메뉴 건너뛰기




Volumn 111, Issue 10, 2014, Pages

Peptidoglycan-binding protein TsaP functions in surface assembly of type IV pili

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; LYSINE; PEPTIDOGLYCAN; SECRETIN; T4P SECRETIN ASSOCIATED PROTEIN; UNCLASSIFIED DRUG;

EID: 84896290115     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1322889111     Document Type: Article
Times cited : (55)

References (70)
  • 1
    • 84870671751 scopus 로고    scopus 로고
    • Type IV pilin proteins: Versatile molecular modules
    • Giltner CL, Nguyen Y, Burrows LL (2012) Type IV pilin proteins: Versatile molecular modules. Microbiol Mol Biol Rev 76(4):740-772.
    • (2012) Microbiol Mol Biol Rev , vol.76 , Issue.4 , pp. 740-772
    • Giltner, C.L.1    Nguyen, Y.2    Burrows, L.L.3
  • 2
    • 84862754646 scopus 로고    scopus 로고
    • The archaellum: An old motility structure with a new name
    • Jarrell KF, Albers SV (2012) The archaellum: An old motility structure with a new name. Trends Microbiol 20(7):307-312.
    • (2012) Trends Microbiol , vol.20 , Issue.7 , pp. 307-312
    • Jarrell, K.F.1    Albers, S.V.2
  • 3
    • 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(5):336-351.
    • (2012) Nat Rev Microbiol , vol.10 , Issue.5 , pp. 336-351
    • Korotkov, K.V.1    Sandkvist, M.2    Hol, W.G.3
  • 4
    • 0242360953 scopus 로고    scopus 로고
    • DNAtransport during transformation
    • Chen I, Dubnau D (2003) DNAtransport during transformation. Front Biosci 8:s544-s556.
    • (2003) Front Biosci , vol.8
    • Chen, I.1    Dubnau, D.2
  • 5
    • 42649085698 scopus 로고    scopus 로고
    • Type IV pili: E pluribus unum
    • Pelicic V (2008) Type IV pili: E pluribus unum? Mol Microbiol 68(4):827-837.
    • (2008) Mol Microbiol , vol.68 , Issue.4 , pp. 827-837
    • Pelicic, V.1
  • 6
    • 84870705958 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa twitching motility: Type IV pili in action
    • Burrows LL (2012) Pseudomonas aeruginosa twitching motility: Type IV pili in action. Annu Rev Microbiol 66:493-520.
    • (2012) Annu Rev Microbiol , vol.66 , pp. 493-520
    • Burrows, L.L.1
  • 7
    • 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(6800):98-102.
    • (2000) Nature , vol.407 , Issue.6800 , pp. 98-102
    • Merz, A.J.1    So, M.2    Sheetz, M.P.3
  • 8
    • 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 USA 98(12):6901-6904.
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.12 , pp. 6901-6904
    • Skerker, J.M.1    Berg, H.C.2
  • 9
    • 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 gen eration is a conserved property of type IV pilus systems. J Bacteriol 191(14): 4633-4638.
    • (2009) J Bacteriol , vol.191 , Issue.14 , pp. 4633-4638
    • Clausen, M.1    Jakovljevic, V.2    Søgaard-Andersen, L.3    Maier, B.4
  • 10
    • 0037058989 scopus 로고    scopus 로고
    • Single pilus motor forces exceed 100 pN
    • Maier B, et al. (2002) Single pilus motor forces exceed 100 pN. Proc Natl Acad Sci USA 99(25):16012-16017.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.25 , pp. 16012-16017
    • Maier, B.1
  • 11
    • 0029008485 scopus 로고
    • Characterization of the pilF-pilD pilus-assembly locus of Neisseria gonorrhoeae
    • Freitag NE, Seifert HS, Koomey M (1995) Characterization of the pilF-pilD pilus-assembly locus of Neisseria gonorrhoeae. Mol Microbiol 16(3):575-586.
    • (1995) Mol Microbiol , vol.16 , Issue.3 , pp. 575-586
    • Freitag, N.E.1    Seifert, H.S.2    Koomey, M.3
  • 12
    • 0027528605 scopus 로고
    • A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type IV pilin family
    • Strom MS, Nunn DN, Lory S (1993) A single bifunctional enzyme, PilD, catalyzes cleavage and N-methylation of proteins belonging to the type IV pilin family. Proc Natl Acad Sci USA 90(6):2404-2408.
