메뉴 건너뛰기




Volumn 4, Issue 2, 2003, Pages 105-116

Acquisition of siderophores in gram-negative bacteria

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; IRON; IRON DERIVATIVE; PROTEIN; RECEPTOR; SIDEROPHORE;

EID: 0037317173     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1015     Document Type: Review
Times cited : (307)

References (100)
  • 1
    • 0033759220 scopus 로고    scopus 로고
    • Iron metabolism in pathogenic bacteria
    • Ratledge, C. & Dover L. G. Iron metabolism in pathogenic bacteria Annu. Rev. Microbiol 54, 881-941 (2000).
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 881-941
    • Ratledge, C.1    Dover, L.G.2
  • 3
    • 0032946645 scopus 로고    scopus 로고
    • Bacterial solutions to the iron-supply problem
    • Braun, V. & Killmann, H. Bacterial solutions to the iron- supply problem. Trends Biochem. Sci. 24, 104-109 (1999).
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 104-109
    • Braun, V.1    Killmann, H.2
  • 4
    • 0035352440 scopus 로고    scopus 로고
    • Structural biology of bacterial iron uptake systems
    • Clarke, T. E., Tan, L. W. & Vogel, H. J. Structural biology of bacterial iron uptake systems. Curr. Top. Med. Chem. 1, 7-30 (2001).
    • (2001) Curr. Top. Med. Chem. , vol.1 , pp. 7-30
    • Clarke, T.E.1    Tan, L.W.2    Vogel, H.J.3
  • 5
    • 0025572764 scopus 로고
    • 12 transport in Eschericha coli: Energy coupling between membranes
    • 12 transport in Eschericha coli: energy coupling between membranes. Mol. Microbiol. 4, 2027-2033 (1990). This review, together with references 6 and 11-14, illustrates the evolution of the field of TonB-dependent transport during the past decade. It describes the various permeation mechanisms that were proposed before the determination of the structure of the outer-membrane receptors.
    • (1990) Mol. Microbiol. , vol.4 , pp. 2027-2033
    • Kadner, R.J.1
  • 6
    • 0025666854 scopus 로고
    • TonB and the Gram-negative dilemma
    • Postle, K. TonB and the Gram-negative dilemma. Mol. Microbiol. 4, 2019-2025 (1990).
    • (1990) Mol. Microbiol. , vol.4 , pp. 2019-2025
    • Postle, K.1
  • 8
    • 0032839616 scopus 로고    scopus 로고
    • Structures of Gram-negative cell walls and their derived membrane vesicles
    • Beveridge, T. J. Structures of Gram-negative cell walls and their derived membrane vesicles. J Bacteriol. 181, 4725-4733 (1999).
    • (1999) J Bacteriol. , vol.181 , pp. 4725-4733
    • Beveridge, T.J.1
  • 9
    • 0033942874 scopus 로고    scopus 로고
    • Structure and function of bacterial outer membrane proteins: Barrels in a nutshell
    • Koebnik, R., Locher, K. P. & van Gelder, P. Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Mol. Microbiol. 37, 239-253 (2000).
    • (2000) Mol. Microbiol. , vol.37 , pp. 239-253
    • Koebnik, R.1    Locher, K.P.2    Van Gelder, P.3
  • 10
    • 0027280517 scopus 로고
    • The proton motive force drives the outer membrane transport of cobalamin in Escherichia coli
    • Bradbeer, C. The proton motive force drives the outer membrane transport of cobalamin in Escherichia coli. J. Bacteriol. 175, 3146-3150 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 3146-3150
    • Bradbeer, C.1
  • 11
    • 0027752437 scopus 로고
    • TonB protein and energy transduction between membranes
    • Postle, K. TonB protein and energy transduction between membranes. J. Bioenerg. Biomembr. 25, 591-601 (1993).
    • (1993) J. Bioenerg. Biomembr. , vol.25 , pp. 591-601
    • Postle, K.1
  • 12
    • 0027729136 scopus 로고
    • Mechanisms of TonB-catalyzed iron transport through the enteric bacterial cell envelope
    • Klebba, P. E., Rutz, J. M., Liu, J. & Murphy, C. K. Mechanisms of TonB-catalyzed iron transport through the enteric bacterial cell envelope. J. Bioenerg. Biomembr. 25, 603-611 (1993).
    • (1993) J. Bioenerg. Biomembr. , vol.25 , pp. 603-611
    • Klebba, P.E.1    Rutz, J.M.2    Liu, J.3    Murphy, C.K.4
  • 13
    • 0029155042 scopus 로고
    • Energy-coupled transport and signal transduction through the Gram-negative outer membrane via TonB-ExbB-ExbD-dependent receptor proteins
    • Braun, V. Energy-coupled transport and signal transduction through the Gram-negative outer membrane via TonB-ExbB-ExbD-dependent receptor proteins. FEMS Microbiol. Rev. 16, 295-307 (1995).
    • (1995) FEMS Microbiol. Rev. , vol.16 , pp. 295-307
    • Braun, V.1
  • 14
    • 0031803840 scopus 로고    scopus 로고
    • TonB-dependent iron acquisition: Mechanisms of siderophore-mediated active transport
    • Moeck, G. & Coulton, J. W. TonB-dependent iron acquisition: mechanisms of siderophore-mediated active transport. Mol. Microbiol. 28, 675-681 (1998)
    • (1998) Mol. Microbiol. , vol.28 , pp. 675-681
    • Moeck, G.1    Coulton, J.W.2
  • 15
    • 0033178531 scopus 로고    scopus 로고
    • β-barrel proteins from bacterial outer membranes: Structure, function and refolding
    • Buchanan, S. K. β-Barrel proteins from bacterial outer membranes: structure, function and refolding. Curr. Opin. Struct. Biol. 9, 455-461 (1999).
