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Journal of Bacteriology
Volumn 196, Issue 2, 2014, Pages 378-390
Outside-in assembly pathway of the type IV pilus system in myxococcus xanthus
Author keywords

[No Author keywords available]
Indexed keywords

ADENOSINE TRIPHOSPHATASE; LIPOPROTEIN; PILB PROTEIN; PILIN; PILN PROTEIN; PILO PROTEIN; PILP PROTEIN; PILQ SECRETIN RING; SECRETIN; TGL PROTEIN; UNCLASSIFIED DRUG;
EID: 84890921046     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01094-13     Document Type: Article
Times cited : (72)
References (83)
  • 1
    • 42649085698 scopus 로고    scopus 로고
    • Type IV pili: e pluribus unum?
    • Pelicic V. 2008. Type IV pili: e pluribus unum? Mol. Microbiol. 68:827-837. http://dx.doi.org/10.1111/j.1365-2958.2008.06197.x.
    • (2008) Mol. Microbiol. , vol.68 , pp. 827-837
    • Pelicic, V.1
  • 2
    • 2442589577 scopus 로고    scopus 로고
    • Type IV pilus structure and bacterial pathogenecity
    • Craig L, Pique ME, Tainer JA. 2004. Type IV pilus structure and bacterial pathogenecity. Nat. Rev. Microbiol. 2:363-378. http://dx.doi.org/10.1038/nrmicro885.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 363-378
    • Craig, L.1    Pique, M.E.2    Tainer, J.A.3
  • 3
    • 0141818949 scopus 로고    scopus 로고
    • Involvement of bacterial migration in the development of complex multicellular structures in Pseudomonas aeruginosa biofilms
    • Klausen M, Aaes-Jorgensen A, Molin S, Tolker-Nielsen T. 2003. Involvement of bacterial migration in the development of complex multicellular structures in Pseudomonas aeruginosa biofilms. Mol. Microbiol. 50:61-68. http://dx.doi.org/10.1046/j.1365-2958.2003.03677.x.
    • (2003) Mol. Microbiol. , vol.50 , pp. 61-68
    • Klausen, M.1    Aaes-Jorgensen, A.2    Molin, S.3    Tolker-Nielsen, T.4
  • 4
    • 0031724115 scopus 로고    scopus 로고
    • Flagellar and twitching motility are necessary for Pseudomonas aeruginosa biofilm development
    • O'Toole GA, Kolter R. 1998. Flagellar and twitching motility are necessary for Pseudomonas aeruginosa biofilm development. Mol. Microbiol. 30:295-304. http://dx.doi.org/10.1046/j.1365-2958.1998.01062.x.
    • (1998) Mol. Microbiol. , vol.30 , pp. 295-304
    • O'Toole, G.A.1    Kolter, R.2
  • 5
    • 0036405357 scopus 로고    scopus 로고
    • Type IV pili and twitching motility
    • Mattick JS. 2002. Type IV pili and twitching motility. Annu. Rev. Microbiol. 56:289-314. http://dx.doi.org/10.1146/annurev.micro.56.012302.160938.
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 289-314
    • Mattick, J.S.1
  • 7
    • 3042596928 scopus 로고    scopus 로고
    • DNA uptake during bacterial transformation
    • Chen I, Dubnau D. 2004. DNA uptake during bacterial transformation. Nat. Rev. Microbiol. 2:241-249. http://dx.doi.org/10.1038/nrmicro844.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 241-249
    • Chen, I.1    Dubnau, D.2
  • 8
    • 0034618643 scopus 로고    scopus 로고
    • Pilus retraction powers bacterial twitching motility
    • Merz AJ, So M, Sheetz MP. 2000. Pilus retraction powers bacterial twitching motility. Nature 407:98-102. http://dx.doi.org/10.1038/35024105.
    • (2000) Nature , vol.407 , pp. 98-102
    • Merz, A.J.1    So, M.2    Sheetz, M.P.3
  • 9
    • 0035810950 scopus 로고    scopus 로고
    • Direct observation of extension and retraction of type IV pili
    • Skerker JM, Berg HC. 2001. Direct observation of extension and retraction of type IV pili. Proc. Natl. Acad. Sci. U. S. A. 98:6901-6904. http://dx.doi.org/10.1073/pnas.121171698.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 6901-6904
    • Skerker, J.M.1    Berg, H.C.2
  • 10
    • 75249090304 scopus 로고    scopus 로고
    • Antivirulence drugs to target bacterial secretion systems
    • Baron C. 2010. Antivirulence drugs to target bacterial secretion systems. Curr. Opin. Microbiol. 13:100-105. http://dx.doi.org/10.1016/j.mib.2009.12.003.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 100-105
    • Baron, C.1
  • 11
    • 41949117894 scopus 로고    scopus 로고
    • Type IV pili: paradoxes in form and function
    • Craig L, Li J. 2008. Type IV pili: paradoxes in form and function. Curr. Opin. Struct. Biol. 18:267-277. http://dx.doi.org/10.1016/j.sbi.2007.12.009.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 267-277
    • Craig, L.1    Li, J.2
  • 13
    • 67650321575 scopus 로고    scopus 로고
    • High force generation is a conserved property of type IV pilus systems
    • Clausen M, Jakovljevic V, Søgaard-Andersen L, Maier B. 2009. High force generation is a conserved property of type IV pilus systems. J. Bacteriol. 191:4633-4638. http://dx.doi.org/10.1128/JB.00396-09.
