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Volumn 5, Issue 8, 2010, Pages 1203-1218

Architecture of the type II secretion and type IV pilus machineries

Author keywords

ATPase; inner membrane complex; outer membrane complex; pilotin; platform; secretin; type II secretion; type IV pili

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; LIPOPROTEIN; METHYLTRANSFERASE; PEPTIDASE; PILIN; PILOTIN; PROTEIN GSPC; PROTEIN GSPD; PROTEIN GSPE; PROTEIN GSPF; PROTEIN GSPG; PROTEIN GSPL; PROTEIN GSPM; PROTEIN GSPO; PROTEIN GSPS; SECRETIN; UNCLASSIFIED DRUG;

EID: 77955936558     PISSN: 17460913     EISSN: None     Source Type: Journal    
DOI: 10.2217/fmb.10.76     Document Type: Review
Times cited : (108)

References (130)
  • 1
    • 15944409588 scopus 로고    scopus 로고
    • Bioinformatics, genomics and evolution of non-flagellar type-III secretion systems: A Darwinian perspective
    • Pallen MJ, Beatson SA, Bailey CM: Bioinformatics, genomics and evolution of non-flagellar type-III secretion systems: a Darwinian perspective. FEMS Microbiol. Rev. 29, 201-229 (2005).
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 201-229
    • Pallen, M.J.1    Beatson, S.A.2    Bailey, C.M.3
  • 2
    • 0032511192 scopus 로고    scopus 로고
    • Macromolecular assembly and secretion across the bacterial cell envelope: Type II protein secretion systems
    • Russel M: Macromolecular assembly and secretion across the bacterial cell envelope: type II protein secretion systems. J. Mol. Biol. 279, 485-499 (1998).
    • (1998) J. Mol. Biol. , vol.279 , pp. 485-499
    • Russel, M.1
  • 4
    • 0027450561 scopus 로고
    • The complete general secretory pathway in Gram-negative bacteria
    • Pugsley AP: The complete general secretory pathway in Gram-negative bacteria. Microbiol. Rev. 57, 50-108 (1993).
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 5
    • 26844457990 scopus 로고    scopus 로고
    • Subcomplexes from the Xcp secretion system of Pseudomonas aeruginosa
    • Robert V, Filloux A, Michel GP: Subcomplexes from the Xcp secretion system of Pseudomonas aeruginosa. FEMS Microbiol. Lett. 252, 43-50 (2005).
    • (2005) FEMS Microbiol. Lett. , vol.252 , pp. 43-50
    • Robert, V.1    Filloux, A.2    Michel, G.P.3
  • 6
    • 26044455889 scopus 로고    scopus 로고
    • Role of XcpP in the functionality of the Pseudomonas aeruginosa secreton
    • Robert V, Filloux A, Michel GP: Role of XcpP in the functionality of the Pseudomonas aeruginosa secreton. Res. Microbiol. 156, 880-886 (2005).
    • (2005) Res. Microbiol. , vol.156 , pp. 880-886
    • Robert, V.1    Filloux, A.2    Michel, G.P.3
  • 7
    • 59649092183 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody
    • Korotkov KV, Pardon E, Steyaert J, Hol WG: Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody. Structure 17, 255-265 (2009).
    • (2009) Structure , vol.17 , pp. 255-265
    • Korotkov, K.V.1    Pardon, E.2    Steyaert, J.3    Hol, W.G.4
  • 9
    • 1942424083 scopus 로고    scopus 로고
    • The inner membrane subassembly of the enteropathogenic Escherichia coli bundle-forming pilus machine
    • Crowther LJ, Anantha RP, Donnenberg MS: The inner membrane subassembly of the enteropathogenic Escherichia coli bundle-forming pilus machine. Mol. Microbiol. 52, 67-79 (2004).
    • (2004) Mol. Microbiol. , vol.52 , pp. 67-79
    • Crowther, L.J.1    Anantha, R.P.2    Donnenberg, M.S.3
  • 10
    • 33747093681 scopus 로고    scopus 로고
    • Interaction and localization studies of enteropathogenic Escherichia coli type IV bundle-forming pilus outer membrane components
    • Daniel A, Singh A, Crowther LJ, Fernandes PJ, Schreiber W, Donnenberg MS: Interaction and localization studies of enteropathogenic Escherichia coli type IV bundle-forming pilus outer membrane components. Microbiology 152, 2405-2420 (2006).
    • (2006) Microbiology , vol.152 , pp. 2405-2420
    • Daniel, A.1    Singh, A.2    Crowther, L.J.3    Fernandes, P.J.4    Schreiber, W.5    Donnenberg, M.S.6
  • 11
    • 33644848512 scopus 로고    scopus 로고
    • Polar assembly of the type IV pilus secretin in Myxococcus xanthus
    • Nudleman E, Wall D, Kaiser D: Polar assembly of the type IV pilus secretin in Myxococcus xanthus. Mol. Microbiol. 60, 16-29 (2006).
    • (2006) Mol. Microbiol. , vol.60 , pp. 16-29
    • Nudleman, E.1    Wall, D.2    Kaiser, D.3
  • 12
    • 12344272637 scopus 로고    scopus 로고
    • Type IV pilus biogenesis in Neisseria meningitidis: PilW is involved in a step occurring after pilus assembly, essential for fibre stability and function
    • Carbonnelle E, Helaine S, Prouvensier L, Nassif X, Pelicic V: Type IV pilus biogenesis in Neisseria meningitidis: PilW is involved in a step occurring after pilus assembly, essential for fibre stability and function. Mol. Microbiol. 55, 54-64 (2005).
    • (2005) Mol. Microbiol. , vol.55 , pp. 54-64
    • Carbonnelle, E.1    Helaine, S.2    Prouvensier, L.3    Nassif, X.4    Pelicic, V.5
  • 13
    • 33748484296 scopus 로고    scopus 로고
    • A systematic genetic analysis in Neisseria meningitidis defines the Pil proteins required for assembly, functionality, stabilization and export of type IV pili
    • Carbonnelle E, Helaine S, Nassif X, Pelicic V: A systematic genetic analysis in Neisseria meningitidis defines the Pil proteins required for assembly, functionality, stabilization and export of type IV pili. Mol. Microbiol. 61, 1510-1522 (2006).
    • (2006) Mol. Microbiol. , vol.61 , pp. 1510-1522
    • Carbonnelle, E.1    Helaine, S.2    Nassif, X.3    Pelicic, V.4
  • 14
    • 55749114256 scopus 로고    scopus 로고
    • PilF is an outer membrane lipoprotein required for multimerization and localization of the Pseudomonas aeruginosa type IV pilus secretin
    • Koo J, Tammam S, Ku SY, Sampaleanu LM, Burrows LL, Howell PL: PilF is an outer membrane lipoprotein required for multimerization and localization of the Pseudomonas aeruginosa type IV pilus secretin. J. Bacteriol. 190, 6961-6969 (2008).
    • (2008) J. Bacteriol. , vol.190 , pp. 6961-6969
    • Koo, J.1    Tammam, S.2    Ku, S.Y.3    Sampaleanu, L.M.4    Burrows, L.L.5    Howell, P.L.6
  • 15
    • 70350160784 scopus 로고    scopus 로고
    • Periplasmic domains of Pseudomonas aeruginosa PilN and PilO form a stable heterodimeric complex
    • Sampaleanu LM, Bonanno JB, Ayers M et al: Periplasmic domains of Pseudomonas aeruginosa PilN and PilO form a stable heterodimeric complex. J. Mol. Biol. 394(1), 143-159 (2009).
    • (2009) J. Mol. Biol. , vol.394 , Issue.1 , pp. 143-159
    • Sampaleanu, L.M.1    Bonanno, J.B.2    Ayers, M.3
  • 16
    • 70350141013 scopus 로고    scopus 로고
    • PilM/N/O/P proteins form an inner membrane complex that affects the stability of the Pseudomonas aeruginosa type IV pilus secretin
    • Ayers M, Sampaleanu LM, Tammam S, Koo J, Harvey H, Howell PL, Burrows LL: PilM/N/O/P proteins form an inner membrane complex that affects the stability of the Pseudomonas aeruginosa type IV pilus secretin. J. Mol. Biol. 394, 128-142 (2009).