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 455-461
    • Buchanan, S.K.1
  • 16
    • 0033932639 scopus 로고    scopus 로고
    • β-barrel membrane proteins
    • Schulz, G. E. β-barrel membrane proteins. Curr. Opin. Struct. Biol. 10, 443-447 (2000).
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 443-447
    • Schulz, G.E.1
  • 17
    • 0036511438 scopus 로고    scopus 로고
    • Close before opening
    • Postle, K. Close before opening. Science 295, 1658-1659 (2002).
    • (2002) Science , vol.295 , pp. 1658-1659
    • Postle, K.1
  • 18
    • 0026779245 scopus 로고
    • Crystal structures explain functional properties of two E. coli porins
    • Cowan, S. W. et al. Crystal structures explain functional properties of two E. coli porins. Nature 358, 727-733 (1992).
    • (1992) Nature , vol.358 , pp. 727-733
    • Cowan, S.W.1
  • 19
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1Å resolution
    • Schirmer, T. Keller, T. A., Wang, Y. F. & Rosenbusch, J. P. Structural basis for sugar translocation through maltoporin channels at 3.1Å resolution. Science 267, 512-514 (1995).
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.F.3    Rosenbusch, J.P.4
  • 20
    • 0032034801 scopus 로고    scopus 로고
    • Mechanisms of solute transport through the outer membrane proteins: Burning down the house
    • Klebba, P. E. & Newton, S. M. C. Mechanisms of solute transport through the outer membrane proteins: burning down the house. Curr. Biol. 1, 238-248 (1998).
    • (1998) Curr. Biol. , vol.1 , pp. 238-248
    • Klebba, P.E.1    Newton, S.M.C.2
  • 21
    • 0031857538 scopus 로고    scopus 로고
    • General and specific porins from bacterial outer membranes
    • Schirmer, T. General and specific porins from bacterial outer membranes J. Struct. Biol. 121, 101-109 (1998).
    • (1998) J. Struct. Biol. , vol.121 , pp. 101-109
    • Schirmer, T.1
  • 22
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysacchadde
    • Ferguson, A. D., Hofmann, E., Coulton, J. W., Diederichs, K. & Welte, W. Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysacchadde. Science 282, 2215-2220 (1998).
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 23
    • 0032414254 scopus 로고    scopus 로고
    • Transmembrane signalling across the ligand-gated FhuA receptor: Crystal structures of free and ferrichrome-bound states reveal allosteric changes
    • Lecher, K. P. et al. Transmembrane signalling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes. Cell 95, 771-778 (1998). References 22 and 23 reported simultaneously the atomic structures of the ferrichrome receptor and transporter FhuA in the ligand-free and -bound states, revealing for the first time the existence of an additional protein domain that blocked the permeation pathway, and showing its role in signalling.
    • (1998) Cell , vol.95 , pp. 771-778
    • Lecher, K.P.1
  • 24
    • 0032900438 scopus 로고    scopus 로고
    • Crystal structure of the outer membrane active transporter FepA from Escherichia coli
    • Buchanan, S. K. et al. Crystal structure of the outer membrane active transporter FepA from Escherichia coli. Nature Struct. Biol. 6, 56-63 (1999). This paper reported the atomic structure of the enterobactin receptor and transporter FepA, verifying the common protein architecture of TonB-dependent receptors.
    • (1999) Nature Struct. Biol. , vol.6 , pp. 56-63
    • Buchanan, S.K.1
  • 25
    • 0036500658 scopus 로고    scopus 로고
    • Structural basis of gating by the outer membrane transporter FecA
    • Ferguson, A. D. et al. Structural basis of gating by the outer membrane transporter FecA Science 295, 1715-1719 (2002). This paper reported the atomic structure of FecA in the ligand-free and -bound states, revealing allosteric changes in the extracellular domain that seem to correspond to a gating mechanism, in addition to changes that involved the plug domain as reported previously.
    • (2002) Science , vol.295 , pp. 1715-1719
    • Ferguson, A.D.1
  • 26
    • 0035918333 scopus 로고    scopus 로고
    • Exchangeability of N-termini in the ligandgated porins of Escherichia coli
    • Scott, D. C. et al. Exchangeability of N-termini in the ligandgated porins of Escherichia coli. J. Biol. Chem. 276, 13025-13033 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 13025-13033
    • Scott, D.C.1
  • 27
    • 0030680156 scopus 로고    scopus 로고
    • Cell envelope signalling in Escherichia coli: Ligand binding to the ferrichrome-iron receptor FhuA promotes interaction with the energy-transducing protein TonB
    • Moeck, G., Coulton, J. W. & Postle, K. Cell envelope signalling in Escherichia coli: ligand binding to the ferrichrome-iron receptor FhuA promotes interaction with the energy-transducing protein TonB. J. Biol. Chem. 272, 28391-28397 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 28391-28397
    • Moeck, G.1    Coulton, J.W.2    Postle, K.3
  • 28
    • 0032545215 scopus 로고    scopus 로고
    • Pumping iron through cell membranes
    • Braun, V. Pumping iron through cell membranes. Science 282, 2202-2203 (1998).