    • (2009) J. Bacteriol. , vol.191 , pp. 4633-4638
    • Clausen, M.1    Jakovljevic, V.2    Søgaard-Andersen, L.3    Maier, B.4
  • 14
    • 0027385590 scopus 로고
    • Structure-function and biogenesis of the type IV pili
    • Strom MS, Lory S. 1993. Structure-function and biogenesis of the type IV pili. Annu. Rev. Microbiol. 47:565-596. http://dx.doi.org/10.1146/annurev.mi.47.100193.003025.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 565-596
    • Strom, M.S.1    Lory, S.2
  • 15
    • 0345306190 scopus 로고    scopus 로고
    • Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella
    • Peabody CR, Chung YJ, Yen M-R, Vidal-Ingigliardi D, Pugsley AP, Saier MH, Jr. 2003 Type II protein secretion and its relationship to bacterial type IV pili and archaeal flagella. Microbiology 149:3051-3072. http://dx.doi.org/10.1099/mic.0.26364-0.
    • (2003) Microbiology , vol.149 , pp. 3051-3072
    • Peabody, C.R.1    Chung, Y.J.2    Yen, M.-R.3    Vidal-Ingigliardi, D.4    Pugsley, A.P.5    Saier, M.H.6
  • 16
    • 84859885138 scopus 로고    scopus 로고
    • The type II secretion system: biogenesis, molecular architecture and mechanism
    • Korotkov KV, Sandkvist M, Hol WG. 2012. The type II secretion system: biogenesis, molecular architecture and mechanism. Nat. Rev. Microbiol. 10:336-351. http://dx.doi.org/10.1038/nrmicro2762.
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 336-351
    • Korotkov, K.V.1    Sandkvist, M.2    Hol, W.G.3
  • 17
    • 0035957004 scopus 로고    scopus 로고
    • Phylogeny of genes for secretion NTPases: identification of the widespread tadA subfamily and development of a diagnostic key for gene classification
    • Planet PJ, Kachlany SC, DeSalle R, Figurski DH. 2001. Phylogeny of genes for secretion NTPases: identification of the widespread tadA subfamily and development of a diagnostic key for gene classification. Proc. Natl. Acad. Sci. U. S. A. 98:2503-2508. http://dx.doi.org/10.1073/pnas.051436598.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 2503-2508
    • Planet, P.J.1    Kachlany, S.C.2    DeSalle, R.3    Figurski, D.H.4
  • 18
    • 0027489247 scopus 로고
    • Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and proteinsecretion apparatus: a general system for the formation of surfaceassociated protein complexes
    • Hobbs M, Mattick JS. 1993. Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and proteinsecretion apparatus: a general system for the formation of surfaceassociated protein complexes. Mol. Microbiol. 10:233-243. http://dx.doi.org/10.1111/j.1365-2958.1993.tb01949.x.
    • (1993) Mol. Microbiol. , vol.10 , pp. 233-243
    • Hobbs, M.1    Mattick, J.S.2
  • 19
    • 0034657719 scopus 로고    scopus 로고
    • Pilus formation and protein secretion by the same machinery in Escherichia coli
    • Sauvonnet N, Vignon G, Pugsley AP, Gounon P. 2000. Pilus formation and protein secretion by the same machinery in Escherichia coli. EMBO J. 19:2221-2228. http://dx.doi.org/10.1093/emboj/19.10.2221.
    • (2000) EMBO J. , vol.19 , pp. 2221-2228
    • Sauvonnet, N.1    Vignon, G.2    Pugsley, A.P.3    Gounon, P.4
  • 20
    • 0030911423 scopus 로고    scopus 로고
    • Specific interaction between OutD, an Erwinia chrysanthemi outer membrane protein of the general secretory pathway, and secreted proteins
    • Shevchik VE, Robert-Baudouy J, Condemine G. 1997. Specific interaction between OutD, an Erwinia chrysanthemi outer membrane protein of the general secretory pathway, and secreted proteins. EMBO J. 16:3007-3016. http://dx.doi.org/10.1093/emboj/16.11.3007.
    • (1997) EMBO J. , vol.16 , pp. 3007-3016
    • Shevchik, V.E.1    Robert-Baudouy, J.2    Condemine, G.3
  • 21
    • 33947397246 scopus 로고    scopus 로고
    • Signal recognition particle-dependent inner membrane targeting of the PulG pseudopilin component of a type II secretion system
    • Francetic O, Buddelmeijer N, Lewenza S, Kumamoto CA, Pugsley AP. 2007. Signal recognition particle-dependent inner membrane targeting of the PulG pseudopilin component of a type II secretion system. J. Bacteriol. 189:1783-1793. http://dx.doi.org/10.1128/JB.01230-06.
