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Volumn 367, Issue 1592, 2012, Pages 1073-1087

Assembly and mechanisms of bacterial type IV secretion machines

Author keywords

Bacterial conjugation; Bacterial type IV secretion; Core complex; Effector protein; Horizontal gene transfer; Pilus

Indexed keywords

ANTIBIOTIC RESISTANCE; BIOFILM; GENE EXPRESSION; HETEROGENEITY; MICROBIAL COMMUNITY; MOLECULAR ANALYSIS; PROKARYOTE; PROTEIN; SECRETION;

EID: 84858223937     PISSN: 09628436     EISSN: 14712970     Source Type: Journal    
DOI: 10.1098/rstb.2011.0207     Document Type: Review
Times cited : (138)

References (121)
  • 1
    • 77949570007 scopus 로고    scopus 로고
    • New insights into an old story: Agrobacterium-induced tumour formation in plants by plant transformation
    • doi:10.1038/emboj.2010.8)
    • Pitzschke, A. & Hirt, H. 2010 New insights into an old story: Agrobacterium-induced tumour formation in plants by plant transformation. EMBO J. 29, 1021-1032. (doi:10.1038/emboj.2010.8)
    • (2010) EMBO J , vol.29 , pp. 1021-1032
    • Pitzschke, A.1    Hirt, H.2
  • 2
    • 33645865541 scopus 로고    scopus 로고
    • Type IV secretion systems and their effectors in bacterial pathogenesis
    • doi:10.1016/j.mib. 2006.02.008)
    • Backert, S. & Meyer, T. F. 2006 Type IV secretion systems and their effectors in bacterial pathogenesis. Curr. Opin. Microbiol. 9, 207-217. (doi:10.1016/j.mib. 2006.02.008)
    • (2006) Curr. Opin. Microbiol , vol.9 , pp. 207-217
    • Backert, S.1    Meyer, T.F.2
  • 3
    • 81555197168 scopus 로고    scopus 로고
    • The ins and outs of pertussis toxin
    • doi:10.1111/j.1742-4658.2011.08237.x)
    • Locht, C., Coutte, L. & Mielcarek, N. 2011 The ins and outs of pertussis toxin. FEBS J. 278, 4668-4682. (doi:10.1111/j.1742-4658.2011.08237.x)
    • (2011) FEBS J , vol.278 , pp. 4668-4682
    • Locht, C.1    Coutte, L.2    Mielcarek, N.3
  • 4
    • 33645065353 scopus 로고    scopus 로고
    • Natural transformation of Neisseria gonorrhoeae: From DNA donation to homologous recombination
    • doi:10.1111/j.1365-2958.2005.04964.x)
    • Hamilton, H. L. & Dillard, J. P. 2006 Natural transformation of Neisseria gonorrhoeae: from DNA donation to homologous recombination. Mol. Microbiol. 59, 376-385. (doi:10.1111/j.1365-2958.2005.04964.x)
    • (2006) Mol. Microbiol , vol.59 , pp. 376-385
    • Hamilton, H.L.1    Dillard, J.P.2
  • 5
    • 35748943171 scopus 로고    scopus 로고
    • A novel relaxase homologue is involved in chromosomal DNA processing for type IV secretion in Neisseria gonorrhoeae
    • doi:10.1111/j.1365-2958.2007.05966.x)
    • Salgado-Pabon, W., Jain, S., Turner, N., Van Der Does, C. & Dillard, J. P. 2007 A novel relaxase homologue is involved in chromosomal DNA processing for type IV secretion in Neisseria gonorrhoeae. Mol. Microbiol. 66, 930-947. (doi:10.1111/j.1365-2958.2007.05966.x)
    • (2007) Mol. Microbiol , vol.66 , pp. 930-947
    • Salgado-Pabon, W.1    Jain, S.2    Turner, N.3    van der Does, C.4    Dillard, J.P.5
  • 6
    • 0036532408 scopus 로고    scopus 로고
    • Natural transformation in Helicobacter pylori: DNA transport in an unexpected way
    • doi:10.1016/S0966-842X(02)02314-4)
    • Smeets, L. C. & Kusters, J. G. 2002 Natural transformation in Helicobacter pylori: DNA transport in an unexpected way. Trends Microbiol. 10, 159-162. (doi:10.1016/S0966-842X(02)02314-4)
    • (2002) Trends Microbiol , vol.10 , pp. 159-162
    • Smeets, L.C.1    Kusters, J.G.2
  • 7
    • 77954761569 scopus 로고    scopus 로고
    • Integrative and conjugative elements: Mosaic mobile genetic elements enabling dynamic lateral gene flow
    • doi:10.1038/nrmicro2382)
    • Wozniak, R. A. & Waldor, M. K. 2010 Integrative and conjugative elements: mosaic mobile genetic elements enabling dynamic lateral gene flow. Nat. Rev. Microbiol. 8, 552-563. (doi:10.1038/nrmicro2382)
    • (2010) Nat. Rev. Microbiol , vol.8 , pp. 552-563
    • Wozniak, R.A.1    Waldor, M.K.2
  • 8
    • 0034255091 scopus 로고    scopus 로고
    • Bacterial type IV secretion: Conjugation systems adapted to deliver effector molecules to host cells
    • doi:10.1016/S0966-842X(00)01792-3)
    • Christie, P. J. & Vogel, J. P. 2000 Bacterial type IV secretion: conjugation systems adapted to deliver effector molecules to host cells. Trends Microbiol. 8, 354-360. (doi:10.1016/S0966-842X(00)01792-3)
    • (2000) Trends Microbiol , vol.8 , pp. 354-360
    • Christie, P.J.1    Vogel, J.P.2
  • 9
    • 2442682800 scopus 로고    scopus 로고
    • Definition of a bacterial type IV secretion pathway for a DNA substrate
    • doi:10.1126/science. 1095211)
    • Cascales, E. & Christie, P. J. 2004 Definition of a bacterial type IV secretion pathway for a DNA substrate. Science 304, 1170-1173. (doi:10.1126/science. 1095211)
    • (2004) Science , vol.304 , pp. 1170-1173
    • Cascales, E.1    Christie, P.J.2
  • 10
    • 78049370513 scopus 로고    scopus 로고
    • Modulation of host cell function by Legionella pneumophila type IV effectors
    • doi:10.1146/ annurev-cellbio-100109-104034)
    • Hubber, A. & Roy, C. R. 2010 Modulation of host cell function by Legionella pneumophila type IV effectors. Annu. Rev. Cell Dev. Biol. 26, 261-283. (doi:10.1146/ annurev-cellbio-100109-104034)
    • (2010) Annu. Rev. Cell Dev. Biol , vol.26 , pp. 261-283
    • Hubber, A.1    Roy, C.R.2
  • 11
    • 80455151252 scopus 로고    scopus 로고
    • Type IVB secretion systems of Legionella and other Gram-negative bacteria
    • doi:10.3389/fmicb.2011.00136)
    • Nagai, H. & Kubori, T. 2011 Type IVB secretion systems of Legionella and other Gram-negative bacteria. Front. Microbiol. 2, 136. (doi:10.3389/fmicb.2011.00136)
    • (2011) Front. Microbiol , vol.2 , pp. 136
    • Nagai, H.1    Kubori, T.2
  • 12
    • 79953702794 scopus 로고    scopus 로고
    • Role of the cag-pathogenicity island encoded type IV secretion system in Helicobacter pylori pathogenesis
    • doi:10.1111/j.1742-4658.2011. 08035.x)
    • Tegtmeyer, N., Wessler, S. & Backert, S. 2011 Role of the cag-pathogenicity island encoded type IV secretion system in Helicobacter pylori pathogenesis. FEBS J. 278, 1190-1202. (doi:10.1111/j.1742-4658.2011. 08035.x)
    • (2011) FEBS J , vol.278 , pp. 1190-1202
    • Tegtmeyer, N.1    Wessler, S.2    Backert, S.3
  • 13
    • 47549106865 scopus 로고    scopus 로고
    • Infection-associated type IV secretion systems of Bartonella and their diverse roles in host cell interaction
    • doi:10.1111/j.1462-5822.2008.01171.x)
    • Dehio, C. 2008 Infection-associated type IV secretion systems of Bartonella and their diverse roles in host cell interaction. Cell Microbiol. 10, 1591-1598. (doi:10.1111/j.1462-5822.2008.01171.x)
    • (2008) Cell Microbiol , vol.10 , pp. 1591-1598
    • Dehio, C.1
  • 14
    • 21244462648 scopus 로고    scopus 로고
    • Virulence-associated type IV secretion systems of Bartonella
    • doi:10.1016/j.tim.2005.05.008)
    • Schröder, G. & Dehio, C. 2005 Virulence-associated type IV secretion systems of Bartonella. Trends Microbiol. 13, 336-342. (doi:10.1016/j.tim.2005.05.008)
    • (2005) Trends Microbiol , vol.13 , pp. 336-342
    • Schröder, G.1    Dehio, C.2
  • 17
    • 0141454925 scopus 로고    scopus 로고
    • A bacterial conjugation machinery recruited for pathogenesis
    • doi:10. 1046/j.1365-2958.2003.03650.x)
    • Seubert, A., Hiestand, R., De La Cruz, F. & Dehio, C. 2003 A bacterial conjugation machinery recruited for pathogenesis. Mol. Microbiol. 49, 1253-1266. (doi:10. 1046/j.1365-2958.2003.03650.x)
    • (2003) Mol. Microbiol , vol.49 , pp. 1253-1266
    • Seubert, A.1    Hiestand, R.2    de la Cruz, F.3    Dehio, C.4
  • 18
    • 77954687617 scopus 로고    scopus 로고
    • The Trw type IV secretion system of Bartonella mediates host-specific adhesion to erythrocytes
    • doi:10.1371/journal.ppat.1000946)
    • Vayssier-Taussat, M. et al. 2010 The Trw type IV secretion system of Bartonella mediates host-specific adhesion to erythrocytes. PLoS Pathog. 6, e1000946. (doi:10.1371/journal.ppat.1000946)
    • (2010) PLoS Pathog , vol.6
    • Vayssier-Taussat, M.1
  • 19
    • 0027518747 scopus 로고
    • Molecular characterization of an operon required for pertussis toxin secretion
    • doi:10.1073/pnas.90.7.2970)
    • Weiss, A. A., Johnson, F. D. & Burns, D. L. 1993 Molecular characterization of an operon required for pertussis toxin secretion. Proc. Natl Acad. Sci. USA 90, 2970-2974. (doi:10.1073/pnas.90.7.2970)
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 2970-2974
    • Weiss, A.A.1    Johnson, F.D.2    Burns, D.L.3
  • 20
    • 0032871546 scopus 로고    scopus 로고