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.6 , pp. 2404-2408
    • Strom, M.S.1    Nunn, D.N.2    Lory, S.3
  • 13
    • 2442589577 scopus 로고    scopus 로고
    • Type IV pilus structure and bacterial pathogenicity
    • Craig L, Pique ME, Tainer JA (2004) Type IV pilus structure and bacterial pathogenicity. Nat Rev Microbiol 2(5):363-378.
    • (2004) Nat Rev Microbiol , vol.2 , Issue.5 , pp. 363-378
    • Craig, L.1    Pique, M.E.2    Tainer, J.A.3
  • 14
    • 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(14):9721-9728.
    • (2013) J Biol Chem , vol.288 , Issue.14 , pp. 9721-9728
    • Takhar, H.K.1    Kemp, K.2    Kim, M.3    Howell, P.L.4    Burrows, L.L.5
  • 15
    • 41549119041 scopus 로고    scopus 로고
    • PilB and PilT are ATPases acting antagonistically in type IV pilus function in Myxococcus xanthus
    • Jakovljevic V, Leonardy S, Hoppert M, Søgaard-Andersen L (2008) PilB and PilT are ATPases acting antagonistically in type IV pilus function in Myxococcus xanthus. J Bacteriol 190(7):2411-2421.
    • (2008) J Bacteriol , vol.190 , Issue.7 , pp. 2411-2421
    • Jakovljevic, V.1    Leonardy, S.2    Hoppert, M.3    Søgaard-Andersen, L.4
  • 16
    • 33847668562 scopus 로고    scopus 로고
    • Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility
    • Satyshur KA, et al. (2007) Crystal structures of the pilus retraction motor PilT suggest large domain movements and subunit cooperation drive motility. Structure 15(3): 363-376.
    • (2007) Structure , vol.15 , Issue.3 , pp. 363-376
    • Satyshur, K.A.1
  • 17
    • 84871925500 scopus 로고    scopus 로고
    • PilT2 enhances the speed of gonococcal type IV pilus retraction and of twitching motility
    • Kurre R, Höne A, Clausen M, Meel C, Maier B (2012) PilT2 enhances the speed of gonococcal type IV pilus retraction and of twitching motility. Mol Microbiol 86(4): 857-865.
    • (2012) Mol Microbiol , vol.86 , Issue.4 , pp. 857-865
    • Kurre, R.1    Höne, A.2    Clausen, M.3    Meel, C.4    Maier, B.5
  • 18
    • 83355177983 scopus 로고    scopus 로고
    • Characterization of the PilN, PilO and PilP type IVa pilus subcomplex
    • Tammam S, et al. (2011) Characterization of the PilN, PilO and PilP type IVa pilus subcomplex. Mol Microbiol 82(6):1496-1514.
    • (2011) Mol Microbiol , vol.82 , Issue.6 , pp. 1496-1514
    • Tammam, S.1
  • 19
    • 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 Mi crobiol 84(5):857-873.
    • (2012) Mol Mi Crobiol , vol.84 , Issue.5 , pp. 857-873
    • Georgiadou, M.1    Castagnini, M.2    Karimova, G.3    Ladant, D.4    Pelicic, V.5
  • 20
    • 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, et al. (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(1):128-142.
    • (2009) J Mol Biol , vol.394 , Issue.1 , pp. 128-142
    • Ayers, M.1
  • 21
    • 0034973703 scopus 로고    scopus 로고
    • Analysis of the PilQ se cretin from Neisseria meningitidis by transmission electron microscopy reveals a do-decameric quaternary structure
    • Collins RF, Davidsen L, Derrick JP, Ford RC, Tønjum T (2001) Analysis of the PilQ se cretin from Neisseria meningitidis by transmission electron microscopy reveals a do-decameric quaternary structure. J Bacteriol 183(13):3825-3832.
    • (2001) J Bacteriol , vol.183 , Issue.13 , pp. 3825-3832
    • Collins, R.F.1    Davidsen, L.2    Derrick, J.P.3    Ford, R.C.4    Tønjum, T.5
  • 22
    • 4544346057 scopus 로고    scopus 로고
    • Structure of the Neisseria meningitidis outer membrane PilQ secretin complex at 12 a resolution
    • Collins RF, et al. (2004) Structure of the Neisseria meningitidis outer membrane PilQ secretin complex at 12 A resolution. J Biol Chem 279(38):39750-39756.
