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Volumn 247, Issue 3, 1997, Pages 770-775

Oligomeric states and siderophore binding of the ligand-gated FhuA protein that forms channels across Escherichia coli outer membranes

Author keywords

Analytical ultracentrifugation; Ferrichrome transport; Mmebrane protein; Signal transduction; barrel

Indexed keywords

FERRICHROME; ION CHANNEL; MEMBRANE PROTEIN;

EID: 0030850807     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-1-00770.x     Document Type: Article
Times cited : (51)

References (42)
  • 1
    • 0019348762 scopus 로고
    • Microbial iron compounds
    • Neilands, J. B. (1981) Microbial iron compounds, Annu. Rev. Biochem. 50, 715-731.
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 715-731
    • Neilands, J.B.1
  • 2
    • 0024593726 scopus 로고
    • Evolutionary relationship between TonB-dependent outer membrane transport proteins: Nucleotide and amino acid sequences of the Escherichia coli colicin I receptor gene
    • Nau, C. D. & Konisky, J. (1989) Evolutionary relationship between TonB-dependent outer membrane transport proteins: nucleotide and amino acid sequences of the Escherichia coli colicin I receptor gene. J. Bacteriol. 171, 1041-1047.
    • (1989) J. Bacteriol. , vol.171 , pp. 1041-1047
    • Nau, C.D.1    Konisky, J.2
  • 3
    • 0027945605 scopus 로고
    • Microbial iron transport
    • Guerinot, M. L. (1994) Microbial iron transport, Annu. Rev. Microbiol. 48, 743-772.
    • (1994) Annu. Rev. Microbiol. , vol.48 , pp. 743-772
    • Guerinot, M.L.1
  • 4
    • 0025572764 scopus 로고
    • Vitamin B12 transport in Escherichia coli: Energy coupling between membranes
    • Kadner, R. J. (1990) Vitamin B12 transport in Escherichia coli: energy coupling between membranes, Mol. Microbiol. 4, 2027-2033.
    • (1990) Mol. Microbiol. , vol.4 , pp. 2027-2033
    • Kadner, R.J.1
  • 5
    • 0029155042 scopus 로고
    • Energy-coupled transport and signal transduction through the gram-negative outer membrane via TonB-ExbB-ExbD-dependent receptor proteins
    • Braun, V. (1995) 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) FEMS Microbiol. Rev. , vol.16 , pp. 295-307
    • Braun, V.1
  • 6
    • 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. (1993) Mechanisms of TonB-catalyzed iron transport through the enteric bacterial cell envelope. J. Bioenerg. Biomembr. 25, 603-611.
    • (1993) J. Bioenerg. Biomembr. , vol.25 , pp. 603-611
    • Klebba, P.E.1    Rutz, J.M.2    Liu, J.3    Murphy, C.K.4
  • 7
    • 0025666854 scopus 로고
    • TonB and the Gram-negative dilemma
    • Postle, K. (1990) TonB and the Gram-negative dilemma, Mol. Microbiol. 4, 2019-2025.
    • (1990) Mol. Microbiol. , vol.4 , pp. 2019-2025
    • Postle, K.1
  • 8
    • 0017177442 scopus 로고
    • Functional organization of the outer membrane of Escherichia coli: Phage and colicin receptors as components of iron uptake systems
    • Braun, V., Hancock, R. H. W., Hantke, K. & Hartmann, A. (1976) Functional organization of the outer membrane of Escherichia coli: phage and colicin receptors as components of iron uptake systems, J. Supramol. Struct. 5, 37-58.
    • (1976) J. Supramol. Struct. , vol.5 , pp. 37-58
    • Braun, V.1    Hancock, R.H.W.2    Hantke, K.3    Hartmann, A.4
  • 9
    • 0021090369 scopus 로고
    • Molecular cloning of the ferrichrome-iron receptor of Escherichia coli K-12
    • Coulton, J. W., Mason, P. & DuBow, M. S. (1983) Molecular cloning of the ferrichrome-iron receptor of Escherichia coli K-12, J. Bacteriol. 156, 1315-1321.
    • (1983) J. Bacteriol. , vol.156 , pp. 1315-1321
    • Coulton, J.W.1    Mason, P.2    DuBow, M.S.3
  • 10
    • 0021071840 scopus 로고
    • Cloning and expression of the fhu genes involved in iron(III)-hydroxamate uptake by Escherichia coli
    • Fecker, L. & Braun, V. (1983) Cloning and expression of the fhu genes involved in iron(III)-hydroxamate uptake by Escherichia coli, J. Bacteriol. 156, 1301-1314.
    • (1983) J. Bacteriol. , vol.156 , pp. 1301-1314
    • Fecker, L.1    Braun, V.2
