메뉴 건너뛰기




Volumn 151, Issue 11, 2005, Pages 3541-3548

Fluorescence assays for F-pili and their application

Author keywords

[No Author keywords available]

Indexed keywords

PILIN;

EID: 27744587418     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.28159-0     Document Type: Article
Times cited : (13)

References (50)
  • 1
    • 0000483469 scopus 로고
    • A redefinition of the mating phenomenon in bacteria
    • Edited by J. Reissig London: Chapman & Hall
    • Achtman, M. & Skurray, R. (1977). A redefinition of the mating phenomenon in bacteria. In Microbial Interactions, pp. 234-279. Edited by J. Reissig. London: Chapman & Hall.
    • (1977) Microbial Interactions , pp. 234-279
    • Achtman, M.1    Skurray, R.2
  • 2
    • 0015057741 scopus 로고
    • Beginning a genetic analysis of conjugational transfer determined by the F factor in Escherichia coli by isolation and characterization of transfer-deficient mutants
    • Achtman, M., Willetts, N. & Clark, J. (1972). Beginning a genetic analysis of conjugational transfer determined by the F factor in Escherichia coli by isolation and characterization of transfer-deficient mutants. J Bacteriol 106, 529-538.
    • (1972) J. Bacteriol. , vol.106 , pp. 529-538
    • Achtman, M.1    Willetts, N.2    Clark, J.3
  • 3
    • 0028001615 scopus 로고
    • The role of the pilus in recipient cell recognition during bacterial conjugation mediated by F-like plasmids
    • Anthony, K., Sherburne, C., Sherburne, R. & Frost, L. (1994). The role of the pilus in recipient cell recognition during bacterial conjugation mediated by F-like plasmids. Mol Microbiol 13, 939-953.
    • (1994) Mol. Microbiol. , vol.13 , pp. 939-953
    • Anthony, K.1    Sherburne, C.2    Sherburne, R.3    Frost, L.4
  • 4
    • 0021235913 scopus 로고
    • Light-microscopic visualization of F and type 1 pili
    • Biebricher, C. & Duker, E.-M. (1984). Light-microscopic visualization of F and type 1 pili. J Gen Microbiol 130, 941-949.
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 941-949
    • Biebricher, C.1    Duker, E.-M.2
  • 5
    • 0017180055 scopus 로고
    • Regulation of the regulatory gene for the arabinose pathway, araC
    • Casadaban, M. (1976). Regulation of the regulatory gene for the arabinose pathway, araC. J Mol Biol 104, 557-566.
    • (1976) J. Mol. Biol. , vol.104 , pp. 557-566
    • Casadaban, M.1
  • 6
    • 0014603432 scopus 로고
    • Early stages of conjugation in Escherichia coli
    • Curtiss, R., Caro, L., Allison, D. & Stallions, D. (1969). Early stages of conjugation in Escherichia coli. J Bacteriol 100, 1091-1104.
    • (1969) J. Bacteriol. , vol.100 , pp. 1091-1104
    • Curtiss, R.1    Caro, L.2    Allison, D.3    Stallions, D.4
  • 7
    • 0025934745 scopus 로고
    • Conjugational junctions: Morphology of specific contacts in conjugating Escherichia coli bacteria
    • Durrenberger, M., Villiger, W. & Bachi, Th. (1991). Conjugational junctions: morphology of specific contacts in conjugating Escherichia coli bacteria. J Struct Biol 107, 146-156.
    • (1991) J. Struct. Biol. , vol.107 , pp. 146-156
    • Durrenberger, M.1    Villiger, W.2    Bachi, Th.3
  • 8
    • 0033529624 scopus 로고    scopus 로고
    • Conjugative pili of IncP plasmids, and the Ti plasmid T pilus are composed of cyclic subunits
    • Eisenbrandt, R., Kalkum, M., Lai, E., Lurz, R., Kado, C. & 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.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22548-22555
    • Eisenbrandt, R.1    Kalkum, M.2    Lai, E.3    Lurz, R.4    Kado, C.5    Lanka, E.6
  • 9
    • 0000862044 scopus 로고    scopus 로고
    • Structure and function of the F factor and mechanism of conjugation
    • Edited by F.C. Neidhardt and others Washington DC: American Society for Microbiology
    • Firth, N., Ippen-Ihler, K. & Skurray, R. (1996). Structure and function of the F factor and mechanism of conjugation. In Escherichia coli and Salmonella, Cellular and Molecular Biology, pp. 2377-2401. Edited by F. C. Neidhardt and others. Washington, DC: American Society for Microbiology.