    • (2009) J. Mol. Biol. , vol.394 , pp. 128-142
    • Ayers, M.1    Sampaleanu, L.M.2    Tammam, S.3    Koo, J.4    Harvey, H.5    Howell, P.L.6    Burrows, L.L.7
  • 17
    • 33751086145 scopus 로고    scopus 로고
    • Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin
    • Guilvout I, Chami M, Engel A, Pugsley AP, Bayan N: Bacterial outer membrane secretin PulD assembles and inserts into the inner membrane in the absence of its pilotin. EMBO J. 25, 5241-5249 (2006).
    • (2006) EMBO J , vol.25 , pp. 5241-5249
    • Guilvout, I.1    Chami, M.2    Engel, A.3    Pugsley, A.P.4    Bayan, N.5
  • 19
    • 2442589577 scopus 로고    scopus 로고
    • Type IV pilus structure and bacterial pathogenicity
    • Craig L, Pique ME, Tainer JA: Type IV pilus structure and bacterial pathogenicity. Nat. Rev. Microbiol. 2, 363-378 (2004).
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 363-378
    • Craig, L.1    Pique, M.E.2    Tainer, J.A.3
  • 20
    • 0034618643 scopus 로고    scopus 로고
    • Pilus retraction powers bacterial twitching motility
    • Merz AJ, So M, Sheetz MP: Pilus retraction powers bacterial twitching motility. Nature 407, 98-102 (2000).
    • (2000) Nature , vol.407 , pp. 98-102
    • Merz, A.J.1    So, M.2    Sheetz, M.P.3
  • 22
    • 0032963612 scopus 로고    scopus 로고
    • Twelve pil genes are required for biogenesis of the R64 thin pilus
    • Yoshida T, Kim SR, Komano T: Twelve pil genes are required for biogenesis of the R64 thin pilus. J. Bacteriol. 181, 2038-2043 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 2038-2043
    • Yoshida, T.1    Kim, S.R.2    Komano, T.3
  • 23
    • 0030957263 scopus 로고    scopus 로고
    • The tcp gene cluster of Vibrio cholerae
    • Manning PA: The tcp gene cluster of Vibrio cholerae. Gene 192, 63-70 (1997).
    • (1997) Gene , vol.192 , pp. 63-70
    • Manning, P.A.1
  • 24
    • 34250329174 scopus 로고    scopus 로고
    • Membrane association and multimerization of TcpT, the cognate ATPase ortholog of the Vibrio cholerae toxin-coregulated-pilus biogenesis apparatus
    • Tripathi SA, Taylor RK: Membrane association and multimerization of TcpT, the cognate ATPase ortholog of the Vibrio cholerae toxin-coregulated-pilus biogenesis apparatus. J. Bacteriol. 189, 4401-4409 (2007).
    • (2007) J. Bacteriol. , vol.189 , pp. 4401-4409
    • Tripathi, S.A.1    Taylor, R.K.2
  • 25
    • 38649126553 scopus 로고    scopus 로고
    • Outer membrane components of the Tad (tight adherence) secreton of Aggregatibacter actinomycetemcomitans
    • Clock SA, Planet PJ, Perez BA, Figurski DH: Outer membrane components of the Tad (tight adherence) secreton of Aggregatibacter actinomycetemcomitans. J. Bacteriol. 190, 980-990 (2008).
    • (2008) J. Bacteriol. , vol.190 , pp. 980-990
    • Clock, S.A.1    Planet, P.J.2    Perez, B.A.3    Figurski, D.H.4
  • 26
    • 41949117894 scopus 로고    scopus 로고
    • Type IV pili: Paradoxes in form and function
    • Craig L, Li J: Type IV pili: paradoxes in form and function. Curr. Opin. Struct. Biol. 18, 267-277 (2008).
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 267-277
    • Craig, L.1    Li, J.2
  • 27
    • 33748773323 scopus 로고    scopus 로고
    • Type IV pilin structures: Insights on shared architecture, fiber assembly, receptor binding and type II secretion
    • Hansen JK, Forest KT: Type IV pilin structures: insights on shared architecture, fiber assembly, receptor binding and type II secretion. J. Mol. Microbiol. Biotechnol. 11, 192-207 (2006).
    • (2006) J. Mol. Microbiol. Biotechnol. , vol.11 , pp. 192-207
    • Hansen, J.K.1    Forest, K.T.2
  • 28
    • 33748757929 scopus 로고    scopus 로고
    • Archaeal flagella, bacterial flagella and type IV pili: A comparison of genes and posttranslational modifications
    • Ng SY, Chaban B, Jarrell KF: Archaeal flagella, bacterial flagella and type IV pili: a comparison of genes and posttranslational modifications. J. Mol. Microbiol. Biotechnol. 11, 167-191 (2006).
    • (2006) J. Mol. Microbiol. Biotechnol. , vol.11 , pp. 167-191
    • Ng, S.Y.1    Chaban, B.2    Jarrell, K.F.3
  • 30
    • 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 NT, Hung MN, Chiou SJ et al.: 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).
    • (1992) J. Bacteriol. , vol.174 , pp. 2679-2687
    • Hu, N.T.1    Hung, M.N.2    Chiou, S.J.3
  • 31
    • 0034406525 scopus 로고    scopus 로고
    • Components and dynamics of fiber formation define a ubiquitous biogenesis pathway for bacterial pili
    • Wolfgang M, van Putten JP, Hayes SF, Dorward D, Koomey M: Components and dynamics of fiber formation define a ubiquitous biogenesis pathway for bacterial pili. EMBO J. 19, 6408-6418 (2000).
    • (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
  • 32
    • 0018866264 scopus 로고
    • Wilde CE 3rd, Sawyer WD, Haak RA: High-molecular-weight antigenic protein complex in the outer membrane of Neisseria gonorrhoeae
    • Newhall WJ, Wilde CE 3rd, Sawyer WD, Haak RA: High-molecular-weight antigenic protein complex in the outer membrane of Neisseria gonorrhoeae. Infect. Immun. 27, 475-482 (1980).
    • (1980) Infect. Immun. , vol.27 , pp. 475-482
    • Newhall, W.J.1
  • 33
    • 0031871011 scopus 로고    scopus 로고
    • Structure and function of repetitive sequence elements associated with a highly polymorphic domain of the Neisseria meningitidis PilQ protein
    • Tonjum T, Caugant DA, Dunham SA, Koomey M: Structure and function of repetitive sequence elements associated with a highly polymorphic domain of the Neisseria meningitidis PilQ protein. Mol. Microbiol. 29, 111-124 (1998).
    • (1998) Mol. Microbiol. , vol.29 , pp. 111-124
    • Tonjum, T.1    Caugant, D.A.2    Dunham, S.A.3    Koomey, M.4
  • 34
    • 27844581702 scopus 로고    scopus 로고
    • Structural insights into the secretin PulD and its trypsin-resistant core
    • Chami M, Guilvout I, Gregorini M et al.: Structural insights into the secretin PulD and its trypsin-resistant core. J. Biol. Chem. 280, 37732-37741 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 37732-37741
    • Chami, M.1    Guilvout, I.2    Gregorini, M.3
  • 35
    • 0033529264 scopus 로고    scopus 로고
    • Secretin PulD: Association with pilot PulS, structure, and ion-conducting channel formation
    • Nouwen N, Ranson N, Saibil H et al.: Secretin PulD: association with pilot PulS, structure, and ion-conducting channel formation. Proc. Natl Acad. Sci. USA 96, 8173-8177 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 8173-8177
    • Nouwen, N.1    Ranson, N.2    Saibil, H.3
  • 36
    • 0034973703 scopus 로고    scopus 로고
    • Analysis of the PilQ secretin from Neisseria meningitidis by transmission electron microscopy reveals a dodecameric quaternary structure
    • Collins RF, Davidsen L, Derrick JP, Ford RC, Tonjum T: Analysis of the PilQ secretin from Neisseria meningitidis by transmission electron microscopy reveals a dodecameric quaternary structure. J. Bacteriol. 183, 3825-3832 (2001).