  • 11
    • 0020641329 scopus 로고
    • Integration of the overproduced bacteriophage T5 receptor protein in the outer membrane of Escherichia coli
    • Menichi, B. & Buu, A. (1983) Integration of the overproduced bacteriophage T5 receptor protein in the outer membrane of Escherichia coli. J. Bacteriol. 154, 130-138.
    • (1983) J. Bacteriol. , vol.154 , pp. 130-138
    • Menichi, B.1    Buu, A.2
  • 12
    • 0027450611 scopus 로고
    • Insertion derivatives containing segments of up to 16 amino acids identify surface- and periplasmexposed regions of the Fhua outer membrane receptor of Escherichia coli K-12
    • Koebnik, R. & Braun, V. (1993) Insertion derivatives containing segments of up to 16 amino acids identify surface- and periplasmexposed regions of the Fhua outer membrane receptor of Escherichia coli K-12, J. Bacteriol. 175, 826-839.
    • (1993) J. Bacteriol. , vol.175 , pp. 826-839
    • Koebnik, R.1    Braun, V.2
  • 14
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution
    • Schirmer, T., Keller, T. A., Wang, Y. F. & Rosenbusch, J. P. (1995) Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution, Science 267, 512-514.
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.F.3    Rosenbusch, J.P.4
  • 15
    • 0029914253 scopus 로고    scopus 로고
    • FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5
    • Bonhivers, M., Ghazi, A., Boulanger, P. & Letellier, L. (1996) FhuA, a transporter of the Escherichia coli outer membrane, is converted into a channel upon binding of bacteriophage T5, EMBO J. 15, 1850-1856.
    • (1996) EMBO J. , vol.15 , pp. 1850-1856
    • Bonhivers, M.1    Ghazi, A.2    Boulanger, P.3    Letellier, L.4
  • 16
    • 0031033539 scopus 로고    scopus 로고
    • Modeling ligand-gated receptor activity: FhuA-mediated ferrichrome efflux from lipid vesicles triggered by Phage T5
    • Locher, K. P. & Rosenbusch, J. P. (1997) Modeling ligand-gated receptor activity: FhuA-mediated ferrichrome efflux from lipid vesicles triggered by Phage T5, J. Biol. Chem. 272, 1448-1451.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1448-1451
    • Locher, K.P.1    Rosenbusch, J.P.2
  • 17
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, J. & Changeux, J.-P. (1965) On the nature of allosteric transitions: a plausible model, J. Mol. Biol. 12, 88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.-P.3
  • 18
    • 0023686033 scopus 로고
    • Signal transduction by allosteric receptor oligomerization
    • Schlessinger, J. (1988) Signal transduction by allosteric receptor oligomerization, Trends Biochem. Sci. 13, 443-447.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 443-447
    • Schlessinger, J.1
  • 19
    • 0028104202 scopus 로고
    • Regulation of signal transduction and signal diversity by receptor oligomerization
    • Lemmon, M. A. & Schlessinger, J. (1994) Regulation of signal transduction and signal diversity by receptor oligomerization, Trends Biochem. Sci. 19, 459-463.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 459-463
    • Lemmon, M.A.1    Schlessinger, J.2
  • 20
    • 0029992660 scopus 로고    scopus 로고
    • Lipidic cubic phases: A novel concept for the crystallization of membrane proteins
    • Landau, E. M. & Rosenbusch, J. P. (1996) Lipidic cubic phases: a novel concept for the crystallization of membrane proteins, Proc. Natl Acad. Sci. USA 93, 14532-14535.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14532-14535
    • Landau, E.M.1    Rosenbusch, J.P.2
  • 21
    • 0022589342 scopus 로고
    • Preparation of the FhuA (TonA) receptor protein from cell envelopes of an overproducing strain of Escherichia coli K-12
    • Hoffmann, H., Fischer, E., Kraut, H. & Braun, V. (1986) Preparation of the FhuA (TonA) receptor protein from cell envelopes of an overproducing strain of Escherichia coli K-12, J. Bacteriol. 166, 404-411.
    • (1986) J. Bacteriol. , vol.166 , pp. 404-411
    • Hoffmann, H.1    Fischer, E.2    Kraut, H.3    Braun, V.4
  • 22
    • 0022558545 scopus 로고
    • Isolation and crystallization of bacterial porin