    • (2007) J. Bacteriol. , vol.189 , pp. 1783-1793
    • Francetic, O.1    Buddelmeijer, N.2    Lewenza, S.3    Kumamoto, C.A.4    Pugsley, A.P.5
  • 22
    • 33947360771 scopus 로고    scopus 로고
    • Export of the pseudopilin XcpT of the Pseudomonas aeruginosa type II secretion system via the signal recognition particle-Sec pathway
    • Arts J, van Boxtel R, Filloux A, Tommassen J, Koster M. 2007. Export of the pseudopilin XcpT of the Pseudomonas aeruginosa type II secretion system via the signal recognition particle-Sec pathway. J. Bacteriol. 189:2069-2076. http://dx.doi.org/10.1128/JB.01236-06.
    • (2007) J. Bacteriol. , vol.189 , pp. 2069-2076
    • Arts, J.1    van Boxtel, R.2    Filloux, A.3    Tommassen, J.4    Koster, M.5
  • 23
    • 0026345424 scopus 로고
    • Product of the Pseudomonas aeruginosa gene pilD is a prepilin leader peptidase
    • Nunn DN, Lory S. 1991. Product of the Pseudomonas aeruginosa gene pilD is a prepilin leader peptidase. Proc. Natl. Acad. Sci. U. S. A. 88:3281-3285. http://dx.doi.org/10.1073/pnas.88.8.3281.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 3281-3285
    • Nunn, D.N.1    Lory, S.2
  • 24
    • 0025978598 scopus 로고
    • Amino acid substitutions in pilin of Pseudomonas aeruginosa. Effect on leader peptide cleavage, amino-terminal methylation, and pilus assembly
    • Strom MS, 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
  • 26
    • 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. 2001. Analysis of the PilQ secretin from Neisseria meningitidis by transmission electron microscopy reveals a dodecameric quaternary structure. J. Bacteriol. 183:3825-3832. http://dx.doi.org/10.1128/JB.183.13.3825-3832.2001.
    • (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
  • 27
    • 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. 2004. Structure of the Neisseria meningitidis outer membrane PilQ secretin complex at 12 A resolution. J. Biol. Chem. 279:39750-39756. http://dx.doi.org/10.1074/jbc.M405971200.
    • (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
  • 28
    • 79551629041 scopus 로고    scopus 로고
    • Structural characterization of outer membrane components of the type IV pili system in pathogenic Neisseria
    • Jain S, Moscicka KB, Bos MP, Pachulec E, Stuart MC, Keegstra W, Boekema EJ, van der Does C. 2011. Structural characterization of outer membrane components of the type IV pili system in pathogenic Neisseria. PLoS One 6:e16624. http://dx.doi.org/10.1371/journal.pone.0016624.
    • (2011) PLoS One , vol.6
    • Jain, S.1    Moscicka, K.B.2    Bos, M.P.3    Pachulec, E.4    Stuart, M.C.5    Keegstra, W.6    Boekema, E.J.7    van der Does, C.8
  • 29
    • 79953227678 scopus 로고    scopus 로고
    • Structure and function of PilQ, a secretin of the DNA transporter from the thermophilic bacterium Thermus thermophilus HB27
    • Burkhardt J, Vonck J, Averhoff B. 2011. Structure and function of PilQ, a secretin of the DNA transporter from the thermophilic bacterium Thermus thermophilus HB27. J. Biol. Chem. 286:9977-9984. http://dx.doi.org/10.1074/jbc.M110.212688.
    • (2011) J. Biol. Chem. , vol.286 , pp. 9977-9984
    • Burkhardt, J.1    Vonck, J.2    Averhoff, B.3
  • 30
    • 0034406525 scopus 로고    scopus 로고
    • Components and dynamics of fiber formation define a ubiquitous biogenesis pathway for bacterial pili
    • Wolfgang M, van Putten JPM, Hayes SF, Dorward D, Koomey M. 2000. Components and dynamics of fiber formation define a ubiquitous biogenesis pathway for bacterial pili. EMBO J. 19:6408-6418. http://dx.doi.org/10.1093/emboj/19.23.6408.
    • (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
  • 31
    • 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. 1996. Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein. EMBO J. 15:978-988.
    • (1996) EMBO J. , vol.15 , pp. 978-988
    • Hardie, K.R.1    Lory, S.2    Pugsley, A.P.3
  • 32
    • 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. 2008. PilF is an outer membrane lipoprotein required for multimerization and localization of the Pseudomonas aeruginosa type IV pilus secretin. J. Bacteriol. 190:6961-6969. http://dx.doi.org/10.1128/JB.00996-08.
    • (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
  • 33
    • 33644848512 scopus 로고    scopus 로고
    • Polar assembly of the type IV pilus secretin in Myxococcus xanthus
    • Nudleman E, Wall D, Kaiser D. 2006. Polar assembly of the type IV pilus secretin in Myxococcus xanthus. Mol. Microbiol. 60:16-29. http://dx.doi.org/10.1111/j.1365-2958.2006.05095.x.
    • (2006) Mol. Microbiol. , vol.60 , pp. 16-29
    • Nudleman, E.1    Wall, D.2    Kaiser, D.3
  • 34
    • 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. 2005. 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. http://dx.doi.org/10.1111/j.1365-2958.2004.04364.x.