    • (2004) J Biol Chem , vol.279 , Issue.38 , pp. 39750-39756
    • Collins, R.F.1
  • 23
    • 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 (1994) 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(1): 112-118.
    • (1994) Mol Gen Genet , vol.243 , Issue.1 , pp. 112-118
    • Genin, S.1    Boucher, C.A.2
  • 24
    • 79961171407 scopus 로고    scopus 로고
    • Secretins: Dynamic channels for protein transport across membranes
    • Korotkov KV, Gonen T, Hol WG (2011) Secretins: Dynamic channels for protein transport across membranes. Trends Biochem Sci 36(8):433-443.
    • (2011) Trends Biochem Sci , vol.36 , Issue.8 , pp. 433-443
    • Korotkov, K.V.1    Gonen, T.2    Hol, W.G.3
  • 25
    • 84866903914 scopus 로고    scopus 로고
    • Structure and assembly of a trans-periplasmic channel for type IV pili in Neisseria meningitidis
    • Berry JL, et al. (2012) Structure and assembly of a trans-periplasmic channel for type IV pili in Neisseria meningitidis. PLoS Pathog 8(9):e1002923.
    • (2012) PLoS Pathog , vol.8 , Issue.9
    • Berry, J.L.1
  • 26
    • 84888318245 scopus 로고    scopus 로고
    • Structure and assembly of an inner membrane platform for initiation of type IV pilus biogenesis
    • Karuppiah V, Collins RF, Thistlethwaite A, Gao Y, Derrick JP (2013) Structure and assembly of an inner membrane platform for initiation of type IV pilus biogenesis. Proc Natl Acad Sci USA 110(48):E4638-E4647.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.48
    • Karuppiah, V.1    Collins, R.F.2    Thistlethwaite, A.3    Gao, Y.4    Derrick, J.P.5
  • 27
    • 27844581702 scopus 로고    scopus 로고
    • Structural insights into the secretin PulD and its trypsin-resistant core
    • Chami M, et al. (2005) Structural insights into the secretin PulD and its trypsin-resistant core. J Biol Chem 280(45):37732-37741.
    • (2005) J Biol Chem , vol.280 , Issue.45 , pp. 37732-37741
    • Chami, M.1
  • 28
    • 77957813869 scopus 로고    scopus 로고
    • Structure of the cholera toxin secretion channel in its closed state
    • Reichow SL, Korotkov KV, Hol WG, Gonen T (2010) Structure of the cholera toxin secretion channel in its closed state. Nat Struct Mol Biol 17(10):1226-1232.
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.10 , pp. 1226-1232
    • Reichow, S.L.1    Korotkov, K.V.2    Hol, W.G.3    Gonen, T.4
  • 29
    • 79952262440 scopus 로고    scopus 로고
    • Three-dimensional model of Salmonella's needle complex at subnanometer resolution
    • Schraidt O, Marlovits TC (2011) Three-dimensional model of Salmonella's needle complex at subnanometer resolution. Science 331 (6021):1192-1195.
    • (2011) Science , vol.331 , Issue.6021 , pp. 1192-1195
    • Schraidt, O.1    Marlovits, T.C.2
  • 30
    • 0037225318 scopus 로고    scopus 로고
    • Structure of the filamentous phage pIV multimer by cryo-electron microscopy
    • Opalka N, et al. (2003) Structure of the filamentous phage pIV multimer by cryo-electron microscopy. J Mol Biol 325(3):461-470.
    • (2003) J Mol Biol , vol.325 , Issue.3 , pp. 461-470
    • Opalka, N.1
  • 31
    • 59649092183 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nano-body
    • Korotkov KV, Pardon E, Steyaert J, Hol WG (2009) Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nano-body. Structure 17(2):255-265.
    • (2009) Structure , vol.17 , Issue.2 , pp. 255-265
    • Korotkov, K.V.1    Pardon, E.2    Steyaert, J.3    Hol, W.G.4
  • 32
    • 66149092022 scopus 로고    scopus 로고
    • A conserved structural motif mediates formation of the peri-plasmic rings in the type III secretion system
    • Spreter T, et al. (2009) A conserved structural motif mediates formation of the peri-plasmic rings in the type III secretion system. Nat Struct Mol Biol 16(5):468-476.