    • Garavito, R. M. & Rosenbusch, J. P. (1986) Isolation and crystallization of bacterial porin, Methods Enzymol. 125, 309-328.
    • (1986) Methods Enzymol. , vol.125 , pp. 309-328
    • Garavito, R.M.1    Rosenbusch, J.P.2
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 50549164858 scopus 로고
    • A rapid and sensitive submicro phosphorous determination
    • Boettcher, C. J. F., Van Gent, C. M. & Fries, C. (1961) A rapid and sensitive submicro phosphorous determination, Anal. Chim. Acta 24, 203-204.
    • (1961) Anal. Chim. Acta , vol.24 , pp. 203-204
    • Boettcher, C.J.F.1    Van Gent, C.M.2    Fries, C.3
  • 25
    • 77956985612 scopus 로고
    • Thin-layer chromatography of lipids
    • Skipski, V. P. & Barclay, M. (1969) Thin-layer chromatography of lipids, Methods Enzymol. 14, 530-598.
    • (1969) Methods Enzymol. , vol.14 , pp. 530-598
    • Skipski, V.P.1    Barclay, M.2
  • 26
    • 0028861610 scopus 로고
    • Cross-linking of porin with glutardialdehyde: A test for the adequacy of premises of cross-linking theory
    • Azem, A., Shaked, I., Rosenbusch, J. P. & Daniel, E. (1995) Cross-linking of porin with glutardialdehyde: a test for the adequacy of premises of cross-linking theory, Biochim. Biophys. Acta 1243, 151-156.
    • (1995) Biochim. Biophys. Acta , vol.1243 , pp. 151-156
    • Azem, A.1    Shaked, I.2    Rosenbusch, J.P.3    Daniel, E.4
  • 27
    • 0019877287 scopus 로고
    • Hydrodynamic properties of phospholipid vesicles and of sucrase isomaltase-phospholipid vesicles
    • Spiess, M., Hauser, H., Rosenbusch, J. P. & Semenza, G. (1981) Hydrodynamic properties of phospholipid vesicles and of sucrase isomaltase-phospholipid vesicles, J. Biol. Chem. 256, 8977-8982.
    • (1981) J. Biol. Chem. , vol.256 , pp. 8977-8982
    • Spiess, M.1    Hauser, H.2    Rosenbusch, J.P.3    Semenza, G.4
  • 28
    • 0019208235 scopus 로고
    • TonB-independent ferrichrome-mediated iron transport in Escherichia coli spheroplasts
    • Weaver, C. A. & Konisky, J. (1980) tonB-independent ferrichrome-mediated iron transport in Escherichia coli spheroplasts, J. Bacteriol. 143, 1513-1518.
    • (1980) J. Bacteriol. , vol.143 , pp. 1513-1518
    • Weaver, C.A.1    Konisky, J.2
  • 29
    • 0015798050 scopus 로고
    • Carbamyl phosphate binding to aspartate transcarbamylase
    • Rosenbusch, J. P. & Griffin, J. G. (1973) Carbamyl phosphate binding to aspartate transcarbamylase, J. Biol. Chem. 248, 5063-5066.
    • (1973) J. Biol. Chem. , vol.248 , pp. 5063-5066
    • Rosenbusch, J.P.1    Griffin, J.G.2
  • 30
    • 0016823156 scopus 로고
    • Cell-wall lipopolysaccharide from Escherichia coli B
    • Prehm, P., Szrim, S., Jann, B. & Jann, K. (1975) Cell-wall lipopolysaccharide from Escherichia coli B, Eur. J. Biochem. 56, 41-55.
    • (1975) Eur. J. Biochem. , vol.56 , pp. 41-55
    • Prehm, P.1    Szrim, S.2    Jann, B.3    Jann, K.4
  • 31
    • 0004384704 scopus 로고
    • Matrix porin: A periodically arranged protein in the outer membrane of Escherichia coli
    • (Baumeister, W. & Vogell, W., eds) Springer Verlag, Heidelberg-New York
    • Rosenbusch, J. P., Steven, A. C., Alkan, M. & Regenass, M. (1980) Matrix porin: a periodically arranged protein in the outer membrane of Escherichia coli, in: Electron microscopy at molecular dimensions (Baumeister, W. & Vogell, W., eds) pp. 1-10, Springer Verlag, Heidelberg-New York.
    • (1980) Electron Microscopy at Molecular Dimensions , pp. 1-10
    • Rosenbusch, J.P.1    Steven, A.C.2    Alkan, M.3    Regenass, M.4
  • 32
    • 0021111646 scopus 로고
    • X-ray diffraction analysis of matrix porin, an integral membrane protein from Escheriehia coli outer membranes
    • Garavito, R. M., Jenkins, J., Jansonius, J. N., Karlsson, R. & Rosenbusch, J. P. (1983) X-ray diffraction analysis of matrix porin, an integral membrane protein from Escheriehia coli outer membranes, J. Mol. Biol. 164, 313-327.
    • (1983) J. Mol. Biol. , vol.164 , pp. 313-327
    • Garavito, R.M.1    Jenkins, J.2    Jansonius, J.N.3    Karlsson, R.4    Rosenbusch, J.P.5