    • Mutants in the ptlA-H genes of Bordetella pertussis are deficient for pertussis toxin secretion
    • doi:10.1111/j.1574-6968.1999.tb08766.x)
    • Craig-Mylius, K. A. & Weiss, A. A. 1999 Mutants in the ptlA-H genes of Bordetella pertussis are deficient for pertussis toxin secretion. FEMS Microbiol. Lett. 179, 479-484. (doi:10.1111/j.1574-6968.1999.tb08766.x)
    • (1999) FEMS Microbiol. Lett , vol.179 , pp. 479-484
    • Craig-Mylius, K.A.1    Weiss, A.A.2
  • 21
    • 0036178028 scopus 로고    scopus 로고
    • Membrane localization of the S1 subunit of pertussis toxin in Bordetella pertussis and implications for pertussis toxin secretion
    • doi:10.1128/IAI.70.3.1193-1201.2002)
    • Farizo, K. M., Fiddner, S., Cheung, A. M. & Burns, D. L. 2002 Membrane localization of the S1 subunit of pertussis toxin in Bordetella pertussis and implications for pertussis toxin secretion. Infect. Immun. 70, 1193-1201. (doi:10.1128/IAI.70.3.1193-1201.2002)
    • (2002) Infect. Immun , vol.70 , pp. 1193-1201
    • Farizo, K.M.1    Fiddner, S.2    Cheung, A.M.3    Burns, D.L.4
  • 22
    • 77949696055 scopus 로고    scopus 로고
    • Increased expression of the type IV secretion system in piliated Neisseria gonorrhoeae variants
    • doi:10.1128/JB.01357-09)
    • Salgado-Pabon, W., Du, Y., Hackett, K. T., Lyons, K. M., Arvidson, C. G. & Dillard, J. P. 2010 Increased expression of the type IV secretion system in piliated Neisseria gonorrhoeae variants. J. Bacteriol. 192, 1912-1920. (doi:10.1128/JB.01357-09)
    • (2010) J. Bacteriol , vol.192 , pp. 1912-1920
    • Salgado-Pabon, W.1    Du, Y.2    Hackett, K.T.3    Lyons, K.M.4    Arvidson, C.G.5    Dillard, J.P.6
  • 23
    • 0034903021 scopus 로고    scopus 로고
    • Natural transformation competence in Helicobacter pylori is mediated by the basic components of a type IV secretion system
    • doi:10.1046/j.1365-2958.2001.02502.x)
    • Hofreuter, D., Odenbreit, S. & Haas, R. 2001 Natural transformation competence in Helicobacter pylori is mediated by the basic components of a type IV secretion system. Mol. Microbiol. 41, 379-391. (doi:10.1046/j.1365-2958.2001.02502.x)
    • (2001) Mol. Microbiol , vol.41 , pp. 379-391
    • Hofreuter, D.1    Odenbreit, S.2    Haas, R.3
  • 24
    • 31344443610 scopus 로고    scopus 로고
    • Functional and topological characterization of novel components of the comB DNA transformation competence system in Helicobacter pylori
    • doi:10. 1128/JB.188.3.882-893.2006)
    • Karnholz, A., Hoefler, C., Odenbreit, S., Fischer, W., Hofreuter, D. & Haas, R. 2006 Functional and topological characterization of novel components of the comB DNA transformation competence system in Helicobacter pylori. J. Bacteriol. 188, 882-893. (doi:10. 1128/JB.188.3.882-893.2006)
    • (2006) J. Bacteriol , vol.188 , pp. 882-893
    • Karnholz, A.1    Hoefler, C.2    Odenbreit, S.3    Fischer, W.4    Hofreuter, D.5    Haas, R.6
  • 25
    • 75749148434 scopus 로고    scopus 로고
    • Composite system mediates two-step DNA uptake into Helicobacter pylori
    • doi:10.1073/ pnas.0909955107)
    • Stingl, K., Muller, S., Scheidgen-Kleyboldt, G., Clausen, M. & Maier, B. 2010 Composite system mediates two-step DNA uptake into Helicobacter pylori. Proc. Natl Acad. Sci. USA 107, 1184-1189. (doi:10.1073/ pnas.0909955107)
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 1184-1189
    • Stingl, K.1    Muller, S.2    Scheidgen-Kleyboldt, G.3    Clausen, M.4    Maier, B.5
  • 26
    • 58149375801 scopus 로고    scopus 로고
    • Structure of a type IV secretion system core complex
    • doi:10.1126/science.1166101)
    • Fronzes, R., Schafer, E., Wang, L., Saibil, H. R., Orlova, E. V. & Waksman, G. 2009 Structure of a type IV secretion system core complex. Science 323, 266-268. (doi:10.1126/science.1166101)
    • (2009) Science , vol.323 , pp. 266-268
    • Fronzes, R.1    Schafer, E.2    Wang, L.3    Saibil, H.R.4    Orlova, E.V.5    Waksman, G.6
  • 27
    • 77649247997 scopus 로고    scopus 로고
    • Agrobacterium type IV secretion system and its substrates form helical arrays around the circumference of virulence-induced cells
    • doi:10.1073/pnas.0914940107)
    • Aguilar, J., Zupan, J., Cameron, T. A. & Zambryski, P. C. 2010 Agrobacterium type IV secretion system and its substrates form helical arrays around the circumference of virulence-induced cells. Proc. Natl Acad. Sci. USA 107, 3758-3763. (doi:10.1073/pnas.0914940107)
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 3758-3763
    • Aguilar, J.1    Zupan, J.2    Cameron, T.A.3    Zambryski, P.C.4
  • 28
    • 22544443955 scopus 로고    scopus 로고
    • Identification of the VirB4-VirB8-VirB5-VirB2 pilus assembly sequence of type IV secretion systems
    • doi:10.1074/jbc. M502347200)
    • Yuan, Q., Carle, A., Gao, C., Sivanesan, D., Aly, K. A., Hoppner, C., Krall, L., Domke, N. & Baron, C. 2005 Identification of the VirB4-VirB8-VirB5-VirB2 pilus assembly sequence of type IV secretion systems. J. Biol. Chem. 280, 26349-26359. (doi:10.1074/jbc. M502347200)
    • (2005) J. Biol. Chem , vol.280 , pp. 26349-26359
    • Yuan, Q.1    Carle, A.2    Gao, C.3    Sivanesan, D.4    Aly, K.A.5    Hoppner, C.6    Krall, L.7    Domke, N.8    Baron, C.9
  • 29
    • 79955527260 scopus 로고    scopus 로고
    • The dimer interface of Agrobacterium tumefaciens VirB8 is important for type IV secretion system function, stability, and association of VirB2 with the core complex
    • doi:10.1128/JB.00907-10)
    • Sivanesan, D. & Baron, C. 2011 The dimer interface of Agrobacterium tumefaciens VirB8 is important for type IV secretion system function, stability, and association of VirB2 with the core complex. J. Bacteriol. 193, 2097-2106. (doi:10.1128/JB.00907-10)
    • (2011) J. Bacteriol , vol.193 , pp. 2097-2106
    • Sivanesan, D.1    Baron, C.2
  • 30
    • 15444380769 scopus 로고    scopus 로고
    • Structures of two core subunits of the bacterial type IV secretion system, VirB8 from Brucella suis and ComB10 from Helicobacter pylori
    • doi:10.1073/pnas.0408927102)
    • Terradot, L., Bayliss, R., Oomen, C., Leonard, G. A., Baron, C. & Waksman, G. 2005 Structures of two core subunits of the bacterial type IV secretion system, VirB8 from Brucella suis and ComB10 from Helicobacter pylori. Proc. Natl Acad. Sci. USA 102, 4596-4601. (doi:10.1073/pnas.0408927102)
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 4596-4601
    • Terradot, L.1    Bayliss, R.2    Oomen, C.3    Leonard, G.A.4    Baron, C.5    Waksman, G.6
  • 31
    • 72949109740 scopus 로고    scopus 로고
    • Structure of the outer membrane complex of a type IV secretion system
    • doi:10.1038/nature08588)
    • Chandran, V., Fronzes, R., Duquerroy, S., Cronin, N., Navaza, J. & Waksman, G. 2009 Structure of the outer membrane complex of a type IV secretion system. Nature 462, 1011-1015. (doi:10.1038/nature08588)
    • (2009) Nature , vol.462 , pp. 1011-1015
    • Chandran, V.1    Fronzes, R.2    Duquerroy, S.3    Cronin, N.4    Navaza, J.5    Waksman, G.6
  • 32
    • 58449091300 scopus 로고    scopus 로고
    • Agrobacterium VirB10 domain requirements for type IV secretion and T pilus biogenesis
    • doi:10.1111/j.1365- 2958.2008.06565.x)
    • Jakubowski, S. J., Kerr, J. E., Garza, I., Krishnamoorthy, V., Bayliss, R., Waksman, G. & Christie, P. J. 2009 Agrobacterium VirB10 domain requirements for type IV secretion and T pilus biogenesis. Mol. Microbiol. 71, 779-794. (doi:10.1111/j.1365- 2958.2008.06565.x)
    • (2009) Mol. Microbiol , vol.71 , pp. 779-794
    • Jakubowski, S.J.1    Kerr, J.E.2    Garza, I.3    Krishnamoorthy, V.4    Bayliss, R.5    Waksman, G.6    Christie, P.J.7
  • 34
    • 27744478719 scopus 로고    scopus 로고
    • Functional interactions between type IV secretion systems involved in DNA transfer and virulence
    • doi:10.1099/mic.0. 28410-0)
    • De Paz, H. D., Sangari, F. J., Bolland, S., Garcia-Lobo, J. M., Dehio, C., De La Cruz, F. & Llosa, M. 2005 Functional interactions between type IV secretion systems involved in DNA transfer and virulence. Microbiology 151, 3505-3516. (doi:10.1099/mic.0. 28410-0)
    • (2005) Microbiology , vol.151 , pp. 3505-3516
    • de Paz, H.D.1    Sangari, F.J.2    Bolland, S.3    Garcia-Lobo, J.M.4    Dehio, C.5    de la Cruz, F.6    Llosa, M.7
  • 35
    • 0032873607 scopus 로고    scopus 로고
    • TraC of IncN plasmid pKM101 associates with membranes and extracellular high-molecular-weight structures in Escherichia coli
    • Schmidt-Eisenlohr, H., Domke, N. & Baron, C. 1999 TraC of IncN plasmid pKM101 associates with membranes and extracellular high-molecular-weight structures in Escherichia coli. J. Bacteriol. 181, 5563-5571.