    • (1996) Escherichia Coli and Salmonella, Cellular and Molecular Biology , pp. 2377-2401
    • Firth, N.1    Ippen-Ihler, K.2    Skurray, R.3
  • 11
    • 0021021912 scopus 로고
    • Genetic mapping and transcriptional orientation of the fimD gene
    • Freitag, C. & Eisenstein, B. (1983). Genetic mapping and transcriptional orientation of the fimD gene. J Bacteriol 156, 1052-1058.
    • (1983) J. Bacteriol. , vol.156 , pp. 1052-1058
    • Freitag, C.1    Eisenstein, B.2
  • 12
    • 0024049602 scopus 로고
    • DNA sequence analysis of point mutations in traA, the F-pilin gene, reveal two domains involved in F-specific phage attachment
    • Frost, L. & Paranchych, W. (1988). DNA sequence analysis of point mutations in traA, the F-pilin gene, reveal two domains involved in F-specific phage attachment. Mol Gen Genet 213, 134-139.
    • (1988) Mol. Gen. Genet. , vol.213 , pp. 134-139
    • Frost, L.1    Paranchych, W.2
  • 13
    • 0021505406 scopus 로고
    • DNA sequence of the F traALE region that includes the gene for F-pilin
    • Frost, L., Paranchych, W. & Willetts, N. (1984). DNA sequence of the F traALE region that includes the gene for F-pilin. J Bacteriol 160, 395-401.
    • (1984) J. Bacteriol. , vol.160 , pp. 395-401
    • Frost, L.1    Paranchych, W.2    Willetts, N.3
  • 14
    • 0022405839 scopus 로고
    • Characterization and sequence analysis of pilin from F-like plasmids
    • Frost, L., Finlay, B., Opgenorth, A., Paranchych, W. & Lee, J. (1985). Characterization and sequence analysis of pilin from F-like plasmids. J Bacteriol 164, 1238-1247.
    • (1985) J. Bacteriol. , vol.164 , pp. 1238-1247
    • Frost, L.1    Finlay, B.2    Opgenorth, A.3    Paranchych, W.4    Lee, J.5
  • 15
    • 0029799766 scopus 로고    scopus 로고
    • Pilus assembly by Agrobacterium T DNA genes
    • Fullner, K., Lara, J. & Nester, E. (1996). Pilus assembly by Agrobacterium T DNA genes. Science 273, 1107-1109.
    • (1996) Science , vol.273 , pp. 1107-1109
    • Fullner, K.1    Lara, J.2    Nester, E.3
  • 16
    • 0035159046 scopus 로고    scopus 로고
    • Cellular location and temperature-dependent assembly of IncH1 plasmid R27-encoded TrhC-associated conjugative transport protein complexes
    • Gilmour, M., Lawley, T., Rooker, M., Newnham, P. & Taylor, D. (2001). Cellular location and temperature-dependent assembly of IncH1 plasmid R27-encoded TrhC-associated conjugative transport protein complexes. Mol Microbiol 42, 705-715.
    • (2001) Mol. Microbiol. , vol.42 , pp. 705-715
    • Gilmour, M.1    Lawley, T.2    Rooker, M.3    Newnham, P.4    Taylor, D.5
  • 17
    • 0034050765 scopus 로고    scopus 로고
    • Components of the RP4 conjugative transfer apparatus form an envelope structure bridging inner and outer membranes of donor cells, implications for related macromolecular transport systems
    • Grahn, A., Haase, J., Bamford, D. & Lanka, E. (2000). Components of the RP4 conjugative transfer apparatus form an envelope structure bridging inner and outer membranes of donor cells, implications for related macromolecular transport systems. J Bacteriol 182, 1564-1574.
