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Volumn 84, Issue 5-6, 2002, Pages 413-421

Analysis of the Escherichia coli Tol-Pal and TonB systems by periplasmic production of Tol, TonB, colicin, or phage capsid soluble domains

Author keywords

Colicins; G3p; Protein interaction; Tol Pal; TonB; Translocation domain

Indexed keywords

BACTERIAL PROTEIN; CAPSID PROTEIN; COLICIN; EXBB PROTEIN; PROTEIN EXBD; PROTEIN G3P; PROTEIN PAL; PROTEIN TOL; PROTEIN TONB; UNCLASSIFIED DRUG; BACTERIOPHAGE FD GENE 3 PROTEIN; DNA BINDING PROTEIN; ESCHERICHIA COLI PROTEIN; EXBB PROTEIN, E COLI; EXBD PROTEIN, E COLI; MEMBRANE PROTEIN; TOLA PROTEIN, E COLI; TONB PROTEIN, BACTERIA; TONB PROTEIN, E COLI; VIRUS FUSION PROTEIN;

EID: 0036589252     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(02)01423-2     Document Type: Review
Times cited : (37)

References (45)
  • 1
    • 0031803840 scopus 로고    scopus 로고
    • TonB-dependent iron acquisition: Mechanisms of siderophore-mediated active transport
    • G.S. Moeck, J.W. Coulton, TonB-dependent iron acquisition: mechanisms of siderophore-mediated active transport, Mol. Microbiol. 28 (1998) 675-681.
    • (1998) Mol. Microbiol. , vol.28 , pp. 675-681
    • Moeck, G.S.1    Coulton, J.W.2
  • 2
    • 0033637616 scopus 로고    scopus 로고
    • Proton motive force drives the interaction of the inner membrane TolA and outer membrane pal proteins in Escherichia coli
    • E. Cascales, M. Gavioli, J.N. Sturgis, R. Lloubes, Proton motive force drives the interaction of the inner membrane TolA and outer membrane pal proteins in Escherichia coli, Mol. Microbiol. 38 (2000) 904-915.
    • (2000) Mol. Microbiol. , vol.38 , pp. 904-915
    • Cascales, E.1    Gavioli, M.2    Sturgis, J.N.3    Lloubes, R.4
  • 3
    • 0035163972 scopus 로고    scopus 로고
    • The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotA-MotB
    • E. Cascales, R. Lloubes, J.N. Sturgis, The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotA-MotB, Mol. Microbiol. 42 (2001) 795-807.
    • (2001) Mol. Microbiol. , vol.42 , pp. 795-807
    • Cascales, E.1    Lloubes, R.2    Sturgis, J.N.3
  • 4
    • 0034944420 scopus 로고    scopus 로고
    • The Tol-Pal proteins of the Escherichia coli cell envelope: An energized system required for outer membrane integrity?
    • R. Lloubès, E. Cascales, A. Walburger, E. Bouveret, C. Lazdunski, A. Bernadac, et al., The Tol-Pal proteins of the Escherichia coli cell envelope: an energized system required for outer membrane integrity? Res. Microbiol. 152 (2001) 523-529.
    • (2001) Res. Microbiol. , vol.152 , pp. 523-529
    • Lloubès, R.1    Cascales, E.2    Walburger, A.3    Bouveret, E.4    Lazdunski, C.5    Bernadac, A.6
  • 5
    • 0033744105 scopus 로고    scopus 로고
    • Colicin import into Escherichia coli cells requires the proximity of the inner and outer membranes and other factors
    • C. Lazdunski, E. Bouveret, A. Rigal, L. Journet, R. Lloubes, H. Benedetti, Colicin import into Escherichia coli cells requires the proximity of the inner and outer membranes and other factors, Int. J. Med. Microbiol. 290 (2000) 337-344.
    • (2000) Int. J. Med. Microbiol. , vol.290 , pp. 337-344
    • Lazdunski, C.1    Bouveret, E.2    Rigal, A.3    Journet, L.4    Lloubes, R.5    Benedetti, H.6
  • 7
    • 0035930345 scopus 로고    scopus 로고
    • Crystal structure of colicin E3: Implications for cell entry and ribosome inactivation
    • S. Soelaiman, K. Jakes, N. Wu, C. Li, M. Shoham, Crystal structure of colicin E3: implications for cell entry and ribosome inactivation, Mol. Cell 8 (2001) 1053-1062.