    • (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
  • 37
    • 0037389450 scopus 로고    scopus 로고
    • Three-dimensional structure of the Neisseria meningitidis secretin PilQ determined from negative-stain transmission electron microscopy
    • Collins RF, Ford RC, Kitmitto A, Olsen RO, Tonjum T, Derrick JP: Three-dimensional structure of the Neisseria meningitidis secretin PilQ determined from negative-stain transmission electron microscopy. J. Bacteriol. 185, 2611-2617 (2003).
    • (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
  • 38
    • 4544346057 scopus 로고    scopus 로고
    • Structure of the Neisseria meningitidis outer membrane PilQ secretin complex at 12 A resolution
    • Collins RF, Frye SA, Kitmitto A, Ford RC, Tonjum T, Derrick JP: Structure of the Neisseria meningitidis outer membrane PilQ secretin complex at 12 A resolution. J. Biol. Chem. 279, 39750-39756 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 39750-39756
    • Collins, R.F.1    Frye, S.A.2    Kitmitto, A.3    Ford, R.C.4    Tonjum, T.5    Derrick, J.P.6
  • 39
    • 0034906825 scopus 로고    scopus 로고
    • Structure-function analysis of BfpB, a secretin-like protein encoded by the bundle-forming-pilus operon of enteropathogenic Escherichia coli
    • Schmidt SA, Bieber D, Ramer SW, Hwang J, Wu CY, Schoolnik G: Structure-function analysis of BfpB, a secretin-like protein encoded by the bundle-forming-pilus operon of enteropathogenic Escherichia coli. J. Bacteriol. 183, 4848-4859 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 4848-4859
    • Schmidt, S.A.1    Bieber, D.2    Ramer, S.W.3    Hwang, J.4    Wu, C.Y.5    Schoolnik, G.6
  • 40
    • 0029904580 scopus 로고    scopus 로고
    • BfpB, an outer membrane lipoprotein required for the biogenesis of bundle-forming pili in enteropathogenic Escherichia coli
    • Ramer SW, Bieber D, Schoolnik GK: BfpB, an outer membrane lipoprotein required for the biogenesis of bundle-forming pili in enteropathogenic Escherichia coli. J. Bacteriol. 178, 6555-6563 (1996).
    • (1996) J. Bacteriol. , vol.178 , pp. 6555-6563
    • Ramer, S.W.1    Bieber, D.2    Schoolnik, G.K.3
  • 41
    • 0026939131 scopus 로고
    • TCP pilus biosynthesis in Vibrio cholerae O1: Gene sequence of tcpC encoding an outer membrane lipoprotein
    • Ogierman MA, Manning PA: TCP pilus biosynthesis in Vibrio cholerae O1: gene sequence of tcpC encoding an outer membrane lipoprotein. FEMS Microbiol. Lett. 76, 179-184 (1992).
    • (1992) FEMS Microbiol. Lett. , vol.76 , pp. 179-184
    • Ogierman, M.A.1    Manning, P.A.2
  • 42
    • 15244343311 scopus 로고    scopus 로고
    • Identification of a TcpC-TcpQ outer membrane complex involved in the biogenesis of the toxin-coregulated pilus of Vibrio cholerae
    • Bose N, Taylor RK: Identification of a TcpC-TcpQ outer membrane complex involved in the biogenesis of the toxin-coregulated pilus of Vibrio cholerae. J. Bacteriol. 187, 2225-2232
    • J. Bacteriol. , vol.187 , pp. 2225-2232
    • Bose, N.1    Taylor, R.K.2
  • 43
    • 0034657105 scopus 로고    scopus 로고
    • Domain structure of secretin PulD revealed by limited proteolysis and electron microscopy
    • Nouwen N, Stahlberg H, Pugsley AP, Engel A: Domain structure of secretin PulD revealed by limited proteolysis and electron microscopy. EMBO J. 19, 2229-2236 (2000).
    • (2000) EMBO J , vol.19 , pp. 2229-2236
    • Nouwen, N.1    Stahlberg, H.2    Pugsley, A.P.3    Engel, A.4
  • 44
    • 0027235766 scopus 로고
    • Characterization of pilQ, a new gene required for the biogenesis of type 4 fimbriae in Pseudomonas aeruginosa
    • Martin PR, Hobbs M, Free PD, Jeske Y, Mattick JS: Characterization of pilQ, a new gene required for the biogenesis of type 4 fimbriae in Pseudomonas aeruginosa. Mol. Microbiol. 9, 857-868 (1993).
    • (1993) Mol. Microbiol. , vol.9 , pp. 857-868
    • Martin, P.R.1    Hobbs, M.2    Free, P.D.3    Jeske, Y.4    Mattick, J.S.5
  • 45
    • 0028353854 scopus 로고
    • A superfamily of proteins involved in different secretion pathways in Gram-negative bacteria: Modular structure and specificity of the N-terminal domain
    • Genin S, Boucher CA: A superfamily of proteins involved in different secretion pathways in Gram-negative bacteria: modular structure and specificity of the N-terminal domain. Mol. Gen. Genet. 243, 112-118 (1994).
    • (1994) Mol. Gen. Genet. , vol.243 , pp. 112-118
    • Genin, S.1    Boucher, C.A.2
  • 46
    • 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, Tommassen J: 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).
    • (1998) Mol. Microbiol. , vol.27 , pp. 209-219
    • Bitter, W.1    Koster, M.2    Latijnhouwers, M.3    De Cock, H.4    Tommassen, J.5
  • 47
    • 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 et al.: The C-terminal domain of the Pseudomonas secretin XcpQ forms oligomeric rings with pore activity. J. Mol. Biol. 294, 1169-1179 (1999).
    • (1999) J. Mol. Biol. , vol.294 , pp. 1169-1179
    • Brok, R.1    Van Gelder, P.2    Winterhalter, M.3
  • 49
    • 0032901093 scopus 로고    scopus 로고
    • The Myxococcus xanthuspilQ (sglA) gene encodes a secretin homolog required for type IV pilus biogenesis, social motility, and development
    • Wall D, Kolenbrander PE, Kaiser D: The Myxococcus xanthuspilQ (sglA) gene encodes a secretin homolog required for type IV pilus biogenesis, social motility, and development. J. Bacteriol. 181, 24-33 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 24-33
    • Wall, D.1    Kolenbrander, P.E.2    Kaiser, D.3
  • 50
    • 33747872707 scopus 로고    scopus 로고
    • Type IV pilus structure by cryo-electron microscopy and crystallography: Implications for pilus assembly and functions
    • Craig L, Volkmann N, Arvai AS et al.: Type IV pilus structure by cryo-electron microscopy and crystallography: implications for pilus assembly and functions. Mol. Cell 23, 651-662
    • Mol. Cell , vol.23 , pp. 651-662
    • Craig, L.1    Volkmann, N.2    Arvai, A.S.3
  • 52
    • 21444443674 scopus 로고    scopus 로고
    • Interaction with type IV pili induces structural changes in the bacterial outer membrane secretin PilQ
    • Collins RF, Frye SA, Balasingham S, Ford RC, Tonjum T, Derrick JP: Interaction with type IV pili induces structural changes in the bacterial outer membrane secretin PilQ. J. Biol. Chem. 280, 18923-18930 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 18923-18930
    • Collins, R.F.1    Frye, S.A.2    Balasingham, S.3    Ford, R.C.4    Tonjum, T.5    Derrick, J.P.6
  • 53
    • 33745614951 scopus 로고    scopus 로고
    • Identification, subcellular localization and functional interactions of PilMNOWQ and PilA4 involved in transformation competency and pilus biogenesis in the thermophilic bacterium Thermus thermophilus HB27
    • Rumszauer J, Schwarzenlander C, Averhoff B: Identification, subcellular localization and functional interactions of PilMNOWQ and PilA4 involved in transformation competency and pilus biogenesis in the thermophilic bacterium Thermus thermophilus HB27. FEBSJ. 273, 3261-3272 (2006).