    • (2005) Mol. Microbiol. , vol.55 , pp. 54-64
    • Carbonnelle, E.1    Helaine, S.2    Prouvensier, L.3    Nassif, X.4    Pelicic, V.5
  • 35
    • 84861340405 scopus 로고    scopus 로고
    • Large-scale study of the interactions between proteins involved in type IV pilus biology in Neisseria meningitidis: characterization of a subcomplex involved in pilus assembly
    • Georgiadou M, Castagnini M, Karimova G, Ladant D, Pelicic V. 2012. Large-scale study of the interactions between proteins involved in type IV pilus biology in Neisseria meningitidis: characterization of a subcomplex involved in pilus assembly. Mol. Microbiol. 84:857-873. http://dx.doi.org/10.1111/j.1365-2958.2012.08062.x.
    • (2012) Mol. Microbiol. , vol.84 , pp. 857-873
    • Georgiadou, M.1    Castagnini, M.2    Karimova, G.3    Ladant, D.4    Pelicic, V.5
  • 37
    • 84880764637 scopus 로고    scopus 로고
    • Type IV pilus proteins form an integrated structure extending from the cytoplasm to the outer membrane
    • Li C, Wallace RA, Black WP, Li YZ, Yang Z. 2013. Type IV pilus proteins form an integrated structure extending from the cytoplasm to the outer membrane. PLoS One 8:e70144. http://dx.doi.org/10.1371/journal.pone.0070144.
    • (2013) PLoS One , vol.8
    • Li, C.1    Wallace, R.A.2    Black, W.P.3    Li, Y.Z.4    Yang, Z.5
  • 39
    • 0031025472 scopus 로고    scopus 로고
    • PilP, a pilus biogenesis lipoprotein in Neisseria gonorrhoeae, affects expression of PilQ as a highmolecular-mass multimer
    • Drake SL, Sandstedt SA, Koomey M. 1997. PilP, a pilus biogenesis lipoprotein in Neisseria gonorrhoeae, affects expression of PilQ as a highmolecular-mass multimer. Mol. Microbiol. 23:657-668. http://dx.doi.org/10.1046/j.1365-2958.1997.2511618.x.
    • (1997) Mol. Microbiol. , vol.23 , pp. 657-668
    • Drake, S.L.1    Sandstedt, S.A.2    Koomey, M.3
  • 40
    • 84877065344 scopus 로고    scopus 로고
    • PilMNOPQ from the Pseudomonas aeruginosa type IV pilus system form a transenvelope protein interaction network that interacts with PilA
    • Tammam S, Sampaleanu LM, Koo J, Manoharan K, Daubaras M, Burrows LL, Howell PL. 2013. PilMNOPQ from the Pseudomonas aeruginosa type IV pilus system form a transenvelope protein interaction network that interacts with PilA. J. Bacteriol. 195:2126-2135. http://dx.doi.org/10.1128/JB.00032-13.
    • (2013) J. Bacteriol. , vol.195 , pp. 2126-2135
    • Tammam, S.1    Sampaleanu, L.M.2    Koo, J.3    Manoharan, K.4    Daubaras, M.5    Burrows, L.L.6    Howell, P.L.7
  • 43
    • 79959912261 scopus 로고    scopus 로고
    • Structure of the PilM-PilN inner membrane type IV pilus biogenesis complex from Thermus thermophilus
    • Karuppiah V, Derrick JP. 2011. Structure of the PilM-PilN inner membrane type IV pilus biogenesis complex from Thermus thermophilus. J. Biol. Chem. 286:24434-24442. http://dx.doi.org/10.1074/jbc.M111.243535.
    • (2011) J. Biol. Chem. , vol.286 , pp. 24434-24442
    • Karuppiah, V.1    Derrick, J.P.2
  • 44
    • 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. 2009. 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. http://dx.doi.org/10.1016/j.jmb.2009.09.034.
    • (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
  • 45
    • 21644439403 scopus 로고    scopus 로고
    • The ATPase activity of BfpD is greatly enhanced by zinc and allosteric interactions with other Bfp proteins
    • Crowther LJ, Yamagata A, Craig L, Tainer JA, Donnenberg MS. 2005. The ATPase activity of BfpD is greatly enhanced by zinc and allosteric interactions with other Bfp proteins. J. Biol. Chem. 280:24839-24848. http://dx.doi.org/10.1074/jbc.M500253200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 24839-24848
    • Crowther, L.J.1    Yamagata, A.2    Craig, L.3    Tainer, J.A.4    Donnenberg, M.S.5
  • 46
    • 0035947655 scopus 로고    scopus 로고
    • ATPase activity and multimer formation of PilQ protein are required for thin pilus biogenesis in plasmid R64
    • Sakai D, Horiuchi T, Komano T. 2001. ATPase activity and multimer formation of PilQ protein are required for thin pilus biogenesis in plasmid R64. J. Biol. Chem. 276:17968-17975. http://dx.doi.org/10.1074/jbc.M010652200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17968-17975
    • Sakai, D.1    Horiuchi, T.2    Komano, T.3
  • 47
    • 41549119041 scopus 로고    scopus 로고
    • PilB and PilT are ATPases acting antagonistically in type IV pili function in Myxococcus xanthus
    • Jakovljevic V, Leonardy S, Hoppert M, Søgaard-Andersen L. 2008. PilB and PilT are ATPases acting antagonistically in type IV pili function in Myxococcus xanthus. J. Bacteriol. 190:2411-2421. http://dx.doi.org/10.1128/JB.01793-07.