    • (2009) Nat Struct Mol Biol , vol.16 , Issue.5 , pp. 468-476
    • Spreter, T.1
  • 33
    • 84860904270 scopus 로고    scopus 로고
    • Structural and functional insights into the pilotin-secretin complex of the type II secretion system
    • Gu S, Rehman S, Wang X, Shevchik VE, Pickersgill RW (2012) Structural and functional insights into the pilotin-secretin complex of the type II secretion system. PLoS Pathog 8(2):e1002531.
    • (2012) PLoS Pathog , vol.8 , Issue.2
    • Gu, S.1    Rehman, S.2    Wang, X.3    Shevchik, V.E.4    Pickersgill, R.W.5
  • 34
    • 83355177984 scopus 로고    scopus 로고
    • Pilotin-secretin recognition in the type II secretion system of Klebsiella oxytoca
    • Tosi T, et al. (2011) Pilotin-secretin recognition in the type II secretion system of Klebsiella oxytoca. Mol Microbiol 82(6):1422-1432.
    • (2011) Mol Microbiol , vol.82 , Issue.6 , pp. 1422-1432
    • Tosi, T.1
  • 35
    • 84876697630 scopus 로고    scopus 로고
    • Crystal structure of the pilotin from the enter-ohemorrhagic Escherichia coli type II secretion system
    • Korotkov KV, Hol WG (2013) Crystal structure of the pilotin from the enter-ohemorrhagic Escherichia coli type II secretion system. J Struct Biol 182(2): 186-191.
    • (2013) J Struct Biol , vol.182 , Issue.2 , pp. 186-191
    • Korotkov, K.V.1    Hol, W.G.2
  • 36
    • 55749114256 scopus 로고    scopus 로고
    • PilF is an outer membrane lipoprotein required for multi-merization and localization of the Pseudomonas aeruginosa Type IV pilus secretin
    • Koo J, et al. (2008) PilF is an outer membrane lipoprotein required for multi-merization and localization of the Pseudomonas aeruginosa Type IV pilus secretin. J Bacteriol 190(21):6961-6969.
    • (2008) J Bacteriol , vol.190 , Issue.21 , pp. 6961-6969
    • Koo, J.1
  • 37
    • 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 (2006) 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 (6):1510-1522.
    • (2006) Mol Microbiol , vol.61 , Issue.6 , pp. 1510-1522
    • Carbonnelle, E.1    Helaine, S.2    Nassif, X.3    Pelicic, V.4
  • 38
    • 53049084326 scopus 로고    scopus 로고
    • Structural characterization of the type-III pi lot-secret in complex from Shigella flexneri
    • Okon M, et al. (2008) Structural characterization of the type-III pi lot-secret in complex from Shigella flexneri. Structure 16(10):1544-1554.
    • (2008) Structure , vol.16 , Issue.10 , pp. 1544-1554
    • Okon, M.1
  • 39
    • 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, et al. (2013) PilMNOPQ from the Pseudomonas aeruginosa type IV pilus system form a transenvelope protein interaction network that interacts with PilA. J Bacteriol 195(10):2126-2135.
    • (2013) J Bacteriol , vol.195 , Issue.10 , pp. 2126-2135
    • Tammam, S.1
  • 40
    • 84890921046 scopus 로고    scopus 로고
    • Outside-In Assembly Pathway of the Type IV Pilus System in Myxococcus xanthus
    • Friedrich C, Bulyha I, Søgaard-Andersen L (2014) Outside-In Assembly Pathway of the Type IV Pilus System in Myxococcus xanthus. J Bacteriol 196(2):378-390.
    • (2014) J Bacteriol , vol.196 , Issue.2 , pp. 378-390
    • Friedrich, C.1    Bulyha, I.2    Søgaard-Andersen, L.3
  • 41
    • 78650165803 scopus 로고    scopus 로고
    • Assembly of the type II secretion system: Identification of Exe a residues critical for peptidoglycan binding and secretin multi-merization
    • Li G, Miller A, Bull H, Howard SP (2011) Assembly of the type II secretion system: Identification of Exe A residues critical for peptidoglycan binding and secretin multi-merization. J Bacteriol 193(1):197-204.
    • (2011) J Bacteriol , vol.193 , Issue.1 , pp. 197-204
    • Li, G.1    Miller, A.2    Bull, H.3    Howard, S.P.4
  • 42
    • 78650900316 scopus 로고    scopus 로고
    • The peptidoglycan-binding protein FimV promotes assembly of the Pseudomonas aeruginosa type IV pilus secretin
    • Wehbi H, et al. (2011)The peptidoglycan-binding protein FimV promotes assembly of the Pseudomonas aeruginosa type IV pilus secretin. J Bacteriol 193(2):540-550.