    • (2001) Mol. Cell , vol.8 , pp. 1053-1062
    • Soelaiman, S.1    Jakes, K.2    Wu, N.3    Li, C.4    Shoham, M.5
  • 8
    • 0030797114 scopus 로고    scopus 로고
    • The C-terminal domain of TolA is the coreceptor for filamentous phage infection of E. coli
    • L. Riechmann, P. Holliger, The C-terminal domain of TolA is the coreceptor for filamentous phage infection of E. coli, Cell 90 (1997) 351-360.
    • (1997) Cell , vol.90 , pp. 351-360
    • Riechmann, L.1    Holliger, P.2
  • 9
    • 0032054113 scopus 로고    scopus 로고
    • Filamentous phage structure, infection and assembly
    • D.A. Marvin, Filamentous phage structure, infection and assembly, Curr. Opin. Struct. Biol. 8 (1998) 150-158.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 150-158
    • Marvin, D.A.1
  • 10
    • 0023697146 scopus 로고
    • A hybrid toxin from bacteriophage f1 attachment protein and colicin E3 has altered cell receptor specificity
    • K.S. Jakes, N.G. Davis, N.D. Zinder, A hybrid toxin from bacteriophage f1 attachment protein and colicin E3 has altered cell receptor specificity, J. Bacteriol. 170 (1988) 4231-4238.
    • (1988) J. Bacteriol. , vol.170 , pp. 4231-4238
    • Jakes, K.S.1    Davis, N.G.2    Zinder, N.D.3
  • 12
    • 0015767227 scopus 로고
    • Resistance to colicins E3 and K induced by infection with bacteriophage f1
    • N.D. Zinder, Resistance to colicins E3 and K induced by infection with bacteriophage f1, Proc. Natl. Acad. Sci. USA 70 (1973) 3160-3164.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 3160-3164
    • Zinder, N.D.1
  • 13
    • 0015967828 scopus 로고
    • Bacteriophage f1 infection and colicin tolerance
    • H. Smilowitz, Bacteriophage f1 infection and colicin tolerance, J. Virol. 13 (1974) 100-106.
    • (1974) J. Virol. , vol.13 , pp. 100-106
    • Smilowitz, H.1
  • 14
    • 0019967083 scopus 로고
    • Effects of bacteriophage f1 gene III protein on the host cell membrane
    • J.D. Boeke, P. Model, N.D. Zinder, Effects of bacteriophage f1 gene III protein on the host cell membrane, Mol. Gen. Genet. 186 (1982) 185-192.
    • (1982) Mol. Gen. Genet. , vol.186 , pp. 185-192
    • Boeke, J.D.1    Model, P.2    Zinder, N.D.3
  • 15
    • 0027508718 scopus 로고
    • Role of the carboxyl-terminal domain of TolA in protein import and integrity of the outer membrane
    • S.K. Levengood-Freyermuth, E.M. Click, R.E. Webster, Role of the carboxyl-terminal domain of TolA in protein import and integrity of the outer membrane, J. Bacteriol. 175 (1993) 222-228.
    • (1993) J. Bacteriol. , vol.175 , pp. 222-228
    • Levengood-Freyermuth, S.K.1    Click, E.M.2    Webster, R.E.3
  • 16
    • 0032794147 scopus 로고    scopus 로고
    • Role of TolR N-terminal, central, and C-terminal domains in dimerization and interaction with TolA and tolQ
    • L. Journet, A. Rigal, C. Lazdunski, H. Bénédetti, Role of TolR N-terminal, central, and C-terminal domains in dimerization and interaction with TolA and tolQ, J. Bacteriol. 181 (1999) 4476-4484.
    • (1999) J. Bacteriol. , vol.181 , pp. 4476-4484
    • Journet, L.1    Rigal, A.2    Lazdunski, C.3    Bénédetti, H.4
  • 17
    • 0034805380 scopus 로고    scopus 로고
    • In vivo synthesis of the periplasmic domain of TonB inhibits transport through the FecA and FhuA iron siderophore transporters of Escherichia coli
    • S.P. Howard, C. Herrmann, C.W. Stratilo, V. Braun, In vivo synthesis of the periplasmic domain of TonB inhibits transport through the FecA and FhuA iron siderophore transporters of Escherichia coli, J. Bacteriol. 183 (2001) 5885-5895.