    • (2008) J. Bacteriol. , vol.190 , pp. 2411-2421
    • Jakovljevic, V.1    Leonardy, S.2    Hoppert, M.3    Søgaard-Andersen, L.4
  • 48
    • 84875973097 scopus 로고    scopus 로고
    • The platform protein is essential for type IV pilus biogenesis
    • Takhar HK, Kemp K, Kim M, Howell PL, Burrows LL. 2013. The platform protein is essential for type IV pilus biogenesis. J. Biol. Chem. 288:9721-9728. http://dx.doi.org/10.1074/jbc.M113.453506.
    • (2013) J. Biol. Chem. , vol.288 , pp. 9721-9728
    • Takhar, H.K.1    Kemp, K.2    Kim, M.3    Howell, P.L.4    Burrows, L.L.5
  • 49
    • 0032949378 scopus 로고    scopus 로고
    • Type IV pili and cell motility
    • Wall D, Kaiser D. 1999. Type IV pili and cell motility. Mol. Microbiol. 32:1-10. http://dx.doi.org/10.1046/j.1365-2958.1999.01339.x.
    • (1999) Mol. Microbiol. , vol.32 , pp. 1-10
    • Wall, D.1    Kaiser, D.2
  • 50
    • 0029591872 scopus 로고
    • Genetic and functional evidence that Type IV pili are required for social gliding motility in Myxococcus xanthus
    • Wu SS, Kaiser D. 1995. Genetic and functional evidence that Type IV pili are required for social gliding motility in Myxococcus xanthus. Mol. Microbiol. 18:547-558. http://dx.doi.org/10.1111/j.1365-2958.1995.mmi_18030547.x.
    • (1995) Mol. Microbiol. , vol.18 , pp. 547-558
    • Wu, S.S.1    Kaiser, D.2
  • 51
    • 0018536781 scopus 로고
    • Social gliding is correlated with the presence of pili in Myxococcus xanthus
    • Kaiser D. 1979. Social gliding is correlated with the presence of pili in Myxococcus xanthus. Proc. Natl. Acad. Sci. U. S. A. 76:5952-5956. http://dx.doi.org/10.1073/pnas.76.11.5952.
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 5952-5956
    • Kaiser, D.1
  • 52
    • 0022312753 scopus 로고
    • "Frizzy" genes of Myxococcus xanthus are involved in control of frequency of reversal of gliding motility
    • Blackhart BD, Zusman DR. 1985. "Frizzy" genes of Myxococcus xanthus are involved in control of frequency of reversal of gliding motility. Proc. Natl. Acad. Sci. U. S. A. 82:8767-8770. http://dx.doi.org/10.1073/pnas.82.24.8771.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 8767-8770
    • Blackhart, B.D.1    Zusman, D.R.2
  • 53
    • 0034699345 scopus 로고    scopus 로고
    • Type IV pilus of Myxococcus xanthus is a motility apparatus controlled by the frz chemosensory system
    • Sun H, Zusman DR, Shi W. 2000. Type IV pilus of Myxococcus xanthus is a motility apparatus controlled by the frz chemosensory system. Curr. Biol. 10:1143-1146. http://dx.doi.org/10.1016/S0960-9822(00)00705-3.
    • (2000) Curr. Biol. , vol.10 , pp. 1143-1146
    • Sun, H.1    Zusman, D.R.2    Shi, W.3
  • 55
    • 27644473066 scopus 로고    scopus 로고
    • Regulated pole-to-pole oscillations of a bacterial gliding motility protein
    • Mignot T, Merlie JP, Jr, Zusman DR. 2005. Regulated pole-to-pole oscillations of a bacterial gliding motility protein. Science 310:855-857. http://dx.doi.org/10.1126/science.1119052.
    • (2005) Science , vol.310 , pp. 855-857
    • Mignot, T.1    Merlie, J.P.2    Zusman, D.R.3
  • 56
    • 77953521591 scopus 로고    scopus 로고
    • PilA localization affects extracellular polysaccharide production and fruiting body formation in Myxococcus xanthus
    • Yang Z, Lux R, Hu W, Hu C, Shi W. 2010. PilA localization affects extracellular polysaccharide production and fruiting body formation in Myxococcus xanthus. Mol. Microbiol. 76:1500-1513. http://dx.doi.org/10.1111/j.1365-2958.2010.07180.x.
    • (2010) Mol. Microbiol. , vol.76 , pp. 1500-1513
    • Yang, Z.1    Lux, R.2    Hu, W.3    Hu, C.4    Shi, W.5
  • 57
    • 0017387488 scopus 로고
    • Cell-to-cell stimulation of movement in nonmotile mutants of Myxococcus
    • Hodgkin J, Kaiser D. 1977. Cell-to-cell stimulation of movement in nonmotile mutants of Myxococcus. Proc. Natl. Acad. Sci. U. S. A. 74:2938-2942. http://dx.doi.org/10.1073/pnas.74.7.2938.