    • (1999) J. Bacteriol , vol.181 , pp. 5563-5571
    • Schmidt-Eisenlohr, H.1    Domke, N.2    Baron, C.3
  • 36
    • 0037407708 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens VirB6 protein participates in formation of VirB7 and VirB9 complexes required for type IV secretion
    • doi:10.1128/JB.185.9.2867-2878. 2003)
    • Jakubowski, S. J., Krishnamoorthy, V. & Christie, P. J. 2003 Agrobacterium tumefaciens VirB6 protein participates in formation of VirB7 and VirB9 complexes required for type IV secretion. J. Bacteriol. 185, 2867-2878. (doi:10.1128/JB.185.9.2867-2878. 2003)
    • (2003) J. Bacteriol , vol.185 , pp. 2867-2878
    • Jakubowski, S.J.1    Krishnamoorthy, V.2    Christie, P.J.3
  • 37
    • 0034992789 scopus 로고    scopus 로고
    • VirB7 lipoprotein is exocellular and associates with the Agrobacterium tumefaciens T pilus
    • doi:10.1128/JB. 183.12.3642-3651.2001)
    • Sagulenko, V., Sagulenko, E., Jakubowski, S., Spudich, E. & Christie, P. J. 2001 VirB7 lipoprotein is exocellular and associates with the Agrobacterium tumefaciens T pilus. J. Bacteriol. 183, 3642-3651. (doi:10.1128/JB. 183.12.3642-3651.2001)
    • (2001) J. Bacteriol , vol.183 , pp. 3642-3651
    • Sagulenko, V.1    Sagulenko, E.2    Jakubowski, S.3    Spudich, E.4    Christie, P.J.5
  • 38
    • 77957918692 scopus 로고    scopus 로고
    • Strain-specific genes of Helicobacter pylori: Genome evolution driven by a novel type IV secretion system and genomic island transfer
    • doi:10.1093/nar/gkq378)
    • Fischer, W., Windhager, L., Rohrer, S., Zeiller, M., Karnholz, A., Hoffmann, R., Zimmer, R. & Haas, R. 2010 Strain-specific genes of Helicobacter pylori: genome evolution driven by a novel type IV secretion system and genomic island transfer. Nucleic Acids Res. 38, 6089-6101. (doi:10.1093/nar/gkq378)
    • (2010) Nucleic Acids Res , vol.38 , pp. 6089-6101
    • Fischer, W.1    Windhager, L.2    Rohrer, S.3    Zeiller, M.4    Karnholz, A.5    Hoffmann, R.6    Zimmer, R.7    Haas, R.8
  • 39
    • 79953701623 scopus 로고    scopus 로고
    • Assembly and molecular mode of action of the Helicobacter pylori Cag type IV secretion apparatus
    • doi:10.1111/j. 1742-4658.2011.08036.x)
    • Fischer, W. 2011 Assembly and molecular mode of action of the Helicobacter pylori Cag type IV secretion apparatus. FEBS J. 278, 1203-1212. (doi:10.1111/j. 1742-4658.2011.08036.x)
    • (2011) FEBS J , vol.278 , pp. 1203-1212
    • Fischer, W.1
  • 40
    • 72249106415 scopus 로고    scopus 로고
    • Cag3 is a novel essential component of the Helicobacter pylori Cag type IV secretion system outer membrane subcomplex
    • doi:10.1128/JB. 00946-09)
    • Pinto-Santini, D. M. & Salama, N. R. 2009 Cag3 is a novel essential component of the Helicobacter pylori Cag type IV secretion system outer membrane subcomplex. J. Bacteriol. 191, 7343-7352. (doi:10.1128/JB. 00946-09)
    • (2009) J. Bacteriol , vol.191 , pp. 7343-7352
    • Pinto-Santini, D.M.1    Salama, N.R.2
  • 41
    • 40449098575 scopus 로고    scopus 로고
    • Protein subassemblies of the Helicobacter pylori Cag type IV secretion system revealed by localization and interaction studies
    • doi:10.1128/JB.01341-07)
    • Kutter, S., Buhrdorf, R., Haas, J., Schneider-Brachert, W., Haas, R. & Fischer, W. 2008 Protein subassemblies of the Helicobacter pylori Cag type IV secretion system revealed by localization and interaction studies. J. Bacteriol. 190, 2161-2171. (doi:10.1128/JB.01341-07)
    • (2008) J. Bacteriol , vol.190 , pp. 2161-2171
    • Kutter, S.1    Buhrdorf, R.2    Haas, J.3    Schneider-Brachert, W.4    Haas, R.5    Fischer, W.6
  • 42
    • 0038308165 scopus 로고    scopus 로고
    • F factor conjugation is a true type IV secretion system
    • doi:10.1016/S0378-1097(03)00430-0)
    • Lawley, T. D., Klimke, W. A., Gubbins, M. J. & Frost, L. S. 2003 F factor conjugation is a true type IV secretion system. FEMS Microbiol. Lett. 224, 1-15. (doi:10.1016/S0378-1097(03)00430-0)
    • (2003) FEMS Microbiol. Lett , vol.224 , pp. 1-15
    • Lawley, T.D.1    Klimke, W.A.2    Gubbins, M.J.3    Frost, L.S.4
  • 43
    • 3843054585 scopus 로고    scopus 로고
    • Tra proteins characteristic of F-like type IV secretion systems constitute an interaction group by yeast two-hybrid analysis
    • doi:10.1128/JB.186.16. 5480-5485.2004)
    • Harris, R. L. & Silverman, P. M. 2004 Tra proteins characteristic of F-like type IV secretion systems constitute an interaction group by yeast two-hybrid analysis. J. Bacteriol. 186, 5480-5485. (doi:10.1128/JB.186.16. 5480-5485.2004)
    • (2004) J. Bacteriol , vol.186 , pp. 5480-5485
    • Harris, R.L.1    Silverman, P.M.2
  • 44
    • 0035172604 scopus 로고    scopus 로고
    • Evidence that F-plasmid proteins TraV, TraK and TraB assemble into an envelope-spanning structure in Escherichia coli
    • doi:10.1046/j. 1365-2958.2001.02667.x)
    • Harris, R. L., Hombs, V. & Silverman, P. M. 2001 Evidence that F-plasmid proteins TraV, TraK and TraB assemble into an envelope-spanning structure in Escherichia coli. Mol. Microbiol. 42, 757-766. (doi:10.1046/j. 1365-2958.2001.02667.x)
    • (2001) Mol. Microbiol , vol.42 , pp. 757-766
    • Harris, R.L.1    Hombs, V.2    Silverman, P.M.3
  • 45
    • 77953677151 scopus 로고    scopus 로고
    • New insights into F-pilus structure, dynamics, and function
    • doi:10.1039/b917761b)
    • Silverman, P. M. & Clarke, M. B. 2010 New insights into F-pilus structure, dynamics, and function. Integr. Biol. (Camb.) 2, 25-31. (doi:10.1039/b917761b)
    • (2010) Integr. Biol. (Camb.) , vol.2 , pp. 25-31
    • Silverman, P.M.1    Clarke, M.B.2
  • 46
    • 0024049602 scopus 로고
    • DNA sequence analysis of point mutations in traA, the F pilin gene, reveal two domains involved in F-specific bacteriophage attachment
    • doi:10. 1007/BF00333409)
    • Frost, L. S. & Paranchych, W. 1988 DNA sequence analysis of point mutations in traA, the F pilin gene, reveal two domains involved in F-specific bacteriophage attachment. Mol. Gen. Genet. 213, 134-139. (doi:10. 1007/BF00333409)
    • (1988) Mol. Gen. Genet , vol.213 , pp. 134-139
    • Frost, L.S.1    Paranchych, W.2
  • 47
    • 0343668561 scopus 로고
    • The structure, function, synthesis and genetic control of bacterial pili and a molecular model for DNA and RNA transport in Gramnegative bacteria
    • Brinton Jr., C. C. 1965 The structure, function, synthesis and genetic control of bacterial pili and a molecular model for DNA and RNA transport in Gramnegative bacteria. Trans. NYAcad. Sci. 27, 1003-1054.