    • (2001) J. Bacteriol. , vol.183 , pp. 5885-5895
    • Howard, S.P.1    Herrmann, C.2    Stratilo, C.W.3    Braun, V.4
  • 18
    • 0026089656 scopus 로고
    • Individual domains of colicins confer specificity in colicin uptake, in pore-properties and in immunity requirement
    • H. Bénédetti, M. Frenette, D. Baty, M. Knibiehler, F. Pattus, C. Lazdunski, Individual domains of colicins confer specificity in colicin uptake, in pore-properties and in immunity requirement, J. Mol. Biol. 217 (1991) 429-439.
    • (1991) J. Mol. Biol. , vol.217 , pp. 429-439
    • Bénédetti, H.1    Frenette, M.2    Baty, D.3    Knibiehler, M.4    Pattus, F.5    Lazdunski, C.6
  • 19
    • 0025915509 scopus 로고
    • Protein import into Escherichia coli: Colicins A and E1 interact with a component of their translocation system
    • H. Bénédetti, C. Lazdunski, R. Lloubes, Protein import into Escherichia coli: colicins A and E1 interact with a component of their translocation system, EMBO J. 10 (1991) 1989-1995.
    • (1991) EMBO J. , vol.10 , pp. 1989-1995
    • Bénédetti, H.1    Lazdunski, C.2    Lloubes, R.3
  • 20
    • 0031034934 scopus 로고    scopus 로고
    • The N-terminal domain of colicin E3 interacts with TolB which is involved in the colicin translocation step
    • E. Bouveret, A. Rigal, C. Lazdunski, H. Bénédetti, The N-terminal domain of colicin E3 interacts with TolB which is involved in the colicin translocation step, Mol. Microbiol. 23 (1997) 909-920.
    • (1997) Mol. Microbiol. , vol.23 , pp. 909-920
    • Bouveret, E.1    Rigal, A.2    Lazdunski, C.3    Bénédetti, H.4
  • 21
    • 0031983893 scopus 로고    scopus 로고
    • Distinct regions of the colicin A translocation domain are involved in the interaction with TolA and TolB proteins upon import into Escherichia coli
    • E. Bouveret, A. Rigal, C. Lazdunski, H. Bénédetti, Distinct regions of the colicin A translocation domain are involved in the interaction with TolA and TolB proteins upon import into Escherichia coli, Mol. Microbiol. 27 (1998) 143-157.
    • (1998) Mol. Microbiol. , vol.27 , pp. 143-157
    • Bouveret, E.1    Rigal, A.2    Lazdunski, C.3    Bénédetti, H.4
  • 22
    • 0025049224 scopus 로고
    • Import-defective colicin B derivatives mutated in the TonB-box
    • J. Mende, V. Braun, Import-defective colicin B derivatives mutated in the TonB-box, Mol. Microbiol. 4 (1990) 1523-1533.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1523-1533
    • Mende, J.1    Braun, V.2
  • 23
    • 0032849375 scopus 로고    scopus 로고
    • Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter
    • N. Cadieux, R.J. Kadner, Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter, Proc. Natl. Acad. Sci. USA 96 (1999) 10673-10678.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10673-10678
    • Cadieux, N.1    Kadner, R.J.2
  • 24
    • 0026533769 scopus 로고
    • In vivo inhibition of TonB-dependent processes by a TonB box consensus pentapeptide
    • M. Tuckman, M.S. Osburne, In vivo inhibition of TonB-dependent processes by a TonB box consensus pentapeptide, J. Bacteriol. 174 (1992) 320-323.
    • (1992) J. Bacteriol. , vol.174 , pp. 320-323
    • Tuckman, M.1    Osburne, M.S.2
  • 25
    • 77951352546 scopus 로고
    • Sur la biosynthèse d'une colicine et sur son mode d'action
    • F. Jacob, L. Siminovitch, L. Wollman, Sur la biosynthèse d'une colicine et sur son mode d'action. Ann. Inst. Pasteur. 83 (1952) 295-315.