    • (1977) Proc. Natl. Acad. Sci. U. S. A. , vol.74 , pp. 2938-2942
    • Hodgkin, J.1    Kaiser, D.2
  • 58
    • 38749132556 scopus 로고    scopus 로고
    • Bioinformatics and experimental analysis of proteins of two-component systems in Myxococcus xanthus
    • Shi X, Wegener-Feldbrügge S, Huntley S, Hamann N, Hedderich R, Søgaard-Andersen L. 2008. Bioinformatics and experimental analysis of proteins of two-component systems in Myxococcus xanthus. J. Bacteriol. 190:613-624. http://dx.doi.org/10.1128/JB.01502-07.
    • (2008) J. Bacteriol. , vol.190 , pp. 613-624
    • Shi, X.1    Wegener-Feldbrügge, S.2    Huntley, S.3    Hamann, N.4    Hedderich, R.5    Søgaard-Andersen, L.6
  • 59
    • 0003903343 scopus 로고    scopus 로고
    • Molecular cloning: a laboratory manual, 3rd ed
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sambrook J, Russell DW. 2001. Molecular cloning: a laboratory manual, 3rd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2001)
    • Sambrook, J.1    Russell, D.W.2
  • 60
    • 14044253538 scopus 로고    scopus 로고
    • Analysis of type IV pilus and its associated motility in Myxococcus xanthus using an antibody reactive with native pilin and pili
    • Li Y, Lux R, Pelling AE, Gimzewski JK, Shi W. 2005. Analysis of type IV pilus and its associated motility in Myxococcus xanthus using an antibody reactive with native pilin and pili. Microbiology 151:353-360. http://dx.doi.org/10.1099/mic.0.27614-0.
    • (2005) Microbiology , vol.151 , pp. 353-360
    • Li, Y.1    Lux, R.2    Pelling, A.E.3    Gimzewski, J.K.4    Shi, W.5
  • 61
    • 35648967684 scopus 로고    scopus 로고
    • Coupling of protein localization and cell movements by a dynamically localized response regulator in Myxococcus xanthus
    • Leonardy S, Freymark G, Hebener S, Ellehauge E, Søgaard-Andersen L. 2007. Coupling of protein localization and cell movements by a dynamically localized response regulator in Myxococcus xanthus. EMBO J. 26:4433-4444. http://dx.doi.org/10.1038/sj.emboj.7601877.
    • (2007) EMBO J. , vol.26 , pp. 4433-4444
    • Leonardy, S.1    Freymark, G.2    Hebener, S.3    Ellehauge, E.4    Søgaard-Andersen, L.5
  • 62
    • 33744972113 scopus 로고    scopus 로고
    • The orphan response regulator DigR is required for synthesis of extracellular matrix fibrils in Myxococcus xanthus
    • Overgaard M, Wegener-Feldbrügge S, Søgaard-Andersen L. 2006. The orphan response regulator DigR is required for synthesis of extracellular matrix fibrils in Myxococcus xanthus. J. Bacteriol. 188:4384-4394. http://dx.doi.org/10.1128/JB.00189-06.
    • (2006) J. Bacteriol. , vol.188 , pp. 4384-4394
    • Overgaard, M.1    Wegener-Feldbrügge, S.2    Søgaard-Andersen, L.3
  • 63
    • 0030808285 scopus 로고    scopus 로고
    • Identification and localization of the Tgl protein, which is required for Myxococcus xanthus social motility
    • Rodriguez-Soto JP, Kaiser D. 1997. Identification and localization of the Tgl protein, which is required for Myxococcus xanthus social motility. J. Bacteriol. 179:4372-4381.
    • (1997) J. Bacteriol. , vol.179 , pp. 4372-4381
    • Rodriguez-Soto, J.P.1    Kaiser, D.2
  • 64
    • 0027538171 scopus 로고
    • The two motility systems of Myxococcus xanthus show different selective advantages on various surfaces
    • Shi W, Zusman DR. 1993. The two motility systems of Myxococcus xanthus show different selective advantages on various surfaces. Proc. Natl. Acad. Sci. U. S. A. 90:3378-3382. http://dx.doi.org/10.1073/pnas.90.8.3378.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 3378-3382
    • Shi, W.1    Zusman, D.R.2
  • 65
    • 75749118268 scopus 로고    scopus 로고
    • Extracellular biology of Myxococcus xanthus
    • Konovalova A, Petters T, Søgaard-Andersen L. 2010. Extracellular biology of Myxococcus xanthus. FEMS Microbiol. Rev. 34:89-106. http://dx.doi.org/10.1111/j.1574-6976.2009.00194.x.
    • (2010) FEMS Microbiol. Rev. , vol.34 , pp. 89-106
    • Konovalova, A.1    Petters, T.2    Søgaard-Andersen, L.3
  • 66
    • 80052551898 scopus 로고    scopus 로고
    • Using Superfolder green fluorescent protein for periplasmic protein localization studies
    • Dinh T, Bernhardt TG. 2011. Using Superfolder green fluorescent protein for periplasmic protein localization studies. J. Bacteriol. 193:4984-4987. http://dx.doi.org/10.1128/JB.00315-11.