    • (2011) J Bacteriol , vol.193 , Issue.2 , pp. 540-550
    • Wehbi, H.1
  • 43
    • 79551629041 scopus 로고    scopus 로고
    • Structural characterization of outer membrane components of the type IV pili system in pathogenic Neisseria
    • Jain S, et al. (2011) Structural characterization of outer membrane components of the type IV pili system in pathogenic Neisseria. PLoS ONE 6(1):e16624.
    • (2011) PLoS ONE , vol.6 , Issue.1
    • Jain, S.1
  • 44
    • 33846018001 scopus 로고    scopus 로고
    • Topology of the outer-membrane secretin PilQ from Neisseria meningitidis
    • Frye SA, et al. (2006) Topology of the outer-membrane secretin PilQ from Neisseria meningitidis. Microbiology 152(Pt 12):3751-3764.
    • (2006) Microbiology , vol.152 , Issue.PART 12 , pp. 3751-3764
    • Frye, S.A.1
  • 45
    • 34547628213 scopus 로고    scopus 로고
    • Interactions between the lipoprotein PilP and the se cretin PilQ in Neisseria meningitidis
    • Balasingham SV, et al. (2007) Interactions between the lipoprotein PilP and the se cretin PilQ in Neisseria meningitidis. J Bacteriol 189(15):5716-5727.
    • (2007) J Bacteriol , vol.189 , Issue.15 , pp. 5716-5727
    • Balasingham, S.V.1
  • 46
    • 77957735797 scopus 로고    scopus 로고
    • Proteome analysis of Neisseria meningitidis serogroup strains C associated with outbreaks in China
    • Hu Y, et al. (2010) Proteome analysis of Neisseria meningitidis serogroup strains C associated with outbreaks in China. Biomed Environ Sci 23(4):251-258.
    • (2010) Biomed Environ Sci , vol.23 , Issue.4 , pp. 251-258
    • Hu, Y.1
  • 47
    • 42549103340 scopus 로고    scopus 로고
    • Lys M, a widely distributed protein motif for binding to (peptido)glycans
    • Buist G, Steen A, Kok J, Kuipers OP (2008) Lys M, a widely distributed protein motif for binding to (peptido)glycans. Mol Microbiol 68(4):838-847.
    • (2008) Mol Microbiol , vol.68 , Issue.4 , pp. 838-847
    • Buist, G.1    Steen, A.2    Kok, J.3    Kuipers, O.P.4
  • 48
    • 0034674162 scopus 로고    scopus 로고
    • The structure of a LysM domain from E. Coli membrane-bound lytic murein transglycosylase D (MltD)
    • Bateman A, Bycroft M (2000) The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD). J Mol Biol 299(4):1113-1119.
    • (2000) J Mol Biol , vol.299 , Issue.4 , pp. 1113-1119
    • Bateman, A.1    Bycroft, M.2
  • 49
    • 0034903167 scopus 로고    scopus 로고
    • Insertion-duplication mutagenesis of neisseria: Use in characterization of DNA transfer genes in the gonococcal genetic island
    • Hamilton HL, Schwartz KJ, Dillard JP (2001) Insertion-duplication mutagenesis of neisseria: Use in characterization of DNA transfer genes in the gonococcal genetic island. J Bacteriol183(16):4718-4726.
    • (2001) J Bacteriol , vol.183 , Issue.16 , pp. 4718-4726
    • Hamilton, H.L.1    Schwartz, K.J.2    Dillard, J.P.3
  • 51
    • 3242663192 scopus 로고    scopus 로고
    • Unique modifications with phosphocholine and phosphoe-thanolamine define alternate antigenic forms of Neisseria gonorrhoeae type IV pili
    • Hegge FT, et al. (2004) Unique modifications with phosphocholine and phosphoe-thanolamine define alternate antigenic forms of Neisseria gonorrhoeae type IV pili. Proc Natl Acad Sci USA 101(29):10798-10803.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.29 , pp. 10798-10803
    • Hegge, F.T.1
  • 52
    • 0029837129 scopus 로고    scopus 로고
    • SecA is an intrinsic subunit of the Escherichia coli pre-protein translocase and exposes its carboxyl terminus to the periplasm
    • van der Does C, et al. (1996) SecA is an intrinsic subunit of the Escherichia coli pre-protein translocase and exposes its carboxyl terminus to the periplasm. Mol Microbiol 22(4):619-629.