    • (1998) Science , vol.282 , pp. 2202-2203
    • Braun, V.1
  • 29
    • 0026533769 scopus 로고
    • In vivo inhibition of TonB-dependent processes by a TonB box consensus pentapeptide
    • Tuckman, M. & Osburne, M. S. In vivo inhibition of TonB-dependent processes by a TonB box consensus pentapeptide. J. Bacteriol. 174, 320-323 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 320-323
    • Tuckman, M.1    Osburne, M.S.2
  • 30
    • 0029836552 scopus 로고    scopus 로고
    • Ligand-induced conformational change in the ferrichrome-iron receptor of Escherichia coli
    • Moeck, G. et al. Ligand-induced conformational change in the ferrichrome-iron receptor of Escherichia coli. Mol. Microbiol. 22, 459-471 (1996).
    • (1996) Mol. Microbiol. , vol.22 , pp. 459-471
    • Moeck, G.1
  • 31
    • 0030911410 scopus 로고    scopus 로고
    • Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions
    • Larsen, R. A., Foster-Hartnett, D., McIntosh, M. A. & Postle, K. Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions. J. Bacteriol. 179, 3213-3221 (1997).
    • (1997) J. Bacteriol. , vol.179 , pp. 3213-3221
    • Larsen, R.A.1    Foster-Hartnett, D.2    McIntosh, M.A.3    Postle, K.4
  • 32
    • 0033764762 scopus 로고    scopus 로고
    • Sequence changes in the TonB box region of BtuB affect its transport activities and interaction with TonB protein
    • Cadieux, N., Bradbeer, C. & Kadner, R. J. Sequence changes in the TonB box region of BtuB affect its transport activities and interaction with TonB protein. J. Bacteriol. 182, 5954-5961 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 5954-5961
    • Cadieux, N.1    Bradbeer, C.2    Kadner, R.J.3
  • 33
    • 0034888050 scopus 로고    scopus 로고
    • Mutations in Escherichia coli receptor FepA reveal residues involved in ligand binding and transport
    • Barnard, T. J., Watson, M. E. & McIntosh, M. A. Mutations in Escherichia coli receptor FepA reveal residues involved in ligand binding and transport. Mol. Microbiol. 41, 527-536 (2001).
    • (2001) Mol. Microbiol. , vol.41 , pp. 527-536
    • Barnard, T.J.1    Watson, M.E.2    McIntosh, M.A.3
  • 34
    • 0034093293 scopus 로고    scopus 로고
    • Substrate-induced exposure of an energy-coupling motif of a membrane transporter
    • Merianos, H. J., Cadieux, N., Lin, C. H., Kadner, R. J. & Cafiso, D S. Substrate-induced exposure of an energy-coupling motif of a membrane transporter. Nature Struct. Biol. 7, 205-209 (2000).
    • (2000) Nature Struct. Biol. , vol.7 , pp. 205-209
    • Merianos, H.J.1    Cadieux, N.2    Lin, C.H.3    Kadner, R.J.4    Cafiso, D.S.5
  • 35
    • 0035923423 scopus 로고    scopus 로고
    • Transport-defective mutations alter the conformation of the energy-coupling motif of an outer membrane transporter
    • Coggshall, K. A., Cadieux, N., Piedmont, C., Kadner, R. J. & Cafiso, D. S. Transport-defective mutations alter the conformation of the energy-coupling motif of an outer membrane transporter. Biochemistry 40, 13964-13971 (2001).
    • (2001) Biochemistry , vol.40 , pp. 13964-13971
    • Coggshall, K.A.1    Cadieux, N.2    Piedmont, C.3    Kadner, R.J.4    Cafiso, D.S.5
  • 36
    • 4244198532 scopus 로고    scopus 로고
    • Expression, purification, characterization and crystallization of the E. coli outer membrane cyanocobalamin transporter BtuB
    • Chimento, D. P., Mohanty, A. K., Kadner, R. J. & Wiener, M. C. Expression, purification, characterization and crystallization of the E. coli outer membrane cyanocobalamin transporter BtuB. Biophys. J. 82, 2754A (2002).
    • (2002) Biophys. J. , vol.82
    • Chimento, D.P.1    Mohanty, A.K.2    Kadner, R.J.3    Wiener, M.C.4
  • 37
    • 4244197324 scopus 로고    scopus 로고
    • The crystal structure of the E. coli outer membrane cyanocobalamin transporter BtuB
    • Wiener, M. C., Chimento, D. P., Mohanty, A. K. & Kadner, R. J. The crystal structure of the E. coli outer membrane cyanocobalamin transporter BtuB. Biophys. J. 82, 2514A (2002).
    • (2002) Biophys. J. , vol.82
    • Wiener, M.C.1    Chimento, D.P.2    Mohanty, A.K.3    Kadner, R.J.4
  • 38
    • 0032831642 scopus 로고    scopus 로고
    • The β-barrel domain of FhuAΔ5-160 is sufficient for TonB-dependent activities of Escherichia coli
    • Braun, M., Killman, H. & Braun, V. The β-barrel domain of FhuAΔ5-160 is sufficient for TonB-dependent activities of Escherichia coli. Mol. Microbiol. 33, 1037-1049 (1999). This paper, together with references 26 and 40, is concerned with the activity of receptors that either lack the plug domain or contain a non-native homologue, which illustrates the current debate about the functional relevance of this domain.