  • 34
    • 84969001783 scopus 로고
    • The attractions of proteins for small molecules and ions
    • Scatchard, G. (1949) The attractions of proteins for small molecules and ions, Ann. NY Acad. Sci. 51, 660-672.
    • (1949) Ann. NY Acad. Sci. , vol.51 , pp. 660-672
    • Scatchard, G.1
  • 35
    • 1542722023 scopus 로고
    • Relative free energies and dissociation constants of macroscopic ions
    • Hill, T. L. (1944) Relative free energies and dissociation constants of macroscopic ions, J. Phys. Chem. 48, 101-111.
    • (1944) J. Phys. Chem. , vol.48 , pp. 101-111
    • Hill, T.L.1
  • 36
    • 0016350456 scopus 로고
    • Characterization of the major envelope protein from Escheriehia coli. Regular arrangement on the peptido-glycan and unusual dodecyl sulfate binding
    • Rosenbusch, J. P. (1974) Characterization of the major envelope protein from Escheriehia coli. Regular arrangement on the peptido-glycan and unusual dodecyl sulfate binding. J. Biol. Chem. 249, 8019-8029.
    • (1974) J. Biol. Chem. , vol.249 , pp. 8019-8029
    • Rosenbusch, J.P.1
  • 37
    • 0010287406 scopus 로고    scopus 로고
    • Purification and structural and functional characterization of FhuA, a transporter of the Escherichia coli outer membrane
    • Boulanger, P., Le Maire, M., Bonhivers, M., Dubois, S., Desmadril, M. & Letellier, L. (1996) Purification and structural and functional characterization of FhuA, a transporter of the Escherichia coli outer membrane. Biochemistry 35, 14216-14224.
    • (1996) Biochemistry , vol.35 , pp. 14216-14224
    • Boulanger, P.1    Le Maire, M.2    Bonhivers, M.3    Dubois, S.4    Desmadril, M.5    Letellier, L.6
  • 38
    • 0017037714 scopus 로고
    • Effects of heating in dodecyl sulfate solution on the conformation and electrophoretic mobility of isolated major outer membrane proteins from Escherichia coli K-12
    • Nakamura, K. & Mizushima, S. (1976) Effects of heating in dodecyl sulfate solution on the conformation and electrophoretic mobility of isolated major outer membrane proteins from Escherichia coli K-12, J. Biochem. (Tokyo) 80, 1411-1422.
    • (1976) J. Biochem. (Tokyo) , vol.80 , pp. 1411-1422
    • Nakamura, K.1    Mizushima, S.2
  • 39
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • de Vos, A. M., Ultsch, M. & Kossiakoff, A. A. (1992) Human growth hormone and extracellular domain of its receptor: crystal structure of the complex, Science 255, 306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 40
    • 0027211704 scopus 로고
    • Crystal structure of the soluble human 55 kd TNF receptor-human TNF-beta complex: Implications for TNF receptor activation
    • Banner, D. W., D'Arcy, A., Janes, W., Gentz, R., Schoenfeld, H.-J., Broger, C., Loetscher, H. & Lesslauer, W. (1993) Crystal structure of the soluble human 55 kd TNF receptor-human TNF-beta complex: Implications for TNF receptor activation, Cell 73, 431-445.
    • (1993) Cell , vol.73 , pp. 431-445
    • Banner, D.W.1    D'Arcy, A.2    Janes, W.3    Gentz, R.4    Schoenfeld, H.-J.5    Broger, C.6    Loetscher, H.7    Lesslauer, W.8
  • 41
    • 0026332810 scopus 로고
    • Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule
    • Cunningham, B. C., Ultsch, M., de Vos, A. M., Mulkerrin, M. G., Clauser, K. R. & Wells, J. A. (1991) Dimerization of the extracellular domain of the human growth hormone receptor by a single hormone molecule. Science 254, 821-825.
    • (1991) Science , vol.254 , pp. 821-825
    • Cunningham, B.C.1    Ultsch, M.2    De Vos, A.M.3    Mulkerrin, M.G.4    Clauser, K.R.5    Wells, J.A.6
  • 42
    • 0002773860 scopus 로고
    • Biomembrane fluidity - Studies of model and natural biomembranes
    • (Chapman, D., ed.) Academic Press Inc., London
    • Chapman, D. & Benga, G. (1984) Biomembrane fluidity - studies of model and natural biomembranes, in Biological membranes (Chapman, D., ed.) pp. 1-56, Academic Press Inc., London.
    • (1984) Biological Membranes , pp. 1-56
    • Chapman, D.1    Benga, G.2


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