    • (1996) Mol Microbiol , vol.22 , Issue.4 , pp. 619-629
    • Van Der Does, C.1
  • 53
    • 35748934247 scopus 로고    scopus 로고
    • Genetic manipulation of Neisseria gonorrhoeae
    • Chapter 4:Unit4A2. (Wiley, Hoboken, NJ)
    • Dillard JP (2011) Genetic manipulation of Neisseria gonorrhoeae. Curr Protoc Micro biol Chapter 4:Unit4A2. (Wiley, Hoboken, NJ), pp 1-24.
    • (2011) Curr Protoc Micro Biol , pp. 1-24
    • Dillard, J.P.1
  • 54
    • 55549110786 scopus 로고    scopus 로고
    • Two centuries of meningococcal infection: From Vieusseux to the cellular and molecular basis of disease
    • de Souza AL, Seguro AC (2008) Two centuries of meningococcal infection: From Vieusseux to the cellular and molecular basis of disease. J Med Microbiol 57(Pt 11): 1313-1321.
    • (2008) J Med Microbiol , vol.57 , Issue.PART 11 , pp. 1313-1321
    • De Souza, A.L.1    Seguro, A.C.2
  • 55
    • 84892985277 scopus 로고    scopus 로고
    • Bacterial social networks: Structure and composition of Myxococcus xanthus outer membrane vesicle chains
    • Remis JP, et al. (2014) Bacterial social networks: Structure and composition of Myxococcus xanthus outer membrane vesicle chains. Environ Microbiol 16(2):598-610.
    • (2014) Environ Microbiol , vol.16 , Issue.2 , pp. 598-610
    • Remis, J.P.1
  • 56
    • 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 (2000) Components and dynamics of fiber formation define a ubiquitous biogenesis pathway for bacterial pili. EMBOJ 19(23):6408-6418.
    • (2000) EMBOJ , vol.19 , Issue.23 , pp. 6408-6418
    • Wolfgang, M.1    Van Putten, J.P.2    Hayes, S.F.3    Dorward, D.4    Koomey, M.5
  • 57
    • 78751562995 scopus 로고    scopus 로고
    • Comparative genomic analysis of fruiting body formation in Myxococcales
    • Huntley S, et al. (2011) Comparative genomic analysis of fruiting body formation in Myxococcales. Mol Biol Evol 28(2):1083-1097.
    • (2011) Mol Biol Evol , vol.28 , Issue.2 , pp. 1083-1097
    • Huntley, S.1
  • 58
    • 83355167153 scopus 로고    scopus 로고
    • From individual cell motility to col lective behaviors: Insights from a prokaryote, Myxococcus xanthus
    • Zhang Y, Ducret A, Shaevitz J, Mignot T (2012) From individual cell motility to col lective behaviors: Insights from a prokaryote, Myxococcus xanthus. FEMS Microbiol Rev 36(1): 149-164.
    • (2012) FEMS Microbiol Rev , vol.36 , Issue.1 , pp. 149-164
    • Zhang, Y.1    Ducret, A.2    Shaevitz, J.3    Mignot, T.4
  • 59
    • 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 USA 76(11):5952-5956.
    • (1979) Proc Natl Acad Sci USA , vol.76 , Issue.11 , pp. 5952-5956
    • Kaiser, D.1
  • 60
    • 70350381780 scopus 로고    scopus 로고
    • Regulation of the type IV pili molecular machine by dynamic localization of two motor proteins
    • Bulyha I, et al. (2009) Regulation of the type IV pili molecular machine by dynamic localization of two motor proteins. Mol Microbiol 74(3):691-706.
    • (2009) Mol Microbiol , vol.74 , Issue.3 , pp. 691-706
    • Bulyha, I.1
  • 61
    • 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(1):16-29.
    • (2006) Mol Microbiol , vol.60 , Issue.1 , pp. 16-29
    • Nudleman, E.1    Wall, D.2    Kaiser, D.3
  • 62
    • 0034091536 scopus 로고    scopus 로고
    • Identification of a novel gene, fim V, involved in twitching motility in Pseudomonas aeruginosa
    • Semmler AB, Whitchurch CB, Leech AJ, Mattick JS (2000) Identification of a novel gene, fim V, involved in twitching motility in Pseudomonas aeruginosa. Microbiology 146(Pt6):1321-1332.