    • (1999) Mol. Microbiol. , vol.33 , pp. 1037-1049
    • Braun, M.1    Killman, H.2    Braun, V.3
  • 39
    • 0035957063 scopus 로고    scopus 로고
    • Stability studies of FhuA, a two-domain outer membrane protein from Escherichia coli
    • Bonhivers, M. et al. Stability studies of FhuA, a two-domain outer membrane protein from Escherichia coli. Biochemistry 40, 2606-2613 (2001).
    • (2001) Biochemistry , vol.40 , pp. 2606-2613
    • Bonhivers, M.1
  • 40
    • 0036778139 scopus 로고    scopus 로고
    • FepA with globular domain deletions lacks activity
    • Vakharia, H. & Postle, K. FepA with globular domain deletions lacks activity. J. Bacteriol. 184, 5508-5512 (2002).
    • (2002) J. Bacteriol. , vol.184 , pp. 5508-5512
    • Vakharia, H.1    Postle, K.2
  • 41
    • 0028051476 scopus 로고
    • A site-directed spin-labeling study of ligand-induced conformational change in the ferric enterobactin receptor, FepA
    • Liu, J., Rutz, J. M., Klebba, P. E. & Feix, J. B. A site-directed spin-labeling study of ligand-induced conformational change in the ferric enterobactin receptor, FepA. Biochemistry 33, 13274-13283 (1994).
    • (1994) Biochemistry , vol.33 , pp. 13274-13283
    • Liu, J.1    Rutz, J.M.2    Klebba, P.E.3    Feix, J.B.4
  • 42
    • 0030926805 scopus 로고    scopus 로고
    • Ligand-specific opening of a gated-porin channel in the outer membrane of living bacteria
    • Jiang, X. Q. et al. Ligand-specific opening of a gated-porin channel in the outer membrane of living bacteria. Science 276, 1261-1264 (1997).
    • (1997) Science , vol.276 , pp. 1261-1264
    • Jiang, X.Q.1
  • 43
    • 0031888244 scopus 로고    scopus 로고
    • Specific in vivo labeling of cell surface-exposed protein loops: Reactive cysteines in the predicted gating loop mark a ferrichrome binding site and a ligand-induced conformational change of the Escherichia coli FhuA protein
    • Bös, C., Lorenzen, D. & Braun, V. Specific in vivo labeling of cell surface-exposed protein loops: reactive cysteines in the predicted gating loop mark a ferrichrome binding site and a ligand-induced conformational change of the Escherichia coli FhuA protein. J. Bacteriol. 180, 605-613 (1998).
    • (1998) J. Bacteriol. , vol.180 , pp. 605-613
    • Bös, C.1    Lorenzen, D.2    Braun, V.3
  • 44
    • 0032560604 scopus 로고    scopus 로고
    • Ligand-induced conformational change in the ferric enterobactin receptor FepA as studied by site-directed spin labeling and time-domain ESR
    • Klug, C. S., Eaton, S. S., Eaton, G. R. & Feix, J. B. Ligand-induced conformational change in the ferric enterobactin receptor FepA as studied by site-directed spin labeling and time-domain ESR. Biochemistry 37, 9016-9023 (1998).
    • (1998) Biochemistry , vol.37 , pp. 9016-9023
    • Klug, C.S.1    Eaton, S.S.2    Eaton, G.R.3    Feix, J.B.4
  • 46
    • 0037671392 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the bacterial outer membrane protein FhuA: A study of the ferrichrome-free and bound states
    • in the press
    • Faraldo-Gómez, J. D., Smith, G. R. & Sansom, M. S. P. Molecular dynamics simulations of the bacterial outer membrane protein FhuA: a study of the ferrichrome-free and bound states Biophys. J. (in the press).
    • Biophys. J.
    • Faraldo-Gómez, J.D.1    Smith, G.R.2    Sansom, M.S.P.3
  • 47
    • 0025048105 scopus 로고
    • Molecular dynamics simulations in biology
    • Karplus, M. & Petsko, G. A. Molecular dynamics simulations in biology. Nature 347, 631-639 (1990).
    • (1990) Nature , vol.347 , pp. 631-639
    • Karplus, M.1    Petsko, G.A.2
  • 49
    • 0036725277 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • Karplus, M. & McCammon, J. A. Molecular dynamics simulations of biomolecules. Nature Struct. Biol. 9, 646-652 (2002).
    • (2002) Nature Struct. Biol. , vol.9 , pp. 646-652
    • Karplus, M.1    McCammon, J.A.2
  • 50
    • 0033660186 scopus 로고    scopus 로고
    • The pyoverdin receptor FpvA, a TonB-dependent receptor involved in iron uptake by Pseudomonas aeruginosa
    • Folschweiller, N. et al. The pyoverdin receptor FpvA, a TonB-dependent receptor involved in iron uptake by Pseudomonas aeruginosa. Mol. Membr. Biol. 17, 123-133 (2000).
    • (2000) Mol. Membr. Biol. , vol.17 , pp. 123-133
    • Folschweiller, N.1
  • 51
    • 0033587572 scopus 로고    scopus 로고
    • Copurification of the FpvA ferric pyoverdin receptor of Pseudomonas aeruginosa with its iron-free ligand: Implications for siderophore-mediated iron transport
    • Schalk, I. J. et al. Copurification of the FpvA ferric pyoverdin receptor of Pseudomonas aeruginosa with its iron-free ligand: implications for siderophore-mediated iron transport. Biochemistry 38, 9357-9365 (1999).