    • (1965) Trans. NYAcad. Sci , vol.27 , pp. 1003-1054
    • Brinton, C.C.1
  • 48
    • 0023021741 scopus 로고
    • The conjugation system of F, the fertility factor of Escherichia coli
    • doi:10.1146/ annurev.ge.20.120186.003113)
    • Ippen-Ihler, K. A. & Minkley Jr., E. G. 1986 The conjugation system of F, the fertility factor of Escherichia coli. Annu. Rev. Genet. 20, 593-624. (doi:10.1146/ annurev.ge.20.120186.003113)
    • (1986) Annu. Rev. Genet , vol.20 , pp. 593-624
    • Ippen-Ihler, K.A.1    Minkley, E.G.2
  • 49
    • 0034255183 scopus 로고    scopus 로고
    • The T-pilus of Agrobacterium tumefaciens
    • doi:10.1016/S0966-842X(00)01802-3)
    • Lai, E. M. & Kado, C. I. 2000 The T-pilus of Agrobacterium tumefaciens. Trends Microbiol. 8, 361-369. (doi:10.1016/S0966-842X(00)01802-3)
    • (2000) Trends Microbiol , vol.8 , pp. 361-369
    • Lai, E.M.1    Kado, C.I.2
  • 50
    • 0018420611 scopus 로고
    • X-ray diffraction and electron microscope studies on the structure of bacterial F pili
    • doi:10.1016/0022-2836(79)90423-6)
    • Folkhard, W., Leonard, K. R., Malsey, S., Marvin, D. A., Dubochet, J., Engel, A., Achtman, M. & Helmuth, R. 1979 X-ray diffraction and electron microscope studies on the structure of bacterial F pili. J. Mol. Biol. 130, 145-160. (doi:10.1016/0022-2836(79)90423-6)
    • (1979) J. Mol. Biol , vol.130 , pp. 145-160
    • Folkhard, W.1    Leonard, K.R.2    Malsey, S.3    Marvin, D.A.4    Dubochet, J.5    Engel, A.6    Achtman, M.7    Helmuth, R.8
  • 51
    • 0033529624 scopus 로고    scopus 로고
    • Conjugative pili of IncP plasmids, and the Ti plasmid T pilus are composed of cyclic subunits
    • doi:10.1074/jbc.274.32.22548)
    • Eisenbrandt, R., Kalkum, M., Lai, E. M., Lurz, R., Kado, C. I. & Lanka, E. 1999 Conjugative pili of IncP plasmids, and the Ti plasmid T pilus are composed of cyclic subunits. J. Biol. Chem. 274, 22548-22555. (doi:10.1074/jbc.274.32.22548)
    • (1999) J. Biol. Chem , vol.274 , pp. 22548-22555
    • Eisenbrandt, R.1    Kalkum, M.2    Lai, E.M.3    Lurz, R.4    Kado, C.I.5    Lanka, E.6
  • 52
    • 0036136240 scopus 로고    scopus 로고
    • Biogenesis of T pili in Agrobacterium tumefaciens requires precise VirB2 propilin cleavage and cyclization
    • doi:10. 1128/JB.184.1.327-330.2002)
    • Lai, E. M., Eisenbrandt, R., Kalkum, M., Lanka, E. & Kado, C. I. 2002 Biogenesis of T pili in Agrobacterium tumefaciens requires precise VirB2 propilin cleavage and cyclization. J. Bacteriol. 184, 327-330. (doi:10. 1128/JB.184.1.327-330.2002)
    • (2002) J. Bacteriol , vol.184 , pp. 327-330
    • Lai, E.M.1    Eisenbrandt, R.2    Kalkum, M.3    Lanka, E.4    Kado, C.I.5
  • 53
  • 54
    • 0027167471 scopus 로고
    • H-pilus assembly kinetics determined by electron microscopy
    • Maher, D., Sherburne, R. & Taylor, D. E. 1993 H-pilus assembly kinetics determined by electron microscopy. J. Bacteriol. 175, 2175-2183.
    • (1993) J. Bacteriol , vol.175 , pp. 2175-2183
    • Maher, D.1    Sherburne, R.2    Taylor, D.E.3
  • 55
    • 0032880364 scopus 로고    scopus 로고
    • Comparison of proteins involved in pilus synthesis and mating pair stabilization from the related plasmids F and R100-1: Insights into the mechanism of conjugation
    • Anthony, K.G., Klimke, W.A., Manchak, J. & Frost, L. S. 1999 Comparison of proteins involved in pilus synthesis and mating pair stabilization from the related plasmids F and R100-1: insights into the mechanism of conjugation. J. Bacteriol. 181, 5149-5159.
    • (1999) J. Bacteriol , vol.181 , pp. 5149-5159
    • Anthony, K.G.1    Klimke, W.A.2    Manchak, J.3    Frost, L.S.4
  • 56
    • 77957348046 scopus 로고    scopus 로고
    • Evidence for VirB4- mediated dislocation of membrane-integrated VirB2 pilin during biogenesis of the Agrobacterium VirB/VirD4 type IV secretion system
    • doi:10.1128/JB.00557-10)
    • Kerr, J. E. & Christie, P. J. 2010 Evidence for VirB4- mediated dislocation of membrane-integrated VirB2 pilin during biogenesis of the Agrobacterium VirB/VirD4 type IV secretion system. J. Bacteriol. 192, 4923-4934. (doi:10.1128/JB.00557-10)
    • (2010) J. Bacteriol , vol.192 , pp. 4923-4934
    • Kerr, J.E.1    Christie, P.J.2
  • 57
    • 0018961637 scopus 로고
    • Morphological and serological relationships of conjugative pili
    • doi:10.1016/0147-619X(80)90005-0)
    • Bradley, D. E. 1980 Morphological and serological relationships of conjugative pili. Plasmid 4, 155-169. (doi:10.1016/0147-619X(80)90005-0)
    • (1980) Plasmid , vol.4 , pp. 155-169
    • Bradley, D.E.1
  • 58
    • 0034923461 scopus 로고    scopus 로고
    • Structure of TrwB, a gatekeeper in bacterial conjugation
    • doi:10.1016/S1357-2725(01) 00060-7)
    • Gomis-Rüth, F. X. & Coll, M. 2001 Structure of TrwB, a gatekeeper in bacterial conjugation. Int. J. Biochem. Cell Biol. 33, 839-843. (doi:10.1016/S1357-2725(01) 00060-7)
    • (2001) Int. J. Biochem. Cell Biol , vol.33 , pp. 839-843
    • Gomis-Rüth, F.X.1    Coll, M.2
  • 59
    • 0042838290 scopus 로고    scopus 로고
    • Conjugative coupling proteins interact with cognate and heterologous VirB10-like proteins while exhibiting specificity for cognate relaxosomes
    • doi:10.1073/pnas. 1830264100)
    • Llosa, M., Zunzunegui, S. & De La Cruz, F. 2003 Conjugative coupling proteins interact with cognate and heterologous VirB10-like proteins while exhibiting specificity for cognate relaxosomes. Proc. Natl Acad. Sci USA 100, 10465-10470. (doi:10.1073/pnas. 1830264100)
    • (2003) Proc. Natl Acad. Sci USA , vol.100 , pp. 10465-10470
    • Llosa, M.1    Zunzunegui, S.2    de la Cruz, F.3
  • 60
    • 0038385173 scopus 로고    scopus 로고
    • Interaction between the IncHI1 plasmid R27 coupling protein and type IV secretion system: TraG associates with the coiled-coil mating pair formation protein TrhB
    • doi:10.1046/j.1365-2958.2003.03551.x)
    • Gilmour, M. W., Gunton, J. E., Lawley, T. D. & Taylor, D. E. 2003 Interaction between the IncHI1 plasmid R27 coupling protein and type IV secretion system: TraG associates with the coiled-coil mating pair formation protein TrhB. Mol. Microbiol. 49, 105-116. (doi:10.1046/j.1365-2958.2003.03551.x)
    • (2003) Mol. Microbiol , vol.49 , pp. 105-116
    • Gilmour, M.W.1    Gunton, J.E.2    Lawley, T.D.3    Taylor, D.E.4
  • 61
    • 0036047412 scopus 로고    scopus 로고
    • Bacterial conjugation: A two-step mechanism for DNA transport
    • doi:10. 1046/j.1365-2958.2002.03014.x)
    • Llosa, M., Gomis-Rüth, F. X., Coll, M. & De La Cruz, F. 2002 Bacterial conjugation: a two-step mechanism for DNA transport. Mol. Microbiol. 45, 1-8. (doi:10. 1046/j.1365-2958.2002.03014.x)
    • (2002) Mol. Microbiol , vol.45 , pp. 1-8
    • Llosa, M.1    Gomis-Rüth, F.X.2    Coll, M.3    de la Cruz, F.4
  • 62
    • 0027205506 scopus 로고
    • Computer-assisted dissection of rolling circle DNA replication
    • doi:10.1016/0303-2647(93)90074-M)
    • Koonin, E. V. & Ilyina, T. V. 1993 Computer-assisted dissection of rolling circle DNA replication. Biosystems 30, 241-268. (doi:10.1016/0303-2647(93)90074-M)
    • (1993) Biosystems , vol.30 , pp. 241-268
    • Koonin, E.V.1    Ilyina, T.V.2
  • 63
    • 33846413933 scopus 로고    scopus 로고
    • The structure of the minimal relaxase domain of MobA at 2.1 A°resolution
    • doi:10.1016/j.jmb.2006.11.031)
    • Monzingo, A. F., Ozburn, A., Xia, S., Meyer, R. J. & Robertus, J. D. 2007 The structure of the minimal relaxase domain of MobA at 2.1 A°resolution. J. Mol. Biol. 366, 165-178. (doi:10.1016/j.jmb.2006.11.031)
    • (2007) J. Mol. Biol , vol.366 , pp. 165-178
    • Monzingo, A.F.1    Ozburn, A.2    Xia, S.3    Meyer, R.J.4    Robertus, J.D.5