    • (1952) Ann. Inst. Pasteur. , vol.83 , pp. 295-315
    • Jacob, F.1    Siminovitch, L.2    Wollman, L.3
  • 27
    • 0034767924 scopus 로고    scopus 로고
    • Import of colicins across the outer membrane of Escherichia coli involves multiple protein interactions in the periplasm
    • L. Journet, E. Bouveret, A. Rigal, R. Lloubes, C. Lazdunski, H. Bénédetti, Import of colicins across the outer membrane of Escherichia coli involves multiple protein interactions in the periplasm, Mol. Microbiol. 41 (2001) 331-344.
    • (2001) Mol. Microbiol. , vol.42 , pp. 331-344
    • Journet, L.1    Bouveret, E.2    Rigal, A.3    Lloubes, R.4    Lazdunski, C.5    Bénédetti, H.6
  • 29
    • 0036093944 scopus 로고    scopus 로고
    • The Tol/Pal system function requires an interaction between the C-terminal domain of TolA and the N-terminal domain of TolB
    • A. Walburger, C. Lazdunski, Y. Corda, The Tol/Pal system function requires an interaction between the C-terminal domain of TolA and the N-terminal domain of TolB, Mol. Microbiol. (2002) 695-708.
    • (2002) Mol. Microbiol. , pp. 695-708
    • Walburger, A.1    Lazdunski, C.2    Corda, Y.3
  • 30
    • 0031799096 scopus 로고    scopus 로고
    • Discovery of critical Tol A-binding residues in the bactericidal toxin colicin N: A biophysical approach
    • E.M. Raggett, G. Brainbridge, L.J. Evans, A. Cooper, J.H. Lakey, Discovery of critical Tol A-binding residues in the bactericidal toxin colicin N: a biophysical approach, Mol. Microbiol. 28 (1998) 1335-1343.
    • (1998) Mol. Microbiol. , vol.28 , pp. 1335-1343
    • Raggett, E.M.1    Brainbridge, G.2    Evans, L.J.3    Cooper, A.4    Lakey, J.H.5
  • 31
    • 0037176873 scopus 로고    scopus 로고
    • Macromolecular import into Escherichia coli: The TolA C-terminal domain changes conformation when interacting with the colicin A toxin
    • C. Deprez, L. Blanchard, F. Guerlesquin, M. Gavioli, J.P. Simorre, C. Lazdunski, et al., Macromolecular import into Escherichia coli: the TolA C-terminal domain changes conformation when interacting with the colicin A toxin, Biochemistry 41 (2002) 2589-2598.
    • (2002) Biochemistry , vol.41 , pp. 2589-2598
    • Deprez, C.1    Blanchard, L.2    Guerlesquin, F.3    Gavioli, M.4    Simorre, J.P.5    Lazdunski, C.6
  • 32
    • 0034650563 scopus 로고    scopus 로고
    • The structure of TolB, an essential component of the tol-dependent translocation system, and its protein-protein interaction with the translocation domain of colicin E9
    • S. Carr, C.N. Penfold, V. Bamford, R. James, A.M. Hemmings, The structure of TolB, an essential component of the tol-dependent translocation system, and its protein-protein interaction with the translocation domain of colicin E9, Struct. Fold Des. 8 (2000) 57-66.
    • (2000) Struct. Fold Des. , vol.8 , pp. 57-66
    • Carr, S.1    Penfold, C.N.2    Bamford, V.3    James, R.4    Hemmings, A.M.5
  • 33
    • 0025273561 scopus 로고
    • Dissection of functional domains in phage fd adsorption protein. Discrimination between attachment and penetration sites
    • I. Stengele, P. Bross, X. Garces, J. Giray, I. Rasched, Dissection of functional domains in phage fd adsorption protein. Discrimination between attachment and penetration sites, J. Mol. Biol. 212 (1990) 143-149.
    • (1990) J. Mol. Biol. , vol.212 , pp. 143-149
    • Stengele, I.1    Bross, P.2    Garces, X.3    Giray, J.4    Rasched, I.5
  • 34
    • 0000046526 scopus 로고    scopus 로고
    • Filamentous phage infection: Crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA
    • J. Lubkowski, F. Hennecke, A. Pluckthun, A. Wlodawer, Filamentous phage infection: crystal structure of g3p in complex with its coreceptor, the C-terminal domain of TolA, Struct. Fold Des. 7 (1999) 711-722.