    • (1999) Biochemistry , vol.38 , pp. 9357-9365
    • Schalk, I.J.1
  • 52
    • 0035151056 scopus 로고    scopus 로고
    • Iron-free pyoverdin binds to its outer membrane receptor FpvA in Pseudomonas aeruginosa: A new mechanism for membrane iron transport
    • Schalk, I. J. et al. Iron-free pyoverdin binds to its outer membrane receptor FpvA in Pseudomonas aeruginosa: a new mechanism for membrane iron transport. Mol. Microbiol. 39, 351-360 (2001).
    • (2001) Mol. Microbiol. , vol.39 , pp. 351-360
    • Schalk, I.J.1
  • 53
    • 0037022174 scopus 로고    scopus 로고
    • Recycling of pyoverdin on the FpvA receptor after ferric pyoverdin uptake and dissociation in Pseudomonas aeruginosa
    • Schalk, I. J., Abdallah, M. A. & Pattus, F. Recycling of pyoverdin on the FpvA receptor after ferric pyoverdin uptake and dissociation in Pseudomonas aeruginosa. Biochemistry 41, 1663-1671 (2002). In the studies reported in references 51-53, FRET and radiolabelling techniques were used to characterize the association of the receptor FpvA with the siderophore pyoverdin, as well as to monitor its uptake and recycling into the medium.
    • (2002) Biochemistry , vol.41 , pp. 1663-1671
    • Schalk, I.J.1    Abdallah, M.A.2    Pattus, F.3
  • 54
    • 0034718606 scopus 로고    scopus 로고
    • Microbial iron-transport via a siderophore shuttle: A membrane ion transport paradigm
    • Stintzi, A., Barnes, C., Jide, X. & Raymond, K. N. Microbial iron-transport via a siderophore shuttle: a membrane ion transport paradigm. Proc. Natl Acad Sci. USA 97, 10691-10696 (2000).
    • (2000) Proc. Natl Acad Sci. USA , vol.97 , pp. 10691-10696
    • Stintzi, A.1    Barnes, C.2    Jide, X.3    Raymond, K.N.4
  • 55
    • 0030861787 scopus 로고    scopus 로고
    • Avoidance of iron toxicity through regulation of bacterial iron transport
    • Braun, V. Avoidance of iron toxicity through regulation of bacterial iron transport. Biol. Chem. 378, 779-786 (1997).
    • (1997) Biol. Chem. , vol.378 , pp. 779-786
    • Braun, V.1
  • 56
    • 0344172832 scopus 로고    scopus 로고
    • Opening the iron box: Transcriptional metalloregulation by the Fur protein
    • Escolar, L., Pérez-Martín, J. & de Lorenzo, V. Opening the iron box: transcriptional metalloregulation by the Fur protein, J. Bacteriol. 181, 6223-6229 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 6223-6229
    • Escolar, L.1    Pérez-Martín, J.2    De Lorenzo, V.3
  • 57
    • 0030925485 scopus 로고    scopus 로고
    • Surface signalling: Novel transcription initiation mechanism starting from the cell surface
    • Braun, V. Surface signalling: novel transcription initiation mechanism starting from the cell surface. Arch. Microbiol. 167 (1997). This review and reference 59 describe the process whereby the transcription of the Fec uptake system is regulated by the presence of ferric citrate at the level of the cell surface.
    • (1997) Arch. Microbiol. , vol.167
    • Braun, V.1
  • 58
    • 0031811067 scopus 로고    scopus 로고
    • Iron regulates transcription of the Escherichia coli ferric citrate transport genes directly and through the transcription initiation proteins
    • Angerer, A. & Braun, V. Iron regulates transcription of the Escherichia coli ferric citrate transport genes directly and through the transcription initiation proteins. Arch. Microbiol. 189, 483-490 (1998).
    • (1998) Arch. Microbiol. , vol.189 , pp. 483-490
    • Angerer, A.1    Braun, V.2
  • 59
    • 0033954445 scopus 로고    scopus 로고
    • Surface signaling in ferric citrate transport gene induction: Interaction of the FecA, FecR and Fed regulatory proteins
    • Enz, S, Mahren, S., Stroeher, U. W. & Braun, V. Surface signaling in ferric citrate transport gene induction: interaction of the FecA, FecR and Fed regulatory proteins. J Bacteriol. 182, 637-646 (2000).
    • (2000) J Bacteriol. , vol.182 , pp. 637-646
    • Enz, S.1    Mahren, S.2    Stroeher, U.W.3    Braun, V.4
  • 60
    • 0035180675 scopus 로고    scopus 로고
    • Control of the ferric citrate transport system of Escherichia coli: Mutations in region 2.1 of the Fecl extracytoplasmic-function sigma factor suppress mutations in the FecR transmembrane regulatory protein
    • Stiefel, A. et al. Control of the ferric citrate transport system of Escherichia coli: mutations in region 2.1 of the Fecl extracytoplasmic-function sigma factor suppress mutations in the FecR transmembrane regulatory protein. J. Bacteriol. 183, 162-170 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 162-170
    • Stiefel, A.1
  • 61
    • 0031035649 scopus 로고    scopus 로고
    • Transcription induction of the ferric citrate transport genes via the N-terminus of the FecA outer membrane protein, the Ton system and the electrochemical potential of the cytoplasmic membrane
    • Kim, I., Stiefel, A., Plantör, A., Angerer, A. & Braun, V. Transcription induction of the ferric citrate transport genes via the N-terminus of the FecA outer membrane protein, the Ton system and the electrochemical potential of the cytoplasmic membrane. Mol. Microbiol. 23, 333-344 (1997).