    • (2000) J. Bacteriol. , vol.182 , pp. 1564-1574
    • Grahn, A.1    Haase, J.2    Bamford, D.3    Lanka, E.4
  • 18
    • 0024614137 scopus 로고
    • Structure and function of conjugative pili, inducible synthesis of functional F-pili by Escherichia coli K12 containing a lac-tra operon fusion
    • Grossman, T. & Silverman, P. (1989). Structure and function of conjugative pili, inducible synthesis of functional F-pili by Escherichia coli K12 containing a lac-tra operon fusion. J Bacteriol 171, 650-656.
    • (1989) J. Bacteriol. , vol.171 , pp. 650-656
    • Grossman, T.1    Silverman, P.2
  • 19
    • 0025219619 scopus 로고
    • Structure and function of conjugative pili: Monoclonal antibodies as probes for structural variants of F-pili
    • Grossman, T., Frost, L. & Silverman, P. (1990). Structure and function of conjugative pili: monoclonal antibodies as probes for structural variants of F-pili. J Bacteriol 172, 1174-1179.
    • (1990) J. Bacteriol. , vol.172 , pp. 1174-1179
    • Grossman, T.1    Frost, L.2    Silverman, P.3
  • 20
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose pBAD promoter
    • Guzman, L.-M., Belin, D., Carson, M. & Beckwith, J. (1995). Tight regulation, modulation, and high-level expression by vectors containing the arabinose pBAD promoter. J Bacteriol 177, 4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.-M.1    Belin, D.2    Carson, M.3    Beckwith, J.4
  • 21
    • 3843054585 scopus 로고    scopus 로고
    • Tra proteins characteristic of F-like Type IV secretion systems constitute an interaction group by yeast two-hybrid analysis
    • 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.
    • (2004) J. Bacteriol. , vol.186 , pp. 5480-5485
    • Harris, R.L.1    Silverman, P.M.2
  • 22
    • 0032729789 scopus 로고    scopus 로고
    • Interaction between the F plasmid TraA (F-pilin) and TraQ proteins
    • Harris, R., Sholl, A., Conrad, M., Dresser, M. & Silverman, P. (1999). Interaction between the F plasmid TraA (F-pilin) and TraQ proteins. Mol Microbiol 34, 780-791.
    • (1999) Mol. Microbiol. , vol.34 , pp. 780-791
    • Harris, R.1    Sholl, A.2    Conrad, M.3    Dresser, M.4    Silverman, P.5
  • 23
    • 0035172604 scopus 로고    scopus 로고
    • Evidence that F-plasmid proteins TraV, TraK, and TraB assemble into an envelope-spanning structure in Escherichia coli
    • Harris, R., Hombs, V. & Silverman, P. (2001). Evidence that F-plasmid proteins TraV, TraK, and TraB assemble into an envelope-spanning structure in Escherichia coli. Mol Microbiol 42, 757-766.
    • (2001) Mol. Microbiol. , vol.42 , pp. 757-766
    • Harris, R.1    Hombs, V.2    Silverman, P.3
  • 24
    • 0002622006 scopus 로고
    • Conjugation among enteric bacteria: Mating systems dependent on expression of pili
    • Edited by M. Dworkin Washington DC: American Society for Microbiology
    • Ippen-Ihler, K. & Maneewannakul, S. (1991). Conjugation among enteric bacteria: mating systems dependent on expression of pili. In Microbial Cell-Cell Interactions, pp. 35-69. Edited by M. Dworkin. Washington, DC: American Society for Microbiology.