    • (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
  • 63
    • 0020027187 scopus 로고
    • Immunological basis of serum resistance of Neisseria gonorrhoeae
    • Schneider H, Griffiss JM, Williams GD, Pier GB (1982) Immunological basis of serum resistance of Neisseria gonorrhoeae. J Gen Microbiol 128(1):13-22.
    • (1982) J Gen Microbiol , vol.128 , Issue.1 , pp. 13-22
    • Schneider, H.1    Griffiss, J.M.2    Williams, G.D.3    Pier, G.B.4
  • 64
    • 0031724486 scopus 로고    scopus 로고
    • The Myxococcus xanthus lipopolysaccharideO-antigen is required for social motility and multicellular development
    • Bowden MG, Kaplan HB (1998) The Myxococcus xanthus lipopolysaccharideO- antigen is required for social motility and multicellular development. Mol Microbiol 30(2): 275-284.
    • (1998) Mol Microbiol , vol.30 , Issue.2 , pp. 275-284
    • Bowden, M.G.1    Kaplan, H.B.2
  • 65
    • 84885389572 scopus 로고    scopus 로고
    • The crystal structure of the cell division amidase AmiC reveals the fold of the AMIN domain, a new peptidoglycan binding domain
    • Rocaboy M, etal. (2013) The crystal structure of the cell division amidase AmiC reveals the fold of the AMIN domain, a new peptidoglycan binding domain. Mol Microbiol 90(2):267-277.
    • (2013) Mol Microbiol , vol.90 , Issue.2 , pp. 267-277
    • Rocaboy, M.1
  • 66
    • 0023158157 scopus 로고
    • Genetic analysis of variant pilin genes from Neisseria gonorrhoeae P9 cloned in Escherichia coli: Physical and immu nological properties of encoded pilins
    • Nicolson IJ, Perry AC, Heckels JE, Saunders JR (1987) Genetic analysis of variant pilin genes from Neisseria gonorrhoeae P9 cloned in Escherichia coli: Physical and immu nological properties of encoded pilins. J Gen Microbiol 133(3):553-561.
    • (1987) J Gen Microbiol , vol.133 , Issue.3 , pp. 553-561
    • Nicolson, I.J.1    Perry, A.C.2    Heckels, J.E.3    Saunders, J.R.4
  • 67
    • 0018074492 scopus 로고
    • Outer membranes of gram-negative bacteria. XIX. Isolation from Pseudomonas aeruginosa PAO1 and use in reconstitution and defini tion of the permeability barrier
    • Hancock RE, Nikaido H (1978) Outer membranes of gram-negative bacteria. XIX. Isolation from Pseudomonas aeruginosa PAO1 and use in reconstitution and defini tion of the permeability barrier. J Bacteriol 136(1):381-390.
    • (1978) J Bacteriol , vol.136 , Issue.1 , pp. 381-390
    • Hancock, R.E.1    Nikaido, H.2
  • 68
    • 84855768808 scopus 로고    scopus 로고
    • Specificity of motor components in the dual flagellar system of Shewanella putrefaciens CN-32
    • Bubendorfer S, et al. (2012) Specificity of motor components in the dual flagellar system of Shewanella putrefaciens CN-32. Mol Microbiol 83(2):335-350.
    • (2012) Mol Microbiol , vol.83 , Issue.2 , pp. 335-350
    • Bubendorfer, S.1
  • 69
    • 77957351822 scopus 로고    scopus 로고
    • Profiling the outer membrane proteome during growth and development of the social bacterium Myxococcus xanthus by selective biotinylation and analyses of outer membrane vesicles
    • Kahnt J, et al. (2010) Profiling the outer membrane proteome during growth and development of the social bacterium Myxococcus xanthus by selective biotinylation and analyses of outer membrane vesicles. J Proteome Res 9(10):5197-5208.
    • (2010) J Proteome Res , vol.9 , Issue.10 , pp. 5197-5208
    • Kahnt, J.1
  • 70
    • 35648967684 scopus 로고    scopus 로고
    • Coupling of protein localization and cell movements by a dynamically localized response reg ulator 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 reg ulator in Myxococcus xanthus. EMBOJ 26(21):4433-4444.
    • (2007) EMBOJ , vol.26 , Issue.21 , pp. 4433-4444
    • Leonardy, S.1    Freymark, G.2    Hebener, S.3    Ellehauge, E.4    Søgaard-Andersen, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.