    • (2006) FEBS J , vol.273 , pp. 3261-3272
    • Rumszauer, J.1    Schwarzenlander, C.2    Averhoff, B.3
  • 54
    • 35948949060 scopus 로고    scopus 로고
    • A P strand lock exchange for signal transduction in TonB-dependent transducers on the basis of a common structural motif
    • Brillet K, Journet L, Celia H et al.: A P strand lock exchange for signal transduction in TonB-dependent transducers on the basis of a common structural motif. Structure 15, 1383-1391 (2007).
    • (2007) Structure , vol.15 , pp. 1383-1391
    • Brillet, K.1    Journet, L.2    Celia, H.3
  • 56
    • 28244476414 scopus 로고    scopus 로고
    • Nuclear magnetic resonance solution structure of the periplasmic signalling domain of the TonB-dependent outer membrane transporter FecA from Escherichia coli
    • Garcia-Herrero A, Vogel HJ: Nuclear magnetic resonance solution structure of the periplasmic signalling domain of the TonB-dependent outer membrane transporter FecA from Escherichia coli. Mol. Microbiol. 58, 1226-1237 (2005).
    • (2005) Mol. Microbiol. , vol.58 , pp. 1226-1237
    • Garcia-Herrero, A.1    Vogel, H.J.2
  • 57
    • 43549124851 scopus 로고    scopus 로고
    • Structure and function of KH domains
    • Valverde R, Edwards L, Regan L: Structure and function of KH domains. FEBS J. 275, 2712-2726 (2008).
    • (2008) FEBS J , vol.275 , pp. 2712-2726
    • Valverde, R.1    Edwards, L.2    Regan, L.3
  • 58
    • 0027273728 scopus 로고
    • The pre-mRNA binding K protein contains a novel evolutionarily conserved motif
    • Siomi H, Matunis MJ, Michael WM, Dreyfuss G: The pre-mRNA binding K protein contains a novel evolutionarily conserved motif. Nucleic Acids Res. 21, 1193-1198 (1993).
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1193-1198
    • Siomi, H.1    Matunis, M.J.2    Michael, W.M.3    Dreyfuss, G.4
  • 59
    • 34249043058 scopus 로고    scopus 로고
    • The outer membrane secretin PilQ from Neisseria meningitidis binds DNA
    • Assalkhou R, Balasingham S, Collins RF et al.: The outer membrane secretin PilQ from Neisseria meningitidis binds DNA. Microbiology 153, 1593-1603 (2007).
    • (2007) Microbiology , vol.153 , pp. 1593-1603
    • Assalkhou, R.1    Balasingham, S.2    Collins, R.F.3
  • 60
    • 0031025472 scopus 로고    scopus 로고
    • PilP, a pilus biogenesis lipoprotein in Neisseria gonorrhoeae, affects expression of PilQ as a high-molecular-mass multimer
    • Drake SL, Sandstedt SA, Koomey M: PilP, a pilus biogenesis lipoprotein in Neisseria gonorrhoeae, affects expression of PilQ as a high-molecular-mass multimer. Mol. Microbiol. 23, 657-668 (1997).
    • (1997) Mol. Microbiol. , vol.23 , pp. 657-668
    • Drake, S.L.1    Sandstedt, S.A.2    Koomey, M.3
  • 61
    • 34547628213 scopus 로고    scopus 로고
    • Interactions between the lipoprotein PilP and t he secretin Pi lQ in Neisseria meningitides
    • Balasingham SV, Collins RF, Assalkhou R et al.: Interactions between the lipoprotein PilP and t he secretin Pi lQ in Neisseria meningitidis. J. Bacteriol. 189, 5716-5727 (2007).
    • (2007) J. Bacteriol. , vol.189 , pp. 5716-5727
    • Balasingham, S.V.1    Collins, R.F.2    Assalkhou, R.3
  • 62
    • 14244262457 scopus 로고    scopus 로고
    • Associations of the major pseudopilin XpsG with XpsN (GspC) and secretin XpsD of Xanthomonas campestris pv. Campestris type II secretion apparatus revealed by cross-linking analysis
    • Lee MS, Chen LY, Leu WM, Shiau RJ, Hu NT: Associations of the major pseudopilin XpsG with XpsN (GspC) and secretin XpsD of Xanthomonas campestris pv. Campestris type II secretion apparatus revealed by cross-linking analysis. J. Biol. Chem. 280, 4585-4591 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 4585-4591
    • Lee, M.S.1    Chen, L.Y.2    Leu, W.M.3    Shiau, R.J.4    Hu, N.T.5
  • 63
    • 33748951751 scopus 로고    scopus 로고
    • Structural and functional studies of EpsC, a crucial component of the type 2 secretion system from Vibrio cholerae
    • Korotkov KV, Krumm B, Bagdasarian M, Hol WG: Structural and functional studies of EpsC, a crucial component of the type 2 secretion system from Vibrio cholerae. J. Mol. Biol. 363, 311-321 (2006).
    • (2006) J. Mol. Biol. , vol.363 , pp. 311-321
    • Korotkov, K.V.1    Krumm, B.2    Bagdasarian, M.3    Hol, W.G.4
  • 64
    • 2342553878 scopus 로고    scopus 로고
    • Functional dissection of the XpsN (GspC) protein of the Xanthomonas campestris pv. campestris type II secretion machinery
    • Lee HM, Chen JR, Lee HL et al.: Functional dissection of the XpsN (GspC) protein of the Xanthomonas campestris pv. campestris type II secretion machinery. J. Bacteriol. 186, 2946-2955 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 2946-2955
    • Lee, H.M.1    Chen, J.R.2    Lee, H.L.3
  • 65
    • 0036845861 scopus 로고    scopus 로고
    • A reversibly dissociable ternary complex formed by XpsL, XpsM and XpsN of the Xanthomonas campestris pv. campestris type II secretion apparatus
    • Tsai RT, Leu WM, Chen LY, Hu NT: A reversibly dissociable ternary complex formed by XpsL, XpsM and XpsN of the Xanthomonas campestris pv. campestris type II secretion apparatus. Biochem. J. 367, 865-871 (2002).
    • (2002) Biochem. J. , vol.367 , pp. 865-871
    • Tsai, R.T.1    Leu, W.M.2    Chen, L.Y.3    Hu, N.T.4
  • 66
    • 0036279961 scopus 로고    scopus 로고
    • The type IV pilus assembly complex: Biogenic interactions among the bundle-forming pilus proteins of enteropathogenic Escherichia coli
    • Ramer SW, Schoolnik GK, Wu CY, Hwang J, Schmidt SA, Bieber D: The type IV pilus assembly complex: biogenic interactions among the bundle-forming pilus proteins of enteropathogenic Escherichia coli. J. Bacteriol. 184, 3457-3465 (2002).
    • (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
  • 68
    • 0036616572 scopus 로고    scopus 로고
    • Identification of XcpP domains that confer functionality and specificity to the Pseudomonas aeruginosa type II secretion apparatus
    • Gerard-Vincent M, Robert V, Ball G et al.: Identification of XcpP domains that confer functionality and specificity to the Pseudomonas aeruginosa type II secretion apparatus. Mol. Microbiol. 44, 1651-1665 (2002).