    • (1991) Microbial Cell-Cell Interactions , pp. 35-69
    • Ippen-Ihler, K.1    Maneewannakul, S.2
  • 25
    • 0037143720 scopus 로고    scopus 로고
    • Detergent extraction identifies different VirB protein subassemblies of the type IV secretion machinery in the membranes of Agrobacterium tumefaciens
    • Krall, L., Wiedemann, U., Unsin, G., Weiss, S., Domke, N. & Baron, C. (2002). Detergent extraction identifies different VirB protein subassemblies of the type IV secretion machinery in the membranes of Agrobacterium tumefaciens. Proc Natl Acad Sci U S A 99, 11405-11410.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 11405-11410
    • Krall, L.1    Wiedemann, U.2    Unsin, G.3    Weiss, S.4    Domke, N.5    Baron, C.6
  • 26
    • 0034059337 scopus 로고    scopus 로고
    • Subcellular localization of the Agrobacterium tumefaciens T-DNA transport pore proteins: VirB8 is essential for the assembly of the transport pore
    • Kumar, R., Xie, Y.-H. & Das, A. (2000). Subcellular localization of the Agrobacterium tumefaciens T-DNA transport pore proteins: VirB8 is essential for the assembly of the transport pore. Mol Microbiol 36, 608-617.
    • (2000) Mol. Microbiol. , vol.36 , pp. 608-617
    • Kumar, R.1    Xie, Y.-H.2    Das, A.3
  • 27
    • 0031923138 scopus 로고    scopus 로고
    • Processed VirB2 is the major subunit of the promiscuous pilus of Agrobacterium tumefaciens
    • Lai, E.-M. & Kado, C. (1998). Processed VirB2 is the major subunit of the promiscuous pilus of Agrobacterium tumefaciens. J Bacteriol 180, 2711-2717.
    • (1998) J. Bacteriol. , vol.180 , pp. 2711-2717
    • Lai, E.-M.1    Kado, C.2
  • 28
    • 0036098377 scopus 로고    scopus 로고
    • Bacterial conjugative transfer: Visualization of successful mating pairs and plasmid establishment in live Escherichia coli
    • Lawley, T., Gordon, G., Wright, A. & Taylor, D. (2002). Bacterial conjugative transfer: visualization of successful mating pairs and plasmid establishment in live Escherichia coli. Mol Microbiol 44, 947-956.
    • (2002) Mol. Microbiol. , vol.44 , pp. 947-956
    • Lawley, T.1    Gordon, G.2    Wright, A.3    Taylor, D.4
  • 29
    • 0029888601 scopus 로고    scopus 로고
    • Membrane insertion of the F-pilin subunit is Sec independent but requires leader peptidase B and the proton motive force
    • Majdalani, N. & Ippen-Ihler, K. (1996). Membrane insertion of the F-pilin subunit is Sec independent but requires leader peptidase B and the proton motive force. J Bacteriol 178, 3742-3747.
    • (1996) J. Bacteriol. , vol.178 , pp. 3742-3747
    • Majdalani, N.1    Ippen-Ihler, K.2
  • 30
    • 0029884294 scopus 로고    scopus 로고
    • Role of the propilin leader peptide in the maturation of F-pilin
    • Majdalani, N., Moore, D., Maneewannakul, S. & Ippen-Ihler, K. (1996). Role of the propilin leader peptide in the maturation of F-pilin. J Bacteriol 178, 3748-3754.
    • (1996) J. Bacteriol. , vol.178 , pp. 3748-3754
    • Majdalani, N.1    Moore, D.2    Maneewannakul, S.3    Ippen-Ihler, K.4
  • 31
    • 0036193060 scopus 로고    scopus 로고
    • Mutational analysis of F-pilin reveals domains for pilus assembly, phage infection, and DNA transfer
    • Manchak, J., Anthony, K. & Frost, L. (2002). Mutational analysis of F-pilin reveals domains for pilus assembly, phage infection, and DNA transfer. Mol Microbiol 43, 195-205.
    • (2002) Mol. Microbiol. , vol.43 , pp. 195-205
    • Manchak, J.1    Anthony, K.2    Frost, L.3
  • 33
    • 0029009405 scopus 로고
    • Characterization of traX, the F plasmid locus required for acetylation of F-pilin subunits
    • Maneewannakul, K., Maneewannakul, S. & Ippen-Ihler, K. (1995). Characterization of traX, the F plasmid locus required for acetylation of F-pilin subunits. J Bacteriol 177, 2957-2964.