    • (1997) Mol. Microbiol. , vol.23 , pp. 333-344
    • Kim, I.1    Stiefel, A.2    Plantör, A.3    Angerer, A.4    Braun, V.5
  • 62
    • 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
    • Howard, S. P., Hemmann, C., Stratilo, C. W. & Braun, V. 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, 5885-5895 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 5885-5895
    • Howard, S.P.1    Hemmann, C.2    Stratilo, C.W.3    Braun, V.4
  • 63
    • 0015217637 scopus 로고
    • An additional step in the transport of iron defined by the tonb locus of Escherichia coli
    • Wang, C. & Newton, A. An additional step in the transport of iron defined by the tonb locus of Escherichia coli. J. Biol. Chem. 246, 2147-2151 (1971).
    • (1971) J. Biol. Chem. , vol.246 , pp. 2147-2151
    • Wang, C.1    Newton, A.2
  • 64
    • 0019230249 scopus 로고
    • 12 in Escherichia coli. Some observations on the roles of the gene products of btuc and tonb
    • 12 in Escherichia coli. Some observations on the roles of the gene products of btuc and tonb. J. Biol. Chem. 255, 4313-4319 (1980).
    • (1980) J. Biol. Chem. , vol.255 , pp. 4313-4319
    • Reynolds, P.R.1    Mottur, G.P.2    Bradbeer, C.3
  • 65
    • 0023715782 scopus 로고
    • Escherichia coli TonB protein is exported from the cytoplasm without proteolytic cleavage of its amino terminus
    • Postle, K. & Skare, J. T. Escherichia coli TonB protein is exported from the cytoplasm without proteolytic cleavage of its amino terminus. J. Biol. Chem 263, 11000-11007 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 11000-11007
    • Postle, K.1    Skare, J.T.2
  • 66
    • 0022931302 scopus 로고
    • Sequence-imposed structural constraints in the TonB protein of Escherichia coli
    • Evans. J. S., Levine, B. A., Trayer, I. P. Dorman, C. J. & Higgins, C. F. Sequence-imposed structural constraints in the TonB protein of Escherichia coli. FEBS Lett. 208, 211-216 (1986).
    • (1986) FEBS Lett. , vol.208 , pp. 211-216
    • Evans, J.S.1    Levine, B.A.2    Trayer, I.P.3    Dorman, C.J.4    Higgins, C.F.5
  • 67
    • 0025604251 scopus 로고
    • Structure and function of X-Pro dipeptide repeats in the TonB proteins of Salmonella typhimurium and Escherichia coli
    • Brewer, S. et al. Structure and function of X-Pro dipeptide repeats in the TonB proteins of Salmonella typhimurium and Escherichia coli. J. Mol. Biol 216, 883-895 (1990).
    • (1990) J. Mol. Biol. , vol.216 , pp. 883-895
    • Brewer, S.1
  • 68
    • 0027730652 scopus 로고
    • The conserved proline-rich motif is not essential for energy transduction by Escherichia coli TonB protein
    • Larsen, R. A., Wood, C. & Postle, K. The conserved proline-rich motif is not essential for energy transduction by Escherichia coli TonB protein. Mol. Microbiol. 10, 943-953 (1993).
    • (1993) Mol. Microbiol. , vol.10 , pp. 943-953
    • Larsen, R.A.1    Wood, C.2    Postle, K.3
  • 69
    • 0002085577 scopus 로고
    • ed. Schlessinger, D. American Society for Microbiology, Washington D. C.
    • Holroyd, C. D. & Bradbeer, C. in Microbiology (ed. Schlessinger, D.) 21-23 (American Society for Microbiology, Washington D. C., 1984).
    • (1984) Microbiology , pp. 21-23
    • Holroyd, C.D.1    Bradbeer, C.2
  • 70
    • 0032991467 scopus 로고    scopus 로고
    • Protonmotive force, ExbB and ligand-FepA drive conformational changes in TonB
    • Larsen, R. A., Thomas, M. G. & Postle, K. Protonmotive force, ExbB and ligand-FepA drive conformational changes in TonB. Mol. Microbiol. 31, 1809-1824 (1999). This paper presents evidence that supports a mechanism whereby TonB cycles between different conformations in response to the proton gradient across the cytoplasmic membrane, and proposes a model of energy transduction to the outer-membrane receptors.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1809-1824
    • Larsen, R.A.1    Thomas, M.G.2    Postle, K.3
  • 71
    • 0027282061 scopus 로고
    • Energy transduction between membranes: TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vivo to the outer membrane receptor FepA
    • Skare, J. T., Ahmer, B. M. M., Seachord, C. L., Darveau, R. P. & Postle, K. Energy transduction between membranes: TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vivo to the outer membrane receptor FepA. J. Biol. Chem. 268, 16302-16308 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 16302-16308
    • Skare, J.T.1    Ahmer, B.M.M.2    Seachord, C.L.3    Darveau, R.P.4    Postle, K.5
  • 72
    • 0029958770 scopus 로고    scopus 로고
    • Identification of TonB homologs in the family Enterobacteriaceae and evidence for conservation of TonB-dependent energy transduction complexes
    • Larsen, R. A. et al. Identification of TonB homologs in the family Enterobacteriaceae and evidence for conservation of TonB-dependent energy transduction complexes. J. Bacteriol. 178, 1363-1373 (1996).