    • (2002) Mol. Microbiol. , vol.44 , pp. 1651-1665
    • Gerard-Vincent, M.1    Robert, V.2    Ball, G.3
  • 69
    • 77952150444 scopus 로고    scopus 로고
    • A 20-residue peptide of the inner membrane protein OutC mediates interaction with two distinct sites of the outer membrane secretin OutD and is essential for the functional type II secretion system in Erwinia chrysanthemi
    • Login FH, Fries M, Wang X, Pickersgill RW, Shevchik VE: A 20-residue peptide of the inner membrane protein OutC mediates interaction with two distinct sites of the outer membrane secretin OutD and is essential for the functional type II secretion system in Erwinia chrysanthemi. Mol. Microbiol. 76(4), 944-955 (2010).
    • (2010) Mol. Microbiol. , vol.76 , Issue.4 , pp. 944-955
    • Login, F.H.1    Fries, M.2    Wang, X.3    Pickersgill, R.W.4    Shevchik, V.E.5
  • 70
    • 33750431393 scopus 로고    scopus 로고
    • The solution structure of a domain from the Neisseria meningitidis lipoprotein PilP reveals a new p-sandwich fold
    • Golovanov AP, Balasingham S, Tzitzilonis C et al. : The solution structure of a domain from the Neisseria meningitidis lipoprotein PilP reveals a new p-sandwich fold. J. Mol. Biol. 364, 186-195 (2006).
    • (2006) J. Mol. Biol. , vol.364 , pp. 186-195
    • Golovanov, A.P.1    Balasingham, S.2    Tzitzilonis, C.3
  • 71
    • 10544256597 scopus 로고    scopus 로고
    • The secretin-specific, chaperone-like protein of the general secretory pathway: Separation of proteolytic protection and piloting functions
    • Hardie KR, Seydel A, Guilvout I, Pugsley AP: The secretin-specific, chaperone-like protein of the general secretory pathway: separation of proteolytic protection and piloting functions. Mol. Microbiol. 22, 967-976 (1996).
    • (1996) Mol. Microbiol. , vol.22 , pp. 967-976
    • Hardie, K.R.1    Seydel, A.2    Guilvout, I.3    Pugsley, A.P.4
  • 72
    • 0029870545 scopus 로고    scopus 로고
    • Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein
    • Hardie KR, Lory S, Pugsley AP: Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein. EMBO J. 15, 978-988 (1996).
    • (1996) EMBO J , vol.15 , pp. 978-988
    • Hardie, K.R.1    Lory, S.2    Pugsley, A.P.3
  • 73
    • 0030965150 scopus 로고    scopus 로고
    • The C-terminal domain of the secretin PulD contains the binding site for its cognate chaperone, PulS, and confers PulS dependence on pIVf1 function
    • Daefler S, Guilvout I, Hardie KR, Pugsley AP, Russel M: The C-terminal domain of the secretin PulD contains the binding site for its cognate chaperone, PulS, and confers PulS dependence on pIVf1 function. Mol. Microbiol. 24, 465-475 (1997).
    • (1997) Mol. Microbiol. , vol.24 , pp. 465-475
    • Daefler, S.1    Guilvout, I.2    Hardie, K.R.3    Pugsley, A.P.4    Russel, M.5
  • 74
    • 0031736546 scopus 로고    scopus 로고
    • Functional characterization of the Erwinia chrysanthemi OutS protein, an element of a type II secretion system
    • Shevchik VE, Condemine G: Functional characterization of the Erwinia chrysanthemi OutS protein, an element of a type II secretion system. Microbiology 144(Pt 11), 3219-3228 (1998).
    • (1998) Microbiology , vol.144 , Issue.PART 11 , pp. 3219-3228
    • Shevchik, V.E.1    Condemine, G.2
  • 75
    • 42649087451 scopus 로고    scopus 로고
    • Structure of a widely conserved type IV pilus biogenesis factor that affects the stability of secretin multimers
    • Trindade MB, Job V, Contreras-Martel C, Pelicic V, Dessen A: Structure of a widely conserved type IV pilus biogenesis factor that affects the stability of secretin multimers. J. Mol. Biol. 378, 1031-1039 (2008).
    • (2008) J. Mol. Biol. , vol.378 , pp. 1031-1039
    • Trindade, M.B.1    Job, V.2    Contreras-Martel, C.3    Pelicic, V.4    Dessen, A.5
  • 76
    • 30544453079 scopus 로고    scopus 로고
    • Crystal structure of PilF: Functional implication in the type 4 pilus biogenesis in Pseudomonas aeruginosa
    • Kim K, Oh J, Han D, Kim EE, Lee B, Kim Y: Crystal structure of PilF: functional implication in the type 4 pilus biogenesis in Pseudomonas aeruginosa. Biochem. Biophys. Res. Commun. 340, 1028-1038 (2006).
    • (2006) Biochem. Biophys. Res. Commun. , vol.340 , pp. 1028-1038
    • Kim, K.1    Oh, J.2    Han, D.3    Kim, E.E.4    Lee, B.5    Kim, Y.6
  • 77
    • 21644435298 scopus 로고    scopus 로고
    • Cell-to-cell transfer of bacterial outer membrane lipoproteins
    • Nudleman E, Wall D, Kaiser D: Cell-to-cell transfer of bacterial outer membrane lipoproteins. Science 309, 125-127 (2005).
    • (2005) Science , vol.309 , pp. 125-127
    • Nudleman, E.1    Wall, D.2    Kaiser, D.3
  • 78
    • 71749120639 scopus 로고    scopus 로고
    • HxcQ liposecretin is self-piloted to the outer membrane by its N-terminal lipid anchor
    • Viarre V, Cascales E, Ball G, Michel GP, Filloux A, Voulhoux R: HxcQ liposecretin is self-piloted to the outer membrane by its N-terminal lipid anchor. J. Biol. Chem. 284, 33815-33823 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 33815-33823
    • Viarre, V.1    Cascales, E.2    Ball, G.3    Michel, G.P.4    Filloux, A.5    Voulhoux, R.6
  • 79
    • 8844269404 scopus 로고    scopus 로고
    • The underlying mechanisms of type II protein secretion
    • Filloux A: The underlying mechanisms of type II protein secretion. Biochim. Biophys. Acta 1694, 163-179 (2004).
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 163-179
    • Filloux, A.1
  • 80
    • 0036224953 scopus 로고    scopus 로고
    • Expression of the ExeAB complex of Aeromonas hydrophila is required for the localization and assembly of the ExeD secretion port multimer
    • Ast VM, Schoenhofen IC, Langen GR, Stratilo CW, Chamberlain MD, Howard SP: Expression of the ExeAB complex of Aeromonas hydrophila is required for the localization and assembly of the ExeD secretion port multimer. Mol. Microbiol. 44, 217-231 (2002).
    • (2002) Mol. Microbiol. , vol.44 , pp. 217-231
    • Ast, V.M.1    Schoenhofen, I.C.2    Langen, G.R.3    Stratilo, C.W.4    Chamberlain, M.D.5    Howard, S.P.6
  • 81
    • 33645080435 scopus 로고    scopus 로고
    • Interactions between peptidoglycan and the ExeAB complex during assembly of the type II secretin of Aeromonas hydrophila
    • Howard SP, Gebhart C, Langen GR, Li G, Strozen TG: Interactions between peptidoglycan and the ExeAB complex during assembly of the type II secretin of Aeromonas hydrophila. Mol. Microbiol. 59, 1062-1072 (2006).
    • (2006) Mol. Microbiol. , vol.59 , pp. 1062-1072
    • Howard, S.P.1    Gebhart, C.2    Langen, G.R.3    Li, G.4    Strozen, T.G.5
  • 82
    • 0031689660 scopus 로고    scopus 로고
    • An ExeAB complex in the type II secretion pathway of Aeromonas hydrophila: Effect of ATP-binding cassette mutations on complex formation and function
    • Schoenhofen IC, Stratilo C, Howard SP: An ExeAB complex in the type II secretion pathway of Aeromonas hydrophila: effect of ATP-binding cassette mutations on complex formation and function. Mol. Microbiol. 29, 1237-1247 (1998).