  • 64
    • 33646850212 scopus 로고    scopus 로고
    • Unveiling the molecular mechanism of a conjugative relaxase: The structure of TrwC complexed with a 27-mer DNA comprising the recognition hairpin and the cleavage site
    • doi:10. 1016/j.jmb.2006.02.018)
    • Boer, R., Russi, S., Guasch, A., Lucas, M., Blanco, A. G., Pe ́rez-Luque, R., Coll, M. & De La Cruz, F. 2006 Unveiling the molecular mechanism of a conjugative relaxase: the structure of TrwC complexed with a 27-mer DNA comprising the recognition hairpin and the cleavage site. J. Mol. Biol. 358, 857-869. (doi:10. 1016/j.jmb.2006.02.018)
    • (2006) J. Mol. Biol , vol.358 , pp. 857-869
    • Boer, R.1    Russi, S.2    Guasch, A.3    Lucas, M.4    Blanco, A.G.5    Pérez-Luque, R.6    Coll, M.7    de la Cruz, F.8
  • 65
    • 26444521223 scopus 로고    scopus 로고
    • Inter- and intramolecular determinants of the specificity of single-stranded DNA binding and cleavage by the F factor relaxase
    • doi:10. 1016/j.str.2005.06.013)
    • Larkin, C., Datta, S., Harley, M. J., Anderson, B. J., Ebie, A., Hargreaves, V. & Schildbach, J. F. 2005 Inter- and intramolecular determinants of the specificity of single-stranded DNA binding and cleavage by the F factor relaxase. Structure 13, 1533-1544. (doi:10. 1016/j.str.2005.06.013)
    • (2005) Structure , vol.13 , pp. 1533-1544
    • Larkin, C.1    Datta, S.2    Harley, M.J.3    Anderson, B.J.4    Ebie, A.5    Hargreaves, V.6    Schildbach, J.F.7
  • 66
    • 79954432560 scopus 로고    scopus 로고
    • Tyrosine partners coordinate DNA nicking by the Salmonella typhimurium plasmid pCU1 relaxase enzyme
    • doi:10.1016/j. febslet.2011.03.043)
    • Nash, R. P., Niblock, F. C. & Redinbo, M. R. 2011 Tyrosine partners coordinate DNA nicking by the Salmonella typhimurium plasmid pCU1 relaxase enzyme. FEBS Lett. 585, 1216-1222. (doi:10.1016/j. febslet.2011.03.043)
    • (2011) FEBS Lett , vol.585 , pp. 1216-1222
    • Nash, R.P.1    Niblock, F.C.2    Redinbo, M.R.3
  • 67
    • 0038687623 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of MbeA, the relaxase involved in plasmid ColE1 conjugative mobilization
    • doi:10.1046/j.1365-2958.2003.03441.x)
    • Varsaki, A., Lucas, M., Afendra, A. S., Drainas, C. & De La Cruz, F. 2003 Genetic and biochemical characterization of MbeA, the relaxase involved in plasmid ColE1 conjugative mobilization. Mol. Microbiol. 48, 481-493. (doi:10.1046/j.1365-2958.2003.03441.x)
    • (2003) Mol. Microbiol , vol.48 , pp. 481-493
    • Varsaki, A.1    Lucas, M.2    Afendra, A.S.3    Drainas, C.4    de la Cruz, F.5
  • 68
    • 65549113871 scopus 로고    scopus 로고
    • Changing the recognition site of a conjugative relaxase by rational design
    • doi:10.1002/biot.200800184)
    • Gonzalez-Perez, B., Carballeira, J. D., Moncalian, G. & De La Cruz, F. 2009 Changing the recognition site of a conjugative relaxase by rational design. Biotechnol. J. 4, 554-557. (doi:10.1002/biot.200800184)
    • (2009) Biotechnol. J , vol.4 , pp. 554-557
    • Gonzalez-Perez, B.1    Carballeira, J.D.2    Moncalian, G.3    de la Cruz, F.4
  • 69
    • 34547632567 scopus 로고    scopus 로고
    • Disrupting antibiotic resistance propagation by inhibiting the conjugative DNA relaxase
    • doi:10.1073/pnas.0702760104)
    • Lujan, S. A., Guogas, L. M., Ragonese, H., Matson, S. W. & Redinbo, M. R. 2007 Disrupting antibiotic resistance propagation by inhibiting the conjugative DNA relaxase. Proc. Natl Acad. Sci. USA 104, 12282-12287. (doi:10.1073/pnas.0702760104)
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 12282-12287
    • Lujan, S.A.1    Guogas, L.M.2    Ragonese, H.3    Matson, S.W.4    Redinbo, M.R.5
  • 71
    • 0015235693 scopus 로고
    • F 1 sex factor of Escherichia coli. Size and purification in the form of a strand-specific relaxation complex of supercoiled deoxyribonucleic acid and protein
    • doi:10.1021/bi00802a022)
    • Kline, B. C. & Helinski, D. R. 1971 F 1 sex factor of Escherichia coli. Size and purification in the form of a strand-specific relaxation complex of supercoiled deoxyribonucleic acid and protein. Biochemistry 10, 4975-4980. (doi:10.1021/bi00802a022)
    • (1971) Biochemistry , vol.10 , pp. 4975-4980
    • Kline, B.C.1    Helinski, D.R.2
  • 72
    • 49249094306 scopus 로고    scopus 로고
    • An intrastrand three-DNA-base interaction is a key specificity determinant of F transfer initiation and of F TraI relaxase DNA recognition and cleavage
    • doi:10.1093/nar/ gkn422)
    • Hekman, K., Guja, K., Larkin, C. & Schildbach, J. F. 2008 An intrastrand three-DNA-base interaction is a key specificity determinant of F transfer initiation and of F TraI relaxase DNA recognition and cleavage. Nucleic Acids Res. 36, 4565-4572. (doi:10.1093/nar/ gkn422)
    • (2008) Nucleic Acids Res , vol.36 , pp. 4565-4572
    • Hekman, K.1    Guja, K.2    Larkin, C.3    Schildbach, J.F.4
  • 73
    • 32644437865 scopus 로고    scopus 로고
    • Examination of an inverted repeat within the F factor origin of transfer: Context dependence of F TraI relaxase DNA specificity
    • doi:10.1093/nar/ gkj444)
    • Williams, S. L. & Schildbach, J. F. 2006 Examination of an inverted repeat within the F factor origin of transfer: context dependence of F TraI relaxase DNA specificity. Nucleic Acids Res. 34, 426-435. (doi:10.1093/nar/ gkj444)
    • (2006) Nucleic Acids Res , vol.34 , pp. 426-435
    • Williams, S.L.1    Schildbach, J.F.2
  • 74
    • 0030928717 scopus 로고    scopus 로고
    • Chromosome and low copy plasmid segregation in E. coli: Visual evidence for distinct mechanisms
    • doi:10.1016/S0092-8674(00)80377-3)
    • Gordon, G. S., Sitnikov, D., Webb, C. D., Teleman, A., Straight, A., Losick, R., Murray, A. W. & Wright, A. 1997 Chromosome and low copy plasmid segregation in E. coli: visual evidence for distinct mechanisms. Cell 90, 1113-1121. (doi:10.1016/S0092-8674(00)80377-3)
    • (1997) Cell , vol.90 , pp. 1113-1121
    • Gordon, G.S.1    Sitnikov, D.2    Webb, C.D.3    Teleman, A.4    Straight, A.5    Losick, R.6    Murray, A.W.7    Wright, A.8
  • 75
    • 0036098377 scopus 로고    scopus 로고
    • Bacterial conjugative transfer: Visualization of successful mating pairs and plasmid establishment in live Escherichia coli
    • doi:10.1046/j.1365-2958.2002.02938.x)
    • Lawley, T. D., Gordon, G. S., Wright, A. & Taylor, D. E. 2002 Bacterial conjugative transfer: visualization of successful mating pairs and plasmid establishment in live Escherichia coli. Mol. Microbiol. 44, 947-956. (doi:10.1046/j.1365-2958.2002.02938.x)
    • (2002) Mol. Microbiol , vol.44 , pp. 947-956
    • Lawley, T.D.1    Gordon, G.S.2    Wright, A.3    Taylor, D.E.4
  • 76
    • 34249061772 scopus 로고    scopus 로고
    • Agrobacterium ParA/ MinD-like VirC1 spatially coordinates early conjugative DNA transfer reactions
    • doi:10.1038/sj.emboj.7601696)
    • Atmakuri, K., Cascales, E., Burton, O. T., Banta, L. M. & Christie, P. J. 2007 Agrobacterium ParA/ MinD-like VirC1 spatially coordinates early conjugative DNA transfer reactions. EMBO J. 26, 2540-2551. (doi:10.1038/sj.emboj.7601696)
    • (2007) EMBO J , vol.26 , pp. 2540-2551
    • Atmakuri, K.1    Cascales, E.2    Burton, O.T.3    Banta, L.M.4    Christie, P.J.5
  • 77
    • 38049160003 scopus 로고    scopus 로고
    • Recruitment of conjugative DNA transfer substrate to Agrobacterium type IV secretion apparatus
    • doi:10.1073/ pnas.0701738104)
    • Guo, M., Jin, S., Sun, D., Hew, C. L. & Pan, S. Q. 2007 Recruitment of conjugative DNA transfer substrate to Agrobacterium type IV secretion apparatus. Proc. Natl Acad. Sci. USA 104, 20019-20024. (doi:10.1073/ pnas.0701738104)