    • (1995) J. Bacteriol. , vol.177 , pp. 2957-2964
    • Maneewannakul, K.1    Maneewannakul, S.2    Ippen-Ihler, K.3
  • 34
    • 0010524682 scopus 로고
    • Cell-to-cell interactions in conjugating Escherichia coli: The involvement of the cell envelope
    • Edited by M. Inouye New York: Wiley Interscience
    • Manning, P. & Achtman, M. (1979). Cell-to-cell interactions in conjugating Escherichia coli: the involvement of the cell envelope. In Bacterial Outer Membranes, pp. 409-448. Edited by M. Inouye. New York: Wiley Interscience.
    • (1979) Bacterial Outer Membranes , pp. 409-448
    • Manning, P.1    Achtman, M.2
  • 35
    • 0019435792 scopus 로고
    • Location of an F-pilin pool in the inner membrane
    • Moore, D., Sowa, B. & Ippen-Ihler, K. (1981a). Location of an F-pilin pool in the inner membrane. J Bacteriol 146, 251-259.
    • (1981) J. Bacteriol. , vol.146 , pp. 251-259
    • Moore, D.1    Sowa, B.2    Ippen-Ihler, K.3
  • 36
    • 0019807506 scopus 로고
    • The effect of tra mutations on the F-pilin polypeptide
    • Moore, D., Sowa, B. & Ippen-Ihler, K. (1981b). The effect of tra mutations on the F-pilin polypeptide. Mol Gen Genet 184, 260-264.
    • (1981) Mol. Gen. Genet. , vol.184 , pp. 260-264
    • Moore, D.1    Sowa, B.2    Ippen-Ihler, K.3
  • 37
    • 0027417285 scopus 로고
    • The Escherichia coli K-12 F plasmid gene traX is required for acetylation of F-pilin
    • Moore, D., Hamilton, C., Maneewannakul, K., Mintz, Y., Frost, L. & Ippen-Ihler, K. (1993). The Escherichia coli K-12 F plasmid gene traX is required for acetylation of F-pilin. J Bacteriol 175, 1375-1383.
    • (1993) J. Bacteriol. , vol.175 , pp. 1375-1383
    • Moore, D.1    Hamilton, C.2    Maneewannakul, K.3    Mintz, Y.4    Frost, L.5    Ippen-Ihler, K.6
  • 38
    • 0347595335 scopus 로고    scopus 로고
    • Autophagy is dispensable for intracellular replication of Legionella pneumophila in Dictyostelium discoideum
    • Otto, G., Wu, M., Clarke, M., Lu, H., Anderson, O., Hilbi, H., Shuman, H. & Kessin, R. (2004). Autophagy is dispensable for intracellular replication of Legionella pneumophila in Dictyostelium discoideum. Mol Microbiol 51, 63-72.
    • (2004) Mol. Microbiol. , vol.51 , pp. 63-72
    • Otto, G.1    Wu, M.2    Clarke, M.3    Lu, H.4    Anderson, O.5    Hilbi, H.6    Shuman, H.7    Kessin, R.8
  • 39
    • 0027097517 scopus 로고
    • Characterization of F-pilin as an inner membrane component of Escherichia coli K12
    • Paiva, W., Grossman, T. & Silverman, P. (1992). Characterization of F-pilin as an inner membrane component of Escherichia coli K12. J Biol Chem 267, 26191-26197.
    • (1992) J. Biol. Chem. , vol.267 , pp. 26191-26197
    • Paiva, W.1    Grossman, T.2    Silverman, P.3
  • 40
    • 0021821333 scopus 로고
    • DNA transfer occurs during a cell surface contact stage of F sex factor-mediated bacterial conjugation
    • Panicker, M. & Minkley, E., Jr (1985). DNA transfer occurs during a cell surface contact stage of F sex factor-mediated bacterial conjugation. J Bacteriol 162, 584-590.