    • (1998) Mol. Microbiol. , vol.29 , pp. 1237-1247
    • Schoenhofen, I.C.1    Stratilo, C.2    Howard, S.P.3
  • 83
    • 77951569266 scopus 로고    scopus 로고
    • ExeA binds to peptidoglycan and forms a multimer for assembly of the type II secretion apparatus in Aeromonas hydrophila
    • Li G, Howard SP: ExeA binds to peptidoglycan and forms a multimer for assembly of the type II secretion apparatus in Aeromonas hydrophila. Mol. Microbiol. 76(3), 772-781 (2010).
    • (2010) Mol. Microbiol. , vol.76 , Issue.3 , pp. 772-781
    • Li, G.1    Howard, S.P.2
  • 84
    • 0034091536 scopus 로고    scopus 로고
    • Identification of a novel gene, fimV, involved in twitching motility in Pseudomonas aeruginosa
    • Semmler AB, Whitchurch CB, Leech AJ, Mattick JS: Identification of a novel gene, fimV, involved in twitching motility in Pseudomonas aeruginosa. Microbiology 146(Pt 6), 1321-1332 (2000).
    • (2000) Microbiology , vol.146 , Issue.PART 6 , pp. 1321-1332
    • Semmler, A.B.1    Whitchurch, C.B.2    Leech, A.J.3    Mattick, J.S.4
  • 85
    • 0029842085 scopus 로고    scopus 로고
    • Peptidoglycan as a barrier to transenvelope transport
    • Dijkstra AJ, Keck W: Peptidoglycan as a barrier to transenvelope transport. J. Bacteriol. 178, 5555-5562 (1996).
    • (1996) J. Bacteriol. , vol.178 , pp. 5555-5562
    • Dijkstra, A.J.1    Keck, W.2
  • 86
    • 0344393521 scopus 로고    scopus 로고
    • Lytic transglycosylases in macromolecular transport systems of Gram-negative bacteria
    • Koraimann G: Lytic transglycosylases in macromolecular transport systems of Gram-negative bacteria. Cell Mol. Life Sci. 60, 2371-2388 (2003).
    • (2003) Cell Mol. Life Sci. , vol.60 , pp. 2371-2388
    • Koraimann, G.1
  • 87
    • 0033752390 scopus 로고    scopus 로고
    • Characterization of the multimeric Eps complex required for cholera toxin secretion
    • Sandkvist M, Bagdasarian M, Howard SP: Characterization of the multimeric Eps complex required for cholera toxin secretion. Int. J. Med. Microbiol. 290, 345-350 (2000).
    • (2000) Int. J. Med. Microbiol. , vol.290 , pp. 345-350
    • Sandkvist, M.1    Bagdasarian, M.2    Howard, S.P.3
  • 88
    • 0034034763 scopus 로고    scopus 로고
    • Multiple interactions between pullulanase secreton components involved in stabilization and cytoplasmic membrane association of PulE
    • Possot OM, Vignon G, Bomchil N, Ebel F, Pugsley AP: Multiple interactions between pullulanase secreton components involved in stabilization and cytoplasmic membrane association of PulE. J. Bacteriol. 182, 2142-2152 (2000).
    • (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
  • 89
    • 1342302802 scopus 로고    scopus 로고
    • Systematic analysis, by the yeast two-hybrid, of protein interaction between components of the type II secretory machinery of Erwinia chrysanthemi
    • Douet V, Loiseau L, Barras F, Py B: Systematic analysis, by the yeast two-hybrid, of protein interaction between components of the type II secretory machinery of Erwinia chrysanthemi. Res. Microbiol. 155, 71-75 (2004).
    • (2004) Res. Microbiol. , vol.155 , pp. 71-75
    • Douet, V.1    Loiseau, L.2    Barras, F.3    Py, B.4
  • 91
    • 0035065972 scopus 로고    scopus 로고
    • An inner membrane platform in the type II secretion machinery of Gram-negative bacteria
    • Py B, Loiseau L, Barras F: An inner membrane platform in the type II secretion machinery of Gram-negative bacteria. EMBO Rep. 2, 244-248 (2001).
    • (2001) EMBO Rep. , vol.2 , pp. 244-248
    • Py, B.1    Loiseau, L.2    Barras, F.3
  • 92
    • 70349456527 scopus 로고    scopus 로고
    • The dimer formed by the periplasmic domain of EpsL from the type 2 secretion system of Vibrio parahaemolyticus
    • Abendroth J, Kreger AC, Hol WG: The dimer formed by the periplasmic domain of EpsL from the type 2 secretion system of Vibrio parahaemolyticus. J. Struct. Biol. 168, 313-322 (2009).
    • (2009) J. Struct. Biol. , vol.168 , pp. 313-322
    • Abendroth, J.1    Kreger, A.C.2    Hol, W.G.3
  • 93
    • 1842686182 scopus 로고    scopus 로고
    • The crystal structure of the periplasmic domain of the type II secretion system protein EpsM from Vibrio cholerae: The simplest version of the ferredoxin fold
    • Abendroth J, Rice AE, McLuskey K, Bagdasarian M, Hol WG: The crystal structure of the periplasmic domain of the type II secretion system protein EpsM from Vibrio cholerae: the simplest version of the ferredoxin fold. J. Mol. Biol. 338, 585-596 (2004).
    • (2004) J. Mol. Biol. , vol.338 , pp. 585-596
    • Abendroth, J.1    Rice, A.E.2    McLuskey, K.3    Bagdasarian, M.4    Hol, W.G.5
  • 94
    • 7944233830 scopus 로고    scopus 로고
    • The structure of the cytoplasmic domain of EpsL, an inner membrane component of the type II secretion system of Vibrio cholerae: An unusual member of the actin-like ATPase superfamily
    • Abendroth J, Bagdasarian M, Sandkvist M, Hol WG: The structure of the cytoplasmic domain of EpsL, an inner membrane component of the type II secretion system of Vibrio cholerae: an unusual member of the actin-like ATPase superfamily. J. Mol. Biol. 344, 619-633 (2004).
    • (2004) J. Mol. Biol. , vol.344 , pp. 619-633
    • Abendroth, J.1    Bagdasarian, M.2    Sandkvist, M.3    Hol, W.G.4
  • 95
    • 0032909439 scopus 로고    scopus 로고
    • Direct interaction of the EpsL and EpsM proteins of the general secretion apparatus in Vibrio cholerae
    • Sandkvist M, Hough LP, Bagdasarian MM, Bagdasarian M: Direct interaction of the EpsL and EpsM proteins of the general secretion apparatus in Vibrio cholerae. J. Bacteriol. 181, 3129-3135 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 3129-3135
    • Sandkvist, M.1    Hough, L.P.2    Bagdasarian, M.M.3    Bagdasarian, M.4
  • 96
    • 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, Filloux A: Mutual stabilization of the XcpZ and XcpY components of the secretory apparatus in Pseudomonas aeruginosa. Microbiology 144(Pt 12), 3379-3386 (1998).
    • (1998) Microbiology , vol.144 , Issue.PART 12 , pp. 3379-3386
    • Michel, G.1    Bleves, S.2    Ball, G.3    Lazdunski, A.4    Filloux, A.5
  • 97
    • 33646009982 scopus 로고    scopus 로고
    • Green fluorescent chimeras indicate nonpolar localization of pullulanase secreton components PulL and PulM
    • Buddelmeijer N, Francetic O, Pugsley AP: Green fluorescent chimeras indicate nonpolar localization of pullulanase secreton components PulL and PulM. J. Bacteriol. 188, 2928-2935 (2006).
    • (2006) J. Bacteriol. , vol.188 , pp. 2928-2935
    • Buddelmeijer, N.1    Francetic, O.2    Pugsley, A.P.3
  • 98
    • 0029043035 scopus 로고
    • Characterization of a five-gene cluster required for the biogenesis of type 4 fimbriae in Pseudomonas aeruginosa
    • Martin PR, Watson AA, McCaul TF, Mattick JS: Characterization of a five-gene cluster required for the biogenesis of type 4 fimbriae in Pseudomonas aeruginosa. Mol. Microbiol. 16, 497-508 (1995).