    • (1999) Struct. Fold Des. , vol.7 , pp. 711-722
    • Lubkowski, J.1    Hennecke, F.2    Pluckthun, A.3    Wlodawer, A.4
  • 36
    • 0031663159 scopus 로고    scopus 로고
    • Gram-negative bacteria produce membrane vesicles which are capable of killing other bacteria
    • Z. Li, A.J. Clarke, T.J. Beveridge, Gram-negative bacteria produce membrane vesicles which are capable of killing other bacteria, J. Bacteriol. 180 (1998) 5478-5483.
    • (1998) J. Bacteriol. , vol.180 , pp. 5478-5483
    • Li, Z.1    Clarke, A.J.2    Beveridge, T.J.3
  • 40
    • 0033744772 scopus 로고    scopus 로고
    • Surface expression of O-specific lipopolysaccharide in Escherichia coli requires the function of the TolA protein
    • J.A. Gaspar, J.A. Thomas, C.L. Marolda, M.A. Valvano, Surface expression of O-specific lipopolysaccharide in Escherichia coli requires the function of the TolA protein, Mol. Microbiol. 38 (2000) 262-275.
    • (2000) Mol. Microbiol. , vol.38 , pp. 262-275
    • Gaspar, J.A.1    Thomas, J.A.2    Marolda, C.L.3    Valvano, M.A.4
  • 41
    • 0033569296 scopus 로고    scopus 로고
    • Structure of the Escherichia coli TolB protein determined by MAD methods at 1.95 Å resolution
    • C. Abergel, E. Bouveret, J.M. Claverie, K. Brown, A. Rigal, C. Lazdunski, et al., Structure of the Escherichia coli TolB protein determined by MAD methods at 1.95 Å resolution, Struct. Fold Des. 7 (1999) 1291-1300.
    • (1999) Struct. Fold Des. , vol.7 , pp. 1291-1300
    • Abergel, C.1    Bouveret, E.2    Claverie, J.M.3    Brown, K.4    Rigal, A.5    Lazdunski, C.6
  • 42
    • 0035920228 scopus 로고    scopus 로고
    • Crystal structure of the dimeric C-terminal domain of TonB reveals a novel fold
    • C. Chang, A. Mooser, A. Pluckthun, A. Wlodawer, Crystal structure of the dimeric C-terminal domain of TonB reveals a novel fold, J. Biol. Chem. 276 (2001) 27535-27540.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27535-27540
    • Chang, C.1    Mooser, A.2    Pluckthun, A.3    Wlodawer, A.4
  • 43
    • 0035155704 scopus 로고    scopus 로고
    • Organisation and evolution of the tol-pal gene cluster
    • J.N. Sturgis, Organisation and evolution of the tol-pal gene cluster, J. Mol. Microbiol. Biotechnol. 3 (2001) 113-122.
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 113-122
    • Sturgis, J.N.1
  • 44
    • 0030010928 scopus 로고    scopus 로고
    • The conserved 18,000-molecular-weight outer membrane protein on Haemophilus ducreyi has homology to PAL
    • S.M. Spinola, T.J. Hiltke, K. Fortney, K.L. Shanks, The conserved 18,000-molecular-weight outer membrane protein on Haemophilus ducreyi has homology to PAL, Infect. Immun. 64 (1996) 1950-1955.
    • (1996) Infect. Immun. , vol.64 , pp. 1950-1955
    • Spinola, S.M.1    Hiltke, T.J.2    Fortney, K.3    Shanks, K.L.4
  • 45
    • 0030473418 scopus 로고    scopus 로고
    • Identification and characterization of the tolQRA genes of Pseudomonas aeruginosa
    • J.J. Dennis, E.R. Lafontaine, P.A. Sokol, Identification and characterization of the tolQRA genes of Pseudomonas aeruginosa, J. Bacteriol. 178 (1996) 7059-7068.
    • (1996) J. Bacteriol. , vol.178 , pp. 7059-7068
    • Dennis, J.J.1    Lafontaine, E.R.2    Sokol, P.A.3


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