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 20019-20024
    • Guo, M.1    Jin, S.2    Sun, D.3    Hew, C.L.4    Pan, S.Q.5
  • 79
    • 14144249589 scopus 로고    scopus 로고
    • A C-terminal translocation signal required for Dot/Icm-dependent delivery of the Legionella RalF protein to host cells
    • doi:10. 1073/pnas.0406239101)
    • Nagai, H., Cambronne, E. D., Kagan, J. C., Amor, J. C., Kahn, R. A. & Roy, C. R. 2005 A C-terminal translocation signal required for Dot/Icm-dependent delivery of the Legionella RalF protein to host cells. Proc. Natl Acad. Sci USA 102, 826-831. (doi:10. 1073/pnas.0406239101)
    • (2005) Proc. Natl Acad. Sci USA , vol.102 , pp. 826-831
    • Nagai, H.1    Cambronne, E.D.2    Kagan, J.C.3    Amor, J.C.4    Kahn, R.A.5    Roy, C.R.6
  • 80
    • 14144255290 scopus 로고    scopus 로고
    • Positive charge is an important feature of the C-terminal transport signal of the VirB/D4-translocated proteins of Agrobacterium
    • doi:10.1073/pnas.0406241102)
    • Vergunst, A. C., Van Lier, M. C., Den Dulk-Ras, A., Stuve, T. A., Ouwehand, A. & Hooykaas, P. J. 2005 Positive charge is an important feature of the C-terminal transport signal of the VirB/D4-translocated proteins of Agrobacterium. Proc. Natl Acad. Sci USA 102, 832-837. (doi:10.1073/pnas.0406241102)
    • (2005) Proc. Natl Acad. Sci USA , vol.102 , pp. 832-837
    • Vergunst, A.C.1    van Lier, M.C.2    den Dulk-Ras, A.3    Stuve, T.A.4    Ouwehand, A.5    Hooykaas, P.J.6
  • 81
    • 14144255575 scopus 로고    scopus 로고
    • A bipartite signal mediates the transfer of type IV secretion substrates of Bartonella henselae into human cells
    • doi:10.1073/pnas.0406796102)
    • Schulein, R., Guye, P., Rhomberg, T. A., Schmid, M. C., Schröder, G., Vergunst, A. C., Carena, I. & Dehio, C. 2005 A bipartite signal mediates the transfer of type IV secretion substrates of Bartonella henselae into human cells. Proc. Natl Acad. Sci USA 102, 856-861. (doi:10.1073/pnas.0406796102)
    • (2005) Proc. Natl Acad. Sci USA , vol.102 , pp. 856-861
    • Schulein, R.1    Guye, P.2    Rhomberg, T.A.3    Schmid, M.C.4    Schröder, G.5    Vergunst, A.C.6    Carena, I.7    Dehio, C.8
  • 82
    • 33645090948 scopus 로고    scopus 로고
    • A C-terminal translocation signal is necessary, but not sufficient for type IV secretion of the Helicobacter pylori CagA protein
    • doi:10.1111/j.1365-2958.2006.05050.x)
    • Hohlfeld, S., Pattis, I., Puls, J., Plano, G. V., Haas, R. & Fischer, W. 2006 A C-terminal translocation signal is necessary, but not sufficient for type IV secretion of the Helicobacter pylori CagA protein. Mol. Microbiol. 59, 1624-1637. (doi:10.1111/j.1365-2958.2006.05050.x)
    • (2006) Mol. Microbiol , vol.59 , pp. 1624-1637
    • Hohlfeld, S.1    Pattis, I.2    Puls, J.3    Plano, G.V.4    Haas, R.5    Fischer, W.6
  • 83
    • 34548702664 scopus 로고    scopus 로고
    • The R1162 relaxase/ primase contains two, type IV transport signals that require the small plasmid protein MobB
    • doi:10.1111/j.1365-2958.2007. 05925.x)
    • Parker, C. & Meyer, R. J. 2007 The R1162 relaxase/ primase contains two, type IV transport signals that require the small plasmid protein MobB. Mol. Microbiol. 66, 252-261. (doi:10.1111/j.1365-2958.2007. 05925.x)
    • (2007) Mol. Microbiol , vol.66 , pp. 252-261
    • Parker, C.1    Meyer, R.J.2
  • 84
    • 78650030219 scopus 로고    scopus 로고
    • Molecular recognition determinants for type IV secretion of diverse families of conjugative relaxases
    • doi:10. 1111/j.1365-2958.2010.07423.x)
    • Lang, S. et al. 2010 Molecular recognition determinants for type IV secretion of diverse families of conjugative relaxases. Mol. Microbiol. 78, 1539-1555. (doi:10. 1111/j.1365-2958.2010.07423.x)
    • (2010) Mol. Microbiol , vol.78 , pp. 1539-1555
    • Lang, S.1
  • 85
    • 2442483942 scopus 로고    scopus 로고
    • Genetic evidence of a coupling role for the TraG protein family in bacterial conjugation
    • doi:10.1007/s004380050432)
    • Cabezo ́n, E., Sastre, J. I. & De La Cruz, F. 1997 Genetic evidence of a coupling role for the TraG protein family in bacterial conjugation. Mol. Gen. Genet. 254, 400-406. (doi:10.1007/s004380050432)
    • (1997) Mol. Gen. Genet , vol.254 , pp. 400-406
    • Cabezón, E.1    Sastre, J.I.2    de la Cruz, F.3
  • 86
    • 0031765579 scopus 로고    scopus 로고
    • The carboxyl terminus of protein TraD adds specificity and efficiency to F-plasmid conjugative transfer
    • Sastre, J. I., Cabezo ́n, E. & De La Cruz, F. 1998 The carboxyl terminus of protein TraD adds specificity and efficiency to F-plasmid conjugative transfer. J. Bacteriol. 180, 6039-6042.
    • (1998) J. Bacteriol , vol.180 , pp. 6039-6042
    • Sastre, J.I.1    Cabezón, E.2    de la Cruz, F.3
  • 87
    • 0034053027 scopus 로고    scopus 로고
    • TraG from RP4 and TraG and VirD4 from Ti plasmids confer relaxosome specificity to the conjugal transfer system of pTiC58
    • doi:10.1128/JB.182.6.1541-1548.2000)
    • Hamilton, C. M., Lee, H., Li, P. L., Cook, D. M., Piper, K. R., Von Bodman, S. B., Lanka, E., Ream, W. & Farrand, S. K. 2000 TraG from RP4 and TraG and VirD4 from Ti plasmids confer relaxosome specificity to the conjugal transfer system of pTiC58. J. Bacteriol. 182, 1541-1548. (doi:10.1128/JB.182.6.1541-1548.2000)
    • (2000) J. Bacteriol , vol.182 , pp. 1541-1548
    • Hamilton, C.M.1    Lee, H.2    Li, P.L.3    Cook, D.M.4    Piper, K.R.5    von Bodman, S.B.6    Lanka, E.7    Ream, W.8    Farrand, S.K.9
  • 88
    • 80655146184 scopus 로고    scopus 로고
    • Transfer of R388 derivatives by a pathogenesis-associated type IV secretion system into both bacteria and human cells
    • doi:10.1128/JB.05905-11)
    • Ferna ́ndez-Gonza ́lez, E., De Paz, H. D., Alperi, A., Agu ́ndez, L., Faustmann, M., Sangari, F. J., Dehio, C. & Llosa, M. 2011 Transfer of R388 derivatives by a pathogenesis-associated type IV secretion system into both bacteria and human cells. J. Bacteriol. 193, 6257-6265. (doi:10.1128/JB.05905-11)
    • (2011) J. Bacteriol , vol.193 , pp. 6257-6265
    • Fernández-González, E.1    de Paz, H.D.2    Alperi, A.3    Agúndez, L.4    Faustmann, M.5    Sangari, F.J.6    Dehio, C.7    Llosa, M.8
  • 89
    • 71449116162 scopus 로고    scopus 로고
    • Biological diversity of prokaryotic type IV secretion systems
    • doi:10.1128/MMBR.00023-09)
    • Alvarez-Martinez, C. E. & Christie, P. J. 2009 Biological diversity of prokaryotic type IV secretion systems. Microbiol. Mol. Biol. Rev. 73, 775-808. (doi:10.1128/MMBR.00023-09)
    • (2009) Microbiol. Mol. Biol. Rev , vol.73 , pp. 775-808
    • Alvarez-Martinez, C.E.1    Christie, P.J.2
  • 90
    • 33748329483 scopus 로고    scopus 로고
    • The Legionella pneumophila IcmS-LvgA protein complex is important for Dot/Icm-dependent intracellular growth
    • doi:10.1111/j.1365-2958. 2006.05243.x)
    • Vincent, C. D. & Vogel, J. P. 2006 The Legionella pneumophila IcmS-LvgA protein complex is important for Dot/Icm-dependent intracellular growth. Mol. Microbiol. 61, 596-613. (doi:10.1111/j.1365-2958. 2006.05243.x)
    • (2006) Mol. Microbiol , vol.61 , pp. 596-613
    • Vincent, C.D.1    Vogel, J.P.2
  • 91
    • 78649926107 scopus 로고    scopus 로고
    • The coupling protein Cagb and its interaction partner CagZ are required for type IV secretion of the Helicobacter pylori CagA protein
    • doi:10.1128/IAI.00796-10)
    • Jurik, A., Hausser, E., Kutter, S., Pattis, I., Prassl, S., Weiss, E. & Fischer, W. 2010 The coupling protein Cagb and its interaction partner CagZ are required for type IV secretion of the Helicobacter pylori CagA protein. Infect. Immun. 78, 5244-5251. (doi:10.1128/IAI.00796-10)