    • (1995) Mol. Microbiol. , vol.16 , pp. 497-508
    • Martin, P.R.1    Watson, A.A.2    McCaul, T.F.3    Mattick, J.S.4
  • 99
    • 17444370930 scopus 로고    scopus 로고
    • The X-ray structure of the type II secretion system complex formed by the N-terminal domain of EpsE and the cytoplasmic domain of EpsL of Vibrio cholerae
    • Abendroth J, Murphy P, Sandkvist M, Bagdasarian M, Hol WG: The X-ray structure of the type II secretion system complex formed by the N-terminal domain of EpsE and the cytoplasmic domain of EpsL of Vibrio cholerae. J. Mol. Biol. 348, 845-855 (2005).
    • (2005) J. Mol. Biol. , vol.348 , pp. 845-855
    • Abendroth, J.1    Murphy, P.2    Sandkvist, M.3    Bagdasarian, M.4    Hol, W.G.5
  • 100
    • 0032948809 scopus 로고    scopus 로고
    • Assembly of XcpR in the cytoplasmic membrane is required for extracellular protein secretion in Pseudomonas aeruginosa
    • Ball G, Chapon-Herve V, Bleves S, Michel G, Bally M: Assembly of XcpR in the cytoplasmic membrane is required for extracellular protein secretion in Pseudomonas aeruginosa. J. Bacteriol. 181, 382-388 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 382-388
    • Ball, G.1    Chapon-Herve, V.2    Bleves, S.3    Michel, G.4    Bally, M.5
  • 102
    • 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 JM, Bagdasarian M, Howard SP: 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).
    • (2000) J. Bacteriol. , vol.182 , pp. 742-748
    • Sandkvist, M.1    Keith, J.M.2    Bagdasarian, M.3    Howard, S.P.4
  • 103
    • 11144271157 scopus 로고    scopus 로고
    • Molecular analysis of the Vibrio cholerae type II secretion ATPase EpsE
    • Camberg JL, Sandkvist M: Molecular analysis of the Vibrio cholerae type II secretion ATPase EpsE. J. Bacteriol. 187, 249-256 (2005).
    • (2005) J. Bacteriol. , vol.187 , pp. 249-256
    • Camberg, J.L.1    Sandkvist, M.2
  • 104
    • 77954395497 scopus 로고    scopus 로고
    • Genome analysis of Moraxella catarrhalis strain RH4: A human respiratory tract pathogen
    • de Vries SP, van Hijum SA, Schueler W et al.: Genome analysis of Moraxella catarrhalis strain RH4: a human respiratory tract pathogen. J. Bacteriol. 192(14), 3574-3583 (2010).
    • (2010) J. Bacteriol. , vol.192 , Issue.14 , pp. 3574-3583
    • De Vries, S.P.1    Van Hijum, S.A.2    Schueler, W.3
  • 105
    • 13444282405 scopus 로고    scopus 로고
    • Cell division in cocci: Localization and properties of the Streptococcus pneumoniae FtsA protein
    • Lara B, Rico AI, Petruzzelli S et al.: Cell division in cocci: localization and properties of the Streptococcus pneumoniae FtsA protein. Mol. Microbiol. 55, 699-711 (2005).
    • (2005) Mol. Microbiol. , vol.55 , pp. 699-711
    • Lara, B.1    Rico, A.I.2    Petruzzelli, S.3
  • 106
    • 0024095917 scopus 로고
    • Determinations of the DNA sequence of the mreB gene and of the gene products of the mre region that function in formation of the rod shape of Escherichia coli cells
    • Doi M, Wachi M, Ishino F et al.: Determinations of the DNA sequence of the mreB gene and of the gene products of the mre region that function in formation of the rod shape of Escherichia coli cells. J. Bacteriol. 170, 4619-4624 (1988).
    • (1988) J. Bacteriol. , vol.170 , pp. 4619-4624
    • Doi, M.1    Wachi, M.2    Ishino, F.3
  • 107
    • 7044249483 scopus 로고    scopus 로고
    • Expression of type IV pili by Moraxella catarrhalis is essential for natural competence and is affected by iron limitation
    • Luke NR, Howlett AJ, Shao J, Campagnari AA: Expression of type IV pili by Moraxella catarrhalis is essential for natural competence and is affected by iron limitation. Infect. Immun. 72, 6262-6270 (2004).
    • (2004) Infect. Immun. , vol.72 , pp. 6262-6270
    • Luke, N.R.1    Howlett, A.J.2    Shao, J.3    Campagnari, A.A.4
  • 108
    • 2142755863 scopus 로고    scopus 로고
    • Presence of pili on the surface of Francisella tularensis
    • Gil H, Benach JL, Thanassi DG: Presence of pili on the surface of Francisella tularensis. Infect. Immun. 72, 3042-3047
    • Infect. Immun. , vol.72 , pp. 3042-3047
    • Gil, H.1    Benach, J.L.2    Thanassi, D.G.3
  • 109
    • 75049084936 scopus 로고    scopus 로고
    • Bacterial motility complexes require the actin-like protein, MreB and the Ras homologue, MglA
    • Mauriello EM, Mouhamar F, Nan B, Ducret A, Dai D, Zusman DR, Mignot T: Bacterial motility complexes require the actin-like protein, MreB and the Ras homologue, MglA. EMBO J. 29, 315-326 (2010).
    • (2010) EMBO J , vol.29 , pp. 315-326
    • Mauriello, E.M.1    Mouhamar, F.2    Nan, B.3    Ducret, A.4    Dai, D.5    Zusman, D.R.6    Mignot, T.7
  • 110
    • 77953509169 scopus 로고    scopus 로고
    • Surface association and the MreB cytoskeleton regulate pilus production, localization and function in Pseudomonas aeruginosa
    • Cowles KN, Gitai Z: Surface association and the MreB cytoskeleton regulate pilus production, localization and function in Pseudomonas aeruginosa. Mol. Microbiol. 76(6), 1411-1426 (2010).
    • (2010) Mol. Microbiol. , vol.76 , Issue.6 , pp. 1411-1426
    • Cowles, K.N.1    Gitai, Z.2
  • 111
    • 19544364291 scopus 로고    scopus 로고
    • Mutation analysis of the flp operon in Actinobacillus actinomycetemcomitans
    • Wang Y, Chen C: Mutation analysis of the flp operon in Actinobacillus actinomycetemcomitans. Gene 351, 61-71.
    • Gene , vol.351 , pp. 61-71
    • Wang, Y.1    Chen, C.2
  • 112
    • 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, Mattick JS: 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).
    • (1993) Mol. Microbiol. , vol.10 , pp. 233-243
    • Hobbs, M.1    Mattick, J.S.2
  • 113
    • 0025292817 scopus 로고
    • Products of three accessory genes, pilB, pilC, and pilD, are required for biogenesis of Pseudomonas aeruginosa pili
    • Nunn D, Bergman S, Lory S: Products of three accessory genes, pilB, pilC, and pilD, are required for biogenesis of Pseudomonas aeruginosa pili. J. Bacteriol. 172, 2911-2919 (1990).
    • (1990) J. Bacteriol. , vol.172 , pp. 2911-2919
    • Nunn, D.1    Bergman, S.2    Lory, S.3
  • 114
    • 0029030966 scopus 로고
    • Identification and characterization of pilG, a highly conserved pilus-assembly gene in pathogenic Neisseria
    • Tonjum T, Freitag NE, Namork E, Koomey M: Identification and characterization of pilG, a highly conserved pilus-assembly gene in pathogenic Neisseria. Mol. Microbiol. 16, 451-464 (1995).