    • (1985) J. Bacteriol. , vol.162 , pp. 584-590
    • Panicker, M.1    Minkley Jr., E.2
  • 41
    • 0023721293 scopus 로고
    • The physiology and biochemistry of pili
    • Paranchych, W. & Frost, L. (1988). The physiology and biochemistry of pili. Adv Microb Physiol 29, 53-114.
    • (1988) Adv. Microb. Physiol. , vol.29 , pp. 53-114
    • Paranchych, W.1    Frost, L.2
  • 42
    • 0024210147 scopus 로고
    • Antibody-selectable filamentous fd phage vectors: Affinity purification of target genes
    • Parmley, S. & Smith, G. (1988). Antibody-selectable filamentous fd phage vectors: affinity purification of target genes. Gene 73, 305-318.
    • (1988) Gene , vol.73 , pp. 305-318
    • Parmley, S.1    Smith, G.2
  • 43
    • 0034097777 scopus 로고    scopus 로고
    • Conjugative junctions in RP-4-mediated mating of Escherichia coli
    • Samuels, A., Lanka, E. & Davies, J. (2000). Conjugative junctions in RP-4-mediated mating of Escherichia coli. J Bacteriol 182, 2709-2715.
    • (2000) J. Bacteriol. , vol.182 , pp. 2709-2715
    • Samuels, A.1    Lanka, E.2    Davies, J.3
  • 44
    • 0031033180 scopus 로고    scopus 로고
    • Towards a structural biology of bacterial conjugation
    • Silverman, P. (1997). Towards a structural biology of bacterial conjugation. Mol Microbiol 23, 423-429.
    • (1997) Mol. Microbiol. , vol.23 , pp. 423-429
    • Silverman, P.1
  • 45
    • 0020657308 scopus 로고
    • Physiology of F-pilin synthesis and utilization
    • Sowa, B., Moore, D. & Ippen-Ihler, K. (1983). Physiology of F-pilin synthesis and utilization. J Bacteriol 153, 962-968.
    • (1983) J. Bacteriol. , vol.153 , pp. 962-968
    • Sowa, B.1    Moore, D.2    Ippen-Ihler, K.3
  • 46
    • 0027186527 scopus 로고
    • Subcellular localization of seven VirB proteins of Agrobacterium tumefaciens: Implications for the formation of a T-DNA transport structure
    • Thorstenson, Y., Kuldau, G. & Zambryski, P. (1993). Subcellular localization of seven VirB proteins of Agrobacterium tumefaciens: implications for the formation of a T-DNA transport structure. J Bacteriol 175, 5233-5241.
    • (1993) J. Bacteriol. , vol.175 , pp. 5233-5241
    • Thorstenson, Y.1    Kuldau, G.2    Zambryski, P.3
  • 48
    • 77049313195 scopus 로고
    • Acetylornithinase of Escherichia coli: Partial purification and some properties
    • Vogel, H. & Bonner, D. (1956). Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem 218, 97-106.
    • (1956) J. Biol. Chem. , vol.218 , pp. 97-106
    • Vogel, H.1    Bonner, D.2
  • 49
    • 0012130048 scopus 로고
    • Proteins of RNA phages
    • Edited by N.D. Zinder Cold Spring Harbor NY: Cold Spring Harbor Laboratory
    • Weber, K. & Konigsberg, W. (1975). Proteins of RNA phages. In RNA Phages, pp. 51-84. Edited by N. D. Zinder. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
    • (1975) RNA Phages , pp. 51-84
    • Weber, K.1    Konigsberg, W.2
  • 50
    • 0014748362 scopus 로고
    • Rapid bacteriophage sedimentation in the presence of polyethylene glycol and its application to large-scale virus purification
    • Yamamoto, K., Alberts, B., Benziger, R., Lawhorne, L. & Treiber, G. (1972). Rapid bacteriophage sedimentation in the presence of polyethylene glycol and its application to large-scale virus purification. Virology 40, 734-744.
    • (1972) Virology , vol.40 , pp. 734-744
    • Yamamoto, K.1    Alberts, B.2    Benziger, R.3    Lawhorne, L.4    Treiber, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.