    • (1996) J. Bacteriol. , vol.178 , pp. 1363-1373
    • Larsen, R.A.1
  • 73
    • 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
    • Cadieux, N. & Kadner, R. J. 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, 10673-10678 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10673-10678
    • Cadieux, N.1    Kadner, R.J.2
  • 74
    • 0036188943 scopus 로고    scopus 로고
    • TonB interacts with non-receptor proteins at the outer membrane of Escherichia coli
    • Higgs, P. I. et al. TonB interacts with non-receptor proteins at the outer membrane of Escherichia coli. J. Bacteriol. 184, 1640-1648 (2002).
    • (2002) J. Bacteriol. , vol.184 , pp. 1640-1648
    • Higgs, P.I.1
  • 75
    • 0026723111 scopus 로고
    • Membrane topology of the Escherichia coli ExbD protein
    • Kampfenkel, K. & Braun, V. Membrane topology of the Escherichia coli ExbD protein. J. Bacteriol. 174, 5485-5487 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 5485-5487
    • Kampfenkel, K.1    Braun, V.2
  • 76
    • 0027466914 scopus 로고
    • Topology of the ExbB protein in the cytoplasmic membrane of Escherichia coli
    • Kampfenkel, K. & Braun, V. Topology of the ExbB protein in the cytoplasmic membrane of Escherichia coli. J. Biol. Chem. 268, 6050-6057 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 6050-6057
    • Kampfenkel, K.1    Braun, V.2
  • 77
    • 0031791530 scopus 로고    scopus 로고
    • Interactions in the TonB-dependent energy transduction complex: ExbB and ExbD form homomultimers
    • Higgs, P. I., Myers, P. S. & Postle, K. Interactions in the TonB-dependent energy transduction complex: ExbB and ExbD form homomultimers. J. Bacteriol. 180, 6031-6038 (1998).
    • (1998) J. Bacteriol. , vol.180 , pp. 6031-6038
    • Higgs, P.I.1    Myers, P.S.2    Postle, K.3
  • 78
    • 0036231227 scopus 로고    scopus 로고
    • Quantification of known components of the Escherichia coli TonB energy transduction system: TonB, ExbB, ExbD and FepA
    • Higgs, P. I., Larsen, R. A. & Postle, K. Quantification of known components of the Escherichia coli TonB energy transduction system: TonB, ExbB, ExbD and FepA. Mol. Microbiol. 44, 271-281 (2002).
    • (2002) Mol. Microbiol. , vol.44 , pp. 271-281
    • Higgs, P.I.1    Larsen, R.A.2    Postle, K.3
  • 79
    • 0036723874 scopus 로고    scopus 로고
    • ExbB and ExbD do not function independently in TonB-dependant energy transduction
    • Held, K. G. & Postle, K. ExbB and ExbD do not function independently in TonB-dependant energy transduction. J Bacteriol. 184, 5170-5173 (2002). References 77-79 are concerned with the topological characterization of the energy-transducing complex that is formed by the proteins TonB, ExbB and ExbD.
    • (2002) J Bacteriol. , vol.184 , pp. 5170-5173
    • Held, K.G.1    Postle, K.2
  • 80
    • 0027238302 scopus 로고
    • ExbB acts as a chaperone-like protein to stabilize TonB in the cytoplasm
    • Karlsson, M., Hannavy, K. & Higgins, C. F. ExbB acts as a chaperone-like protein to stabilize TonB in the cytoplasm Mol. Microbiol. 8, 389-396 (1993).
    • (1993) Mol. Microbiol. , vol.8 , pp. 389-396
    • Karlsson, M.1    Hannavy, K.2    Higgins, C.F.3
  • 81
    • 0027168466 scopus 로고
    • Activity domains of the TonB protein
    • Traub, I., Gaisser, S. & Braun, V. Activity domains of the TonB protein Mol. Microbiol. 8, 409-423 (1993).
    • (1993) Mol. Microbiol. , vol.8 , pp. 409-423
    • Traub, I.1    Gaisser, S.2    Braun, V.3
  • 82
    • 0028145355 scopus 로고
    • Partial suppression of an Escherichia coli TonB transmembrane domain mutation (ΔV17) by a missense mutation in ExbB
    • Larsen, R. A., Thomas, M. G., Wood, G. E. & Postle, K. Partial suppression of an Escherichia coli TonB transmembrane domain mutation (ΔV17) by a missense mutation in ExbB Mol. Microbiol. 13, 627-640 (1994).
    • (1994) Mol. Microbiol. , vol.13 , pp. 627-640
    • Larsen, R.A.1    Thomas, M.G.2    Wood, G.E.3    Postle, K.4
  • 83
    • 0029913411 scopus 로고    scopus 로고
    • Energy coupled transport across the outer membrane of Escherichia coli: ExbB binds ExbD and TonB in vitro, and leucine 132 in the periplasmic region and aspartate 25 in the transmembrane region are important for ExbD activity
    • Braun, V. et al. Energy coupled transport across the outer membrane of Escherichia coli: ExbB binds ExbD and TonB in vitro, and leucine 132 in the periplasmic region and aspartate 25 in the transmembrane region are important for ExbD activity. J. Bacteriol. 178, 2836-2845 (1996).
