitt, T.J., and Horner, M. (1979) Digital image processing: the Semper system. Ultramicroscopy 4: 343-354.
    • (1979) Ultramicroscopy , vol.4 , pp. 343-354
    • Saxton, W.O.1    Pitt, T.J.2    Horner, M.3
  • 55
    • 0036793095 scopus 로고    scopus 로고
    • Substructure solution with SHELXD
    • Schneider, T.R., and Sheldrick, G.M. (2002) Substructure solution with SHELXD. Acta Cryst D58 1772-1779.
    • (2002) Acta Cryst , vol.D58 , pp. 1772-1779
    • Schneider, T.R.1    Sheldrick, G.M.2
  • 56
    • 0001521247 scopus 로고
    • Computer-generated Fourier transforms of helical particles
    • Smith, P.R., and Aebi, U. (1974) Computer-generated Fourier transforms of helical particles. J Phys 7: 1627-1633.
    • (1974) J Phys , vol.7 , pp. 1627-1633
    • Smith, P.R.1    Aebi, U.2
  • 57
    • 0029916486 scopus 로고    scopus 로고
    • The micrograph data processing program
    • Smith, P.P., and Gottesman, S.M. (1996) The micrograph data processing program. J Struct Biol 116: 35-40.
    • (1996) J Struct Biol , vol.116 , pp. 35-40
    • Smith, P.P.1    Gottesman, S.M.2
  • 58
    • 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 Lory, S. (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
  • 59
    • 0027242120 scopus 로고
    • Identification of active-site cysteines in the conserved domain of PilD, the bifunctional type IV pilin leader peptidase/N-methyltransferase of Pseudomonas aeruginosa
    • Strom, M.S., Bergman, P., and Lory, S. (1993) Identification of active-site cysteines in the conserved domain of PilD, the bifunctional type IV pilin leader peptidase/ N-methyltransferase of Pseudomonas aeruginosa. J Biol Chem 268: 15788-15794.
    • (1993) J Biol Chem , vol.268 , pp. 15788-15794
    • Strom, M.S.1    Bergman, P.2    Lory, S.3
  • 60
    • 0026034189 scopus 로고
    • Localization of protective epitopes within pilin subunit of Vibrio cholerae toxin-coregulated pilus
    • Sun, D., Seyer, J.M., Kovari, I., Siumrada, R.A., and Taylor, R.K. (1991) Localization of protective epitopes within pilin subunit of Vibrio cholerae toxin-coregulated pilus. Infect Immun 59: 114-118.
    • (1991) Infect Immun , vol.59 , pp. 114-118
    • Sun, D.1    Seyer, J.M.2    Kovari, I.3    Siumrada, R.A.4    Taylor, R.K.5
  • 61
    • 0030918120 scopus 로고    scopus 로고
    • Domains within the Vibrio cholerae toxin coregulated pilin sububnit that mediate bacterial colonization
    • Sun, D., Lafferty, M.J., Pek, J.A., and Taylor, R.K. (1997) Domains within the Vibrio cholerae toxin coregulated pilin sububnit that mediate bacterial colonization. Gene 192: 79-85.
    • (1997) Gene , vol.192 , pp. 79-85
    • Sun, D.1    Lafferty, M.J.2    Pek, J.A.3    Taylor, R.K.4
  • 62
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor, S., and Richardson, C.C. (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
  • 63
    • 0037853309 scopus 로고    scopus 로고
    • Type IV-like pili formed by the type II secreton: Specificity, composition, bundling, polar localization and surface presentation of peptides
    • Vignon, G., Köhler, R., Larquet, E., Giroux, S., Prévost, M.-C., Roux, P., and Pugsley, A.P. (2003) Type IV-like pili formed by the type II secreton: specificity, composition, bundling, polar localization and surface presentation of peptides. J Bacteriol 185: 3416-3428.
    • (2003) J Bacteriol , vol.185 , pp. 3416-3428
    • Vignon, G.1    Köhler, R.2    Larquet, E.3    Giroux, S.4    Prévost, M.-C.5    Roux, P.6    Pugsley, A.P.7
  • 64
    • 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.M., 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.M.2    Hayes, S.F.3    Dorward, D.4    Koomey, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.