    • (2011) J. Bacteriol. , vol.193 , pp. 4984-4987
    • Dinh, T.1    Bernhardt, T.G.2
  • 67
    • 79953745092 scopus 로고    scopus 로고
    • Superfolder GFP is fluorescent in oxidizing environments when targeted via the Sec translocon
    • Aronson DE, Costantini LM, Snapp EL. 2011. Superfolder GFP is fluorescent in oxidizing environments when targeted via the Sec translocon. Traffic 12:543-548. http://dx.doi.org/10.1111/j.1600-0854.2011.01168.x.
    • (2011) Traffic , vol.12 , pp. 543-548
    • Aronson, D.E.1    Costantini, L.M.2    Snapp, E.L.3
  • 68
    • 65549139901 scopus 로고    scopus 로고
    • Docking and assembly of the type II secretion complex of Vibrio cholerae
    • Lybarger SR, Johnson TL, Gray MD, Sikora AE, Sandkvist M. 2009. Docking and assembly of the type II secretion complex of Vibrio cholerae. J. Bacteriol. 191:3149-3161. http://dx.doi.org/10.1128/JB.01701-08.
    • (2009) J. Bacteriol. , vol.191 , pp. 3149-3161
    • Lybarger, S.R.1    Johnson, T.L.2    Gray, M.D.3    Sikora, A.E.4    Sandkvist, M.5
  • 69
    • 33646009982 scopus 로고    scopus 로고
    • Green fluorescent chimeras indicate nonpolar localization of pullulanase secreton components PulL and PulM
    • Buddelmeijer N, Francetic O, Pugsley AP. 2006. Green fluorescent chimeras indicate nonpolar localization of pullulanase secreton components PulL and PulM. J. Bacteriol. 188:2928-2935. http://dx.doi.org/10.1128/JB.188.8.2928-2935.2006.
    • (2006) J. Bacteriol. , vol.188 , pp. 2928-2935
    • Buddelmeijer, N.1    Francetic, O.2    Pugsley, A.P.3
  • 70
    • 58149503629 scopus 로고    scopus 로고
    • Type II secretion system secretin PulD localizes in clusters in the Escherichia coli outer membrane
    • Buddelmeijer N, Krehenbrink M, Pecorari F, Pugsley AP. 2009. Type II secretion system secretin PulD localizes in clusters in the Escherichia coli outer membrane. J. Bacteriol. 191:161-168. http://dx.doi.org/10.1128/JB.01138-08.
    • (2009) J. Bacteriol. , vol.191 , pp. 161-168
    • Buddelmeijer, N.1    Krehenbrink, M.2    Pecorari, F.3    Pugsley, A.P.4
  • 71
    • 84872358471 scopus 로고    scopus 로고
    • New insights into the assembly of bacterial secretins: structural studies of the periplasmic domain of XcpQ from Pseudomonas aeruginosa
    • Van der Meeren R, Wen Y, Van Gelder P, Tommassen J, Devreese B, Savvides SN. 2013. New insights into the assembly of bacterial secretins: structural studies of the periplasmic domain of XcpQ from Pseudomonas aeruginosa. J. Biol. Chem. 288:1214-1225. http://dx.doi.org/10.1074/jbc.M112.432096.
    • (2013) J. Biol. Chem. , vol.288 , pp. 1214-1225
    • Van der Meeren, R.1    Wen, Y.2    Van Gelder, P.3    Tommassen, J.4    Devreese, B.5    Savvides, S.N.6
  • 72
    • 79961171407 scopus 로고    scopus 로고
    • Secretins: dynamic channels for protein transport across membranes
    • Korotkov KV, Gonen T, Hol WGJ. 2011. Secretins: dynamic channels for protein transport across membranes. TiBS 36:433-443. http://dx.doi.org/10.1016/j.tibs.2011.04.002.
    • (2011) TiBS , vol.36 , pp. 433-443
    • Korotkov, K.V.1    Gonen, T.2    Hol, W.G.J.3
  • 73
    • 77953123027 scopus 로고    scopus 로고
    • Deciphering the assembly of the Yersinia type III secretion injectisome
    • Diepold A, Amstutz M, Abel S, Sorg I, Jenal U, Cornelis GR. 2010. Deciphering the assembly of the Yersinia type III secretion injectisome. EMBO J. 29:1928-1940. http://dx.doi.org/10.1038/emboj.2010.84.