    • (1996) J. Bacteriol. , vol.178 , pp. 2836-2845
    • Braun, V.1
  • 84
    • 0035896546 scopus 로고    scopus 로고
    • 20 and their relative positioning are essential for TonB activity, cross-linking of TonB with ExbB and the ability of TonB to respond to proton motive force
    • 20 and their relative positioning are essential for TonB activity, cross-linking of TonB with ExbB and the ability of TonB to respond to proton motive force. J. Biol. Chem. 276, 8111-8117 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 8111-8117
    • Larsen, R.A.1    Postle, K.2
  • 85
    • 0035920228 scopus 로고    scopus 로고
    • Crystal structure of the dimeric C-terminal domain of TonB reveals a novel fold
    • Chang, C., Mooser, A., Plückthun, A. & Wlodawer, A. Crystal structure of the dimeric C-terminal domain of TonB reveals a novel fold. J. Biol. Chem. 276, 27535-27540 (2001). This paper reports the atomic structure of a carboxy-terminal fragment of TonB, revealing an unexpected dimeric form.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27535-27540
    • Chang, C.1    Mooser, A.2    Plückthun, A.3    Wlodawer, A.4
  • 86
    • 0035045544 scopus 로고    scopus 로고
    • Characterization of in vitro interactions between a truncated TonB protein from Escherichia coli and the outer membrane receptors FhuA and FepA
    • Moeck, G. & Letellier, L. Characterization of in vitro interactions between a truncated TonB protein from Escherichia coli and the outer membrane receptors FhuA and FepA. J. Bacteriol. 183, 2755-2764 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 2755-2764
    • Moeck, G.1    Letellier, L.2
  • 87
    • 0028850367 scopus 로고
    • Siderophores: Structure and function of microbial iron transport compounds
    • Neilands, J. B. Siderophores: structure and function of microbial iron transport compounds. J. Biol. Chem. 270, 26723-26726 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 26723-26726
    • Neilands, J.B.1
  • 88
    • 0001946395 scopus 로고    scopus 로고
    • Siderophores and iron-transport in microorganisms
    • Pattus, F. & Abdallah, M. A. Siderophores and iron-transport in microorganisms. J. Chin. Chem. Soc. 47, 1-20 (2000).
    • (2000) J. Chin. Chem. Soc. , vol.47 , pp. 1-20
    • Pattus, F.1    Abdallah, M.A.2
  • 89
    • 0034044581 scopus 로고    scopus 로고
    • Studies and synthesis of siderophores, microbial iron chelators and analogs as potential drug delivery agents
    • Roosenberg, J. M., Lin, Y. M., Lu, Y. & Miller, M. J. Studies and synthesis of siderophores, microbial iron chelators and analogs as potential drug delivery agents. Curr. Med. Chem. 7, 159-197 (2000).
    • (2000) Curr. Med. Chem. , vol.7 , pp. 159-197
    • Roosenberg, J.M.1    Lin, Y.M.2    Lu, Y.3    Miller, M.J.4
  • 90
    • 0034079929 scopus 로고    scopus 로고
    • Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA
    • Ferguson, A. D. et al. Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA. Protein Sci. 9, 956-963 (2000).
    • (2000) Protein Sci. , vol.9 , pp. 956-963
    • Ferguson, A.D.1
  • 91
    • 0034886699 scopus 로고    scopus 로고
    • Active transport of an antibiotic ryfamycin derivative by the outer membrane protein FhuA
    • Ferguson, A. D. et al. Active transport of an antibiotic ryfamycin derivative by the outer membrane protein FhuA. Structure 9, 707-716 (2001).
    • (2001) Structure , vol.9 , pp. 707-716
    • Ferguson, A.D.1
  • 92
    • 0036216270 scopus 로고    scopus 로고
    • Active transport of iron and siderophore antibiotics
    • Braun, V. & Braun, M. Active transport of iron and siderophore antibiotics. Curr. Opin Microbiol 5, 194-201 (2002).
    • (2002) Curr. Opin. Microbiol , vol.5 , pp. 194-201
    • Braun, V.1    Braun, M.2
  • 93
    • 0037134502 scopus 로고    scopus 로고
    • X-ray crystallographic structures of the Escherichia coli periplasmic binding protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin
    • Clarke, T. E. Braun, V., Winkelmann, G., Tari, L. W. & Vogel, H. J. X-ray crystallographic structures of the Escherichia coli periplasmic binding protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin. J. Biol. Chem. 277, 13966-13972 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 13966-13972
    • Clarke, T.E.1    Braun, V.2    Winkelmann, G.3    Tari, L.W.4    Vogel, H.J.5
  • 98
    • 0033797234 scopus 로고    scopus 로고
    • Binding of ferric enterobactin by the Escherichia coli periplasmic protein FepB
    • Sprencel, C. et al. Binding of ferric enterobactin by the Escherichia coli periplasmic protein FepB. J. Bacteriol. 182, 5359-5364 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 5359-5364
    • Sprencel, C.1
  • 99
    • 0036180115 scopus 로고    scopus 로고
    • Identification of the periplasmic cobalamin-binding protein BtuF of Escherichia coli
    • Cadieux, N. et al. Identification of the periplasmic cobalamin-binding protein BtuF of Escherichia coli. J. Bacteriol. 184, 706-717 (2002).
    • (2002) J. Bacteriol. , vol.184 , pp. 706-717
    • Cadieux, N.1
  • 100
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher, K. P., Lee, A. T. & Rees, D. C. The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science 296, 1091-1098 (2002).
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.