    • (2010) Infect. Immun , vol.78 , pp. 5244-5251
    • Jurik, A.1    Hausser, E.2    Kutter, S.3    Pattis, I.4    Prassl, S.5    Weiss, E.6    Fischer, W.7
  • 92
    • 0035725211 scopus 로고    scopus 로고
    • Systematic mutagenesis of the Helicobacter pylori cag pathogenicity island: Essential genes for CagA translocation in host cells and induction of interleukin-8
    • doi:10.1046/j.1365-2958.2001.02714.x)
    • Fischer, W., Puls, J., Buhrdorf, R., Gebert, B., Odenbreit, S. & Haas, R. 2001 Systematic mutagenesis of the Helicobacter pylori cag pathogenicity island: essential genes for CagA translocation in host cells and induction of interleukin-8. Mol. Microbiol. 42, 1337-1348. (doi:10.1046/j.1365-2958.2001.02714.x)
    • (2001) Mol. Microbiol , vol.42 , pp. 1337-1348
    • Fischer, W.1    Puls, J.2    Buhrdorf, R.3    Gebert, B.4    Odenbreit, S.5    Haas, R.6
  • 93
    • 0036156209 scopus 로고    scopus 로고
    • Functional analysis of the Helicobacter pylori cag pathogenicity island reveals both VirD4-CagAdependent and VirD4-CagA-independent mechanisms
    • doi:10.1128/IAI.70.2. 665-671.2002)
    • Selbach, M., Moese, S., Meyer, T. F. & Backert, S. 2002 Functional analysis of the Helicobacter pylori cag pathogenicity island reveals both VirD4-CagAdependent and VirD4-CagA-independent mechanisms. Infect. Immun. 70, 665-671. (doi:10.1128/IAI.70.2. 665-671.2002)
    • (2002) Infect. Immun , vol.70 , pp. 665-671
    • Selbach, M.1    Moese, S.2    Meyer, T.F.3    Backert, S.4
  • 94
    • 29644447799 scopus 로고    scopus 로고
    • Interaction with CagF is required for translocation of CagA into the host via the Helicobacter pylori type IV secretion system
    • doi:10.1128/IAI.74.1.273-281.2006)
    • Couturier, M. R., Tasca, E., Montecucco, C. & Stein, M. 2006 Interaction with CagF is required for translocation of CagA into the host via the Helicobacter pylori type IV secretion system. Infect. Immun. 74, 273-281. (doi:10.1128/IAI.74.1.273-281.2006)
    • (2006) Infect. Immun , vol.74 , pp. 273-281
    • Couturier, M.R.1    Tasca, E.2    Montecucco, C.3    Stein, M.4
  • 95
    • 34948822413 scopus 로고    scopus 로고
    • The Helicobacter pylori CagF protein is a type IV secretion chaperone-like molecule that binds close to the C-terminal secretion signal of the CagA effector protein
    • doi:10.1099/ mic.0.2007/007385-0)
    • Pattis, I., Weiss, E., Laugks, R., Haas, R. & Fischer, W. 2007 The Helicobacter pylori CagF protein is a type IV secretion chaperone-like molecule that binds close to the C-terminal secretion signal of the CagA effector protein. Microbiology 153, 2896-2909. (doi:10.1099/ mic.0.2007/007385-0)
    • (2007) Microbiology , vol.153 , pp. 2896-2909
    • Pattis, I.1    Weiss, E.2    Laugks, R.3    Haas, R.4    Fischer, W.5
  • 96
    • 71549146932 scopus 로고    scopus 로고
    • Conjugative DNA metabolism in Gramnegative bacteria
    • doi:10.1111/j.1574-6976.2009.00195.x)
    • De La Cruz, F., Frost, L. S., Meyer, R. J. & Zechner, E. L. 2010 Conjugative DNA metabolism in Gramnegative bacteria. FEMS Microbiol. Rev. 34, 18-40. (doi:10.1111/j.1574-6976.2009.00195.x)
    • (2010) FEMS Microbiol. Rev , vol.34 , pp. 18-40
    • de la Cruz, F.1    Frost, L.S.2    Meyer, R.J.3    Zechner, E.L.4
  • 97
    • 80055090397 scopus 로고    scopus 로고
    • Structural basis of cooperative DNA recognition by the plasmid conjugation factor
    • doi:10. 1093/nar/gkr296)
    • Wong, J. J., Lu, J., Edwards, R. A., Frost, L. S. & Glover, J. N. 2011 Structural basis of cooperative DNA recognition by the plasmid conjugation factor, TraM. Nucleic Acids Res. 12, 6775-6788. (doi:10. 1093/nar/gkr296)
    • (2011) TraM. Nucleic Acids Res , vol.12 , pp. 6775-6788
    • Wong, J.J.1    Lu, J.2    Edwards, R.A.3    Frost, L.S.4    Glover, J.N.5
  • 98
    • 4944235151 scopus 로고    scopus 로고
    • Thirty-eight C-terminal amino acids of the coupling protein TraD of the F-like conjugative resistance plasmid R1 are required and sufficient to confer binding to the substrate selector protein TraM
    • doi:10.1128/JB.186.20.6999-7006.2004)
    • Beranek, A., Zettl, M., Lorenzoni, K., Schauer, A., Manhart, M. & Koraimann, G. 2004 Thirty-eight C-terminal amino acids of the coupling protein TraD of the F-like conjugative resistance plasmid R1 are required and sufficient to confer binding to the substrate selector protein TraM. J. Bacteriol. 186, 6999-7006. (doi:10.1128/JB.186.20.6999-7006.2004)
    • (2004) J. Bacteriol , vol.186 , pp. 6999-7006
    • Beranek, A.1    Zettl, M.2    Lorenzoni, K.3    Schauer, A.4    Manhart, M.5    Koraimann, G.6
  • 99
    • 51649126017 scopus 로고    scopus 로고
    • Structural basis of specific TraD-TraM recognition during F plasmid-mediated bacterial conjugation
    • doi:10.1111/j.1365-2958.2008.06391.x)
    • Lu, J., Wong, J. J., Edwards, R. A., Manchak, J., Frost, L. S. & Glover, J. N. 2008 Structural basis of specific TraD-TraM recognition during F plasmid-mediated bacterial conjugation. Mol. Microbiol. 70, 89-99. (doi:10.1111/j.1365-2958.2008.06391.x)
    • (2008) Mol. Microbiol , vol.70 , pp. 89-99
    • Lu, J.1    Wong, J.J.2    Edwards, R.A.3    Manchak, J.4    Frost, L.S.5    Glover, J.N.6
  • 100
    • 70350445529 scopus 로고    scopus 로고
    • Plasmid R1 conjugative DNA processing is regulated at the coupling protein interface
    • doi:10.1128/ JB.00918-09)
    • Mihajlovic, S. et al. 2009 Plasmid R1 conjugative DNA processing is regulated at the coupling protein interface. J. Bacteriol. 191, 6877-6887. (doi:10.1128/ JB.00918-09)
    • (2009) J. Bacteriol , vol.191 , pp. 6877-6887
    • Mihajlovic, S.1
  • 101
    • 0033579554 scopus 로고    scopus 로고
    • Characterization of ATP and DNA binding activities of TrwB, the coupling protein essential in plasmid R388 conjugation
    • doi:10.1074/jbc.274.51.36117)
    • Moncali ́an, G., Cabezo ́n, E., Alkorta, I., Valle, M., Moro, F., Valpuesta, J. M., Goni, F. M. &De La Cruz, F. 1999 Characterization of ATP and DNA binding activities of TrwB, the coupling protein essential in plasmid R388 conjugation. J. Biol. Chem. 274, 36117-36124. (doi:10.1074/jbc.274.51.36117)
    • (1999) J. Biol. Chem , vol.274 , pp. 36117-36124
    • Moncalían, G.1    Cabezón, E.2    Alkorta, I.3    Valle, M.4    Moro, F.5    Valpuesta, J.M.6    Goni, F.M.7    de la Cruz, F.8
  • 102
    • 16644395003 scopus 로고    scopus 로고
    • Plant proteins that interact with VirB2, the Agrobacterium tumefaciens pilin protein, mediate plant transformation
    • doi:10.1105/tpc.104.026476)
    • Hwang, H. H. & Gelvin, S. B. 2004 Plant proteins that interact with VirB2, the Agrobacterium tumefaciens pilin protein, mediate plant transformation. Plant Cell 16, 3148-3167. (doi:10.1105/tpc.104.026476)
    • (2004) Plant Cell , vol.16 , pp. 3148-3167
    • Hwang, H.H.1    Gelvin, S.B.2
  • 103
    • 74549215037 scopus 로고    scopus 로고
    • Helicobacter pylori type IV secretion apparatus exploits beta1 integrin in a novel RGD-independent manner
    • doi:10.1371/journal.ppat.1000684)
    • Jimenez-Soto, L. F. et al. 2009 Helicobacter pylori type IV secretion apparatus exploits beta1 integrin in a novel RGD-independent manner. PLoS Pathog. 5, e1000684. (doi:10.1371/journal.ppat.1000684)
    • (2009) PLoS Pathog , vol.5
    • Jimenez-Soto, L.F.1
  • 104
    • 0035954733 scopus 로고    scopus 로고
    • Natural conjugative plasmids induce bacterial biofilm development
    • doi:10.1038/35086581)
    • Ghigo, J. M. 2001 Natural conjugative plasmids induce bacterial biofilm development. Nature 412, 442-445. (doi:10.1038/35086581)
    • (2001) Nature , vol.412 , pp. 442-445
    • Ghigo, J.M.1
  • 105
    • 0037512322 scopus 로고    scopus 로고