    • (2010) EMBO J. , vol.29 , pp. 1928-1940
    • Diepold, A.1    Amstutz, M.2    Abel, S.3    Sorg, I.4    Jenal, U.5    Cornelis, G.R.6
  • 74
    • 43849098574 scopus 로고    scopus 로고
    • Coordinating assembly of a bacterial macromolecular machine
    • Chevance FFV, Hughes KT. 2008. Coordinating assembly of a bacterial macromolecular machine. Nat. Rev. Microbiol. 6:455-465. http://dx.doi.org/10.1038/nrmicro1887.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 455-465
    • Chevance, F.F.V.1    Hughes, K.T.2
  • 75
    • 33846190237 scopus 로고    scopus 로고
    • Synergistic stimulation of EpsE ATP hydrolysis by EpsL and acidic phospholipids
    • Camberg JL, Johnson TL, Patrick M, Abendroth J, Hol WGJ, Sandkvist M. 2007. Synergistic stimulation of EpsE ATP hydrolysis by EpsL and acidic phospholipids. EMBO J. 26:19-27. http://dx.doi.org/10.1038/sj.emboj.7601481.
    • (2007) EMBO J. , vol.26 , pp. 19-27
    • Camberg, J.L.1    Johnson, T.L.2    Patrick, M.3    Abendroth, J.4    Hol, W.G.J.5    Sandkvist, M.6
  • 76
    • 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. 2001. An inner membrane platform in the type II secretion machinery of Gram-negative bacteria. EMBORep. 2:244-248. http://dx.doi.org/10.1093/embo-reports/kve042.
    • (2001) EMBORep. , vol.2 , pp. 244-248
    • Py, B.1    Loiseau, L.2    Barras, F.3
  • 78
    • 77954874614 scopus 로고    scopus 로고
    • Regulation of dynamic polarity switching in bacteria by a Ras-like G-protein and its cognate GAP
    • Leonardy S, Miertzschke M, Bulyha I, Sperling E, Wittinghofer A, Søgaard-Andersen L. 2010. Regulation of dynamic polarity switching in bacteria by a Ras-like G-protein and its cognate GAP. EMBO J. 29:2276-2289. http://dx.doi.org/10.1038/emboj.2010.114.
    • (2010) EMBO J. , vol.29 , pp. 2276-2289
    • Leonardy, S.1    Miertzschke, M.2    Bulyha, I.3    Sperling, E.4    Wittinghofer, A.5    Søgaard-Andersen, L.6
  • 79
    • 77955015657 scopus 로고    scopus 로고
    • A bacterial Ras-like small GTP-binding protein and its cognate GAP establish a dynamic spatial polarity axis to control directed motility
    • Zhang Y, Franco M, Ducret A, Mignot T. 2010. A bacterial Ras-like small GTP-binding protein and its cognate GAP establish a dynamic spatial polarity axis to control directed motility. PLoS Biol. 8:e1000430. http://dx.doi.org/10.1371/journal.pbio.1000430.
    • (2010) PLoS Biol. , vol.8
    • Zhang, Y.1    Franco, M.2    Ducret, A.3    Mignot, T.4
  • 80
    • 80054934194 scopus 로고    scopus 로고
    • Structural analysis of the Ras-like G protein MglA and its cognate GAP MglB and implications for bacterial polarity
    • Miertzschke M, Koerner C, Vetter IR, Keilberg D, Hot E, Leonardy S, Søgaard-Andersen L, Wittinghofer A. 2011. Structural analysis of the Ras-like G protein MglA and its cognate GAP MglB and implications for bacterial polarity. EMBO J. 30:4185-4197. http://dx.doi.org/10.1038/emboj.2011.291.
    • (2011) EMBO J. , vol.30 , pp. 4185-4197
    • Miertzschke, M.1    Koerner, C.2    Vetter, I.R.3    Keilberg, D.4    Hot, E.5    Leonardy, S.6    Søgaard-Andersen, L.7    Wittinghofer, A.8
  • 81
    • 0032901093 scopus 로고    scopus 로고
    • The Myxococcus xanthus pilQ (sglA) gene encodes a secretin homolog required for type IV pilus biogenesis, social motility, and development
    • Wall D, Kolenbrander PE, Kaiser D. 1999. The Myxococcus xanthus pilQ (sglA) gene encodes a secretin homolog required for type IV pilus biogenesis, social motility, and development. J. Bacteriol. 181:24-33.
    • (1999) J. Bacteriol. , vol.181 , pp. 24-33
    • Wall, D.1    Kolenbrander, P.E.2    Kaiser, D.3
  • 82
    • 0031021830 scopus 로고    scopus 로고
    • The Myxococcus xanthus pilT locus is required for social gliding motility although pili are still produced
    • Wu SS, Wu J, Kaiser D. 1997. The Myxococcus xanthus pilT locus is required for social gliding motility although pili are still produced. Mol. Microbiol. 23:109-121. http://dx.doi.org/10.1046/j.1365-2958.1997.1791550.x.
    • (1997) Mol. Microbiol. , vol.23 , pp. 109-121
    • Wu, S.S.1    Wu, J.2    Kaiser, D.3
  • 83
    • 0029796393 scopus 로고    scopus 로고
    • Markerless deletions of pil genes in Myxococcus xanthus generated by counterselection with the Bacillus subtilis sacB gene
    • Wu SS, Kaiser D. 1996. Markerless deletions of pil genes in Myxococcus xanthus generated by counterselection with the Bacillus subtilis sacB gene. J. Bacteriol. 178:5817-5821.
    • (1996) J. Bacteriol. , vol.178 , pp. 5817-5821
    • Wu, S.S.1    Kaiser, D.2

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