    • (1995) Mol. Microbiol. , vol.16 , pp. 451-464
    • Tonjum, T.1    Freitag, N.E.2    Namork, E.3    Koomey, M.4
  • 115
    • 67349264483 scopus 로고    scopus 로고
    • The three-dimensional structure of the cytoplasmic domains of EpsF from the type 2 secretion system of Vibrio cholerae
    • Abendroth J, Mitchell DD, Korotkov KV et al.: The three-dimensional structure of the cytoplasmic domains of EpsF from the type 2 secretion system of Vibrio cholerae. J. Struct. Biol. 166, 303-315 (2009).
    • (2009) J. Struct. Biol. , vol.166 , pp. 303-315
    • Abendroth, J.1    Mitchell, D.D.2    Korotkov, K.V.3
  • 116
    • 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, Barras F: 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).
    • (1999) J. Mol. Biol. , vol.289 , pp. 659-670
    • Py, B.1    Loiseau, L.2    Barras, F.3
  • 117
    • 34249025852 scopus 로고    scopus 로고
    • Interaction domains in the Pseudomonas aeruginosa type II secretory apparatus component XcpS (GspF)
    • Arts J, de Groot A, Ball G et al.: Interaction domains in the Pseudomonas aeruginosa type II secretory apparatus component XcpS (GspF). Microbiology 153, 1582-1592 (2007).
    • (2007) Microbiology , vol.153 , pp. 1582-1592
    • Arts, J.1    De Groot, A.2    Ball, G.3
  • 118
    • 34548497618 scopus 로고    scopus 로고
    • Purification and three-dimensional electron microscopy structure of the Neisseria meningitidis type IV pilus biogenesis protein PilG
    • Collins RF, Saleem M, Derrick JP: Purification and three-dimensional electron microscopy structure of the Neisseria meningitidis type IV pilus biogenesis protein PilG. J. Bacteriol. 189, 6389-6396 (2007).
    • (2007) J. Bacteriol. , vol.189 , pp. 6389-6396
    • Collins, R.F.1    Saleem, M.2    Derrick, J.P.3
  • 119
    • 77953592412 scopus 로고    scopus 로고
    • Structure and oligomerization of the PilC type IV pilus biogenesis protein from Thermus thermophilus
    • Karuppiah V, Hassan D, Saleem M, Derrick JP: Structure and oligomerization of the PilC type IV pilus biogenesis protein from Thermus thermophilus. Proteins 78, 20492057 (2010).
    • (2010) Proteins , vol.78 , pp. 2049-2057
    • Karuppiah, V.1    Hassan, D.2    Saleem, M.3    Derrick, J.P.4
  • 120
    • 0034937029 scopus 로고    scopus 로고
    • Novel topology of BfpE, a cytoplasmic membrane protein required for type IV fimbrial biogenesis in enteropathogenic Escherichia coli
    • Blank TE, Donnenberg MS: Novel topology of BfpE, a cytoplasmic membrane protein required for type IV fimbrial biogenesis in enteropathogenic Escherichia coli. J. Bacteriol. 183, 4435-4450 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 4435-4450
    • Blank, T.E.1    Donnenberg, M.S.2
  • 121
    • 75749098143 scopus 로고    scopus 로고
    • Crystal structure analysis reveals Pseudomonas PilY1 as an essential calcium-dependent regulator of bacterial surface motility
    • Orans J, Johnson MD, Coggan KA et al.: Crystal structure analysis reveals Pseudomonas PilY1 as an essential calcium-dependent regulator of bacterial surface motility. Proc. Natl Acad. Sci. USA 107(3), 1065-1070 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , Issue.3 , pp. 1065-1070
    • Orans, J.1    Johnson, M.D.2    Coggan, K.A.3
  • 122
    • 0030574285 scopus 로고    scopus 로고
    • The molecular genetics of type-4 fimbriae in Pseudomonas aeruginosa -a review
    • Mattick JS, Whitchurch CB, Alm RA: The molecular genetics of type-4 fimbriae in Pseudomonas aeruginosa -a review. Gene 179, 147-155 (1996).
    • (1996) Gene , vol.179 , pp. 147-155
    • Mattick, J.S.1    Whitchurch, C.B.2    Alm, R.A.3
  • 123
    • 33847668562 scopus 로고    scopus 로고
    • Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility
    • Satyshur KA, Worzalla GA, Meyer LS et al.: Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility. Structure 15, 363-376 (2007).
    • (2007) Structure , vol.15 , pp. 363-376
    • Satyshur, K.A.1    Worzalla, G.A.2    Meyer, L.S.3
  • 124
    • 38849174766 scopus 로고    scopus 로고
    • Functional role of conserved residues in the characteristic secretion NTPase motifs of the Pseudomonas aeruginosa type IV pilus motor proteins PilB, PilT and PilU
    • Chiang P, Sampaleanu LM, Ayers M, Pahuta M, Howell PL, Burrows LL: Functional role of conserved residues in the characteristic secretion NTPase motifs of the Pseudomonas aeruginosa type IV pilus motor proteins PilB, PilT and PilU. Microbiology 154, 114-126 (2008).
    • (2008) Microbiology , vol.154 , pp. 114-126
    • Chiang, P.1    Sampaleanu, L.M.2    Ayers, M.3    Pahuta, M.4    Howell, P.L.5    Burrows, L.L.6
  • 125
    • 0141862137 scopus 로고    scopus 로고
    • Crystal structure of the extracellular protein secretion NTPase EpsE of Vibrio cholerae
    • Robien MA, Krumm BE, Sandkvist M, Hol WG: Crystal structure of the extracellular protein secretion NTPase EpsE of Vibrio cholerae. J. Mol. Biol. 333, 657-674 (2003).
    • (2003) J. Mol. Biol. , vol.333 , pp. 657-674
    • Robien, M.A.1    Krumm, B.E.2    Sandkvist, M.3    Hol, W.G.4
  • 126
    • 13244258306 scopus 로고    scopus 로고
    • Disparate subcellular localization patterns of Pseudomonas aeruginosa type IV pilus ATPases involved in twitching motility
    • Chiang P, Habash M, Burrows LL: Disparate subcellular localization patterns of Pseudomonas aeruginosa type IV pilus ATPases involved in twitching motility. J. Bacteriol. 187, 829-839 (2005).
    • (2005) J. Bacteriol. , vol.187 , pp. 829-839
    • Chiang, P.1    Habash, M.2    Burrows, L.L.3
  • 127
    • 33645734928 scopus 로고    scopus 로고
    • XpsE oligomerization triggered by ATP binding, not hydrolysis, leads to its association with XpsL
    • Shiue SJ, Kao KM, Leu WM et al.: XpsE oligomerization triggered by ATP binding, not hydrolysis, leads to its association with XpsL. EMBO J. 25, 1426-1435 (2006).
    • (2006) EMBO J , vol.25 , pp. 1426-1435
    • Shiue, S.J.1    Kao, K.M.2    Leu, W.M.3
  • 128
    • 20444488138 scopus 로고    scopus 로고
    • Structural characterization of the molecular platform for type III secretion system assembly
    • Yip CK, Kimbrough TG, Felise HB et al.: Structural characterization of the molecular platform for type III secretion system assembly. Nature 435, 702-707 (2005).
    • (2005) Nature , vol.435 , pp. 702-707
    • Yip, C.K.1    Kimbrough, T.G.2    Felise, H.B.3
  • 129
    • 0032726290 scopus 로고    scopus 로고
    • Genetic dissection of the outer membrane secretin PulD: Are there distinct domains for multimerization and secretion specificity?
    • Guilvout I, Hardie KR, Sauvonnet N, Pugsley AP: Genetic dissection of the outer membrane secretin PulD: are there distinct domains for multimerization and secretion specificity? J. Bacteriol. 181, 7212-7220 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 7212-7220
    • Guilvout, I.1    Hardie, K.R.2    Sauvonnet, N.3    Pugsley, A.P.4
  • 130
    • 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, Condemine G, Shevchik VE: 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. 308, 205-219 (2001).
    • (2001) J. Mol. Biol. , vol.308 , pp. 205-219
    • Bouley, J.1    Condemine, G.2    Shevchik, V.E.3


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