    • Development andmaturation of Escherichia coli K-12 biofilms
    • doi:10.1046/j.1365-2958.2003.03490.x)
    • Reisner, A., Haagensen, J. A. J., Schembri, M. A., Zechner, E. L. & Molin, S. 2003 Development andmaturation of Escherichia coli K-12 biofilms. Mol. Microbiol. 48, 933-946. (doi:10.1046/j.1365-2958.2003.03490.x)
    • (2003) Mol. Microbiol , vol.48 , pp. 933-946
    • Reisner, A.1    Haagensen, J.A.J.2    Schembri, M.A.3    Zechner, E.L.4    Molin, S.5
  • 107
    • 0025934745 scopus 로고
    • Conjugational junctions: Morphology of specific contacts in conjugating Escherichia coli bacteria
    • doi:10.1016/1047-8477(91)90018-R)
    • Durrenberger, M. B., Villiger, W. & Bachi, T. 1991 Conjugational junctions: morphology of specific contacts in conjugating Escherichia coli bacteria. J. Struct. Biol. 107, 146-156. (doi:10.1016/1047-8477(91)90018-R)
    • (1991) J. Struct. Biol , vol.107 , pp. 146-156
    • Durrenberger, M.B.1    Villiger, W.2    Bachi, T.3
  • 108
    • 0034097777 scopus 로고    scopus 로고
    • Conjugative junctions in RP4-mediated mating of Escherichia coli
    • doi:10.1128/JB.182. 10.2709-2715.2000)
    • Samuels, A. L., Lanka, E. & Davies, J. E. 2000 Conjugative junctions in RP4-mediated mating of Escherichia coli. J. Bacteriol. 182, 2709-2715. (doi:10.1128/JB.182. 10.2709-2715.2000)
    • (2000) J. Bacteriol , vol.182 , pp. 2709-2715
    • Samuels, A.L.1    Lanka, E.2    Davies, J.E.3
  • 109
    • 40849098551 scopus 로고    scopus 로고
    • Direct visualization of horizontal gene transfer
    • doi:10.1126/ science.1153498)
    • Babic, A., Lindner, A. B., Vulic, M., Stewart, E. J. & Radman, M. 2008 Direct visualization of horizontal gene transfer. Science 319, 1533-1536. (doi:10.1126/ science.1153498)
    • (2008) Science , vol.319 , pp. 1533-1536
    • Babic, A.1    Lindner, A.B.2    Vulic, M.3    Stewart, E.J.4    Radman, M.5
  • 110
    • 0025678652 scopus 로고
    • The F pilus of Escherichia coli appears to support stable DNA transfer in the absence of wall-to-wall contact between cells
    • Harrington, L. C. & Rogerson, A. C. 1990 The F pilus of Escherichia coli appears to support stable DNA transfer in the absence of wall-to-wall contact between cells. J. Bacteriol. 172, 7263-7264.
    • (1990) J. Bacteriol , vol.172 , pp. 7263-7264
    • Harrington, L.C.1    Rogerson, A.C.2
  • 111
    • 82155162342 scopus 로고    scopus 로고
    • An activation domain of plasmid R1 TraI protein delineates stages of gene transfer initiation
    • doi:10.1111/j.1365-2958. 2011.07872.x)
    • Lang, S., Kirchberger, P. C., Gruber, C. J., Redzej, A., Raffl, S., Zellnig, G., Zangger, K. & Zechner, E. L. 2011 An activation domain of plasmid R1 TraI protein delineates stages of gene transfer initiation. Mol Microbiol. 82, 1071-1085. (doi:10.1111/j.1365-2958. 2011.07872.x)
    • (2011) Mol Microbiol , vol.82 , pp. 1071-1085
    • Lang, S.1    Kirchberger, P.C.2    Gruber, C.J.3    Redzej, A.4    Raffl, S.5    Zellnig, G.6    Zangger, K.7    Zechner, E.L.8
  • 112
    • 77951034296 scopus 로고    scopus 로고
    • Biochemical dissection of the ATPase TraB, the VirB4 homologue of the Escherichia coli pKM101 conjugation machinery
    • doi:10.1128/ JB.01384-09)
    • Durand, E., Oomen, C. & Waksman, G. 2010 Biochemical dissection of the ATPase TraB, the VirB4 homologue of the Escherichia coli pKM101 conjugation machinery. J Bacteriol. 192, 2315-2323. (doi:10.1128/ JB.01384-09)
    • (2010) J Bacteriol , vol.192 , pp. 2315-2323
    • Durand, E.1    Oomen, C.2    Waksman, G.3
  • 113
    • 0026623139 scopus 로고
    • Localization of TraC, a protein involved in assembly of the F conjugative pilus
    • Schandel, K. A., Muller, M. M. & Webster, R. E. 1992 Localization of TraC, a protein involved in assembly of the F conjugative pilus. J. Bacteriol. 174, 3800-3806.
    • (1992) J. Bacteriol , vol.174 , pp. 3800-3806
    • Schandel, K.A.1    Muller, M.M.2    Webster, R.E.3
  • 114
    • 20444431234 scopus 로고    scopus 로고
    • TrwB, the coupling protein involved in DNA transport during bacterial conjugation, is a DNAdependent ATPase
    • doi:10.1073/pnas.0503402102)
    • Tato, I., Zunzunegui, S., De La Cruz, F. & Cabezo ́n, E. 2005 TrwB, the coupling protein involved in DNA transport during bacterial conjugation, is a DNAdependent ATPase. Proc. Natl Acad. Sci. USA 102, 8156-8161. (doi:10.1073/pnas.0503402102)
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 8156-8161
    • Tato, I.1    Zunzunegui, S.2    de la Cruz, F.3    Cabezón, E.4
  • 115
    • 48149115518 scopus 로고    scopus 로고
    • ATPase activity and oligomeric state of TrwK, the VirB4 homologue of the plasmid R388 type IV secretion system
    • doi:10.1128/JB.00321-08)
    • Arechaga, I., Pen ̃a, A., Zunzunegui, S., Del Carmen Ferna ́ndez-Alonso, M., Rivas, G. & De La Cruz, F. 2008 ATPase activity and oligomeric state of TrwK, the VirB4 homologue of the plasmid R388 type IV secretion system. J. Bacteriol. 190, 5472-5479. (doi:10.1128/JB.00321-08)
    • (2008) J. Bacteriol , vol.190 , pp. 5472-5479
    • Arechaga, I.1    Peña, A.2    Zunzunegui, S.3    Carmen, D.4    Fernández-Alonso, M.5    Rivas, G.6    de la Cruz, F.7
  • 116
    • 34548583310 scopus 로고    scopus 로고
    • In vivo oligomerization of the F conjugative coupling protein TraD
    • doi:10.1128/JB.00513-07)
    • Haft, R. J., Gachelet, E. G., Nguyen, T., Toussaint, L., Chivian, D. & Traxler, B. 2007 In vivo oligomerization of the F conjugative coupling protein TraD. J. Bacteriol. 189, 6626-6634. (doi:10.1128/JB.00513-07)
    • (2007) J. Bacteriol , vol.189 , pp. 6626-6634
    • Haft, R.J.1    Gachelet, E.G.2    Nguyen, T.3    Toussaint, L.4    Chivian, D.5    Traxler, B.6
  • 117
    • 82155166306 scopus 로고    scopus 로고
    • Caught in the act: The dialogue between bacteriophage R17 and the type IV secretion machine of plasmid R1
    • doi:10.1111/j.1365-2958.2011.07870.x)
    • Berry, T. M. & Christie, P. J. 2011 Caught in the act: the dialogue between bacteriophage R17 and the type IV secretion machine of plasmid R1. Mol. Microbiol. 82, 1039-1043. (doi:10.1111/j.1365-2958.2011.07870.x)
    • (2011) Mol. Microbiol , vol.82 , pp. 1039-1043
    • Berry, T.M.1    Christie, P.J.2
  • 118
    • 13244296604 scopus 로고    scopus 로고
    • Protein tagging and detection with engineered selfassembling fragments of green fluorescent protein
    • doi:10.1038/nbt1044)
    • Cabantous, S., Terwilliger, T. C. & Waldo, G. S. 2005 Protein tagging and detection with engineered selfassembling fragments of green fluorescent protein. Nat. Biotechnol. 23, 102-107. (doi:10.1038/nbt1044)
    • (2005) Nat. Biotechnol , vol.23 , pp. 102-107
    • Cabantous, S.1    Terwilliger, T.C.2    Waldo, G.S.3
  • 119
    • 11344295652 scopus 로고    scopus 로고
    • Bacterial conjugation: A potential tool for genomic engineering
    • doi:10.1016/j.resmic.2004.07.008)
    • Llosa, M. & De La Cruz, F. 2005 Bacterial conjugation: a potential tool for genomic engineering. Res. Microbiol. 156, 1-6. (doi:10.1016/j.resmic.2004.07.008)
    • (2005) Res. Microbiol , vol.156 , pp. 1-6
    • Llosa, M.1    de la Cruz, F.2
  • 120
    • 33645945885 scopus 로고    scopus 로고
    • Agrobacterium-mediated genetic transformation of plants: Biology and biotechnology
    • doi:10. 1016/j.copbio.2006.01.009)
    • Tzfira, T. & Citovsky, V. 2006 Agrobacterium-mediated genetic transformation of plants: biology and biotechnology. Curr. Opin. Biotechnol. 17, 147-154. (doi:10. 1016/j.copbio.2006.01.009)
    • (2006) Curr. Opin. Biotechnol , vol.17 , pp. 147-154
    • Tzfira, T.1    Citovsky, V.2


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