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The Enzymes of Biological Membranes pp 617–652Cite as

The Iron-Transport Systems of Escherichia coli

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Abstract

Cells of E. coli like those of the other gram-negative bacteria are surrounded by two membranes, the outer membrane and the cytoplasmic membrane. Between these two membranes is situated the murein or peptidoglycan layer which confers rigidity to the cells. It is part of the periplasmic space from which water-soluble proteins can be released without release of the cytoplasmic proteins by a treatment called osmotic shock. Solutes which are taken up by the cells have therefore to be translocated through two membranes, the periplasmic space and the murein layer. The latter two are not considered to form a permeability barrier.

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References

  • Aisen, A., and Leibman, A., 1972, Lactoferrin and transferrin: A comparative study, Biochim. Biophys. Acta 257: 314–323.

    PubMed  CAS  Google Scholar 

  • Argast, M., and Boos, W., 1980, Co-regulation in Escherichia coli of a novel transport system for snglycerol-3-phosphate and outer membrane protein Ic(e,E) with alkaline phosphatase and phosphate binding protein, J. Bacteritol. 143: 142–150.

    CAS  Google Scholar 

  • Arnold, R. R., Cole, M. F., and McGhee, J. R., 1977, A bactericidal effect for human lactoferrin, Science 197: 163–265.

    Google Scholar 

  • Bauminger, E. R., Cohen, S. G., Dickson, D. P. E., Levy, A., Ofer, S., and Jariv, J. Y., 1980, Mössbauer spectroscopy of Escherichia coli and its iron storage protein, Biochim. Biophys. Acta 623: 237–242.

    PubMed  CAS  Google Scholar 

  • Bavoil, P., and Nikaido, H., 1981, Physical interaction between the phage X receptor protein and the carrier-immobilized maltose-binding protein of Escherichia coli, J. Biol. Chem. 256: 11385–11388.

    PubMed  CAS  Google Scholar 

  • Bennett, J. L., Jr., Eddie-Quartey, A. C., and Holt, P. J. L., 1973, Lactoferrin—an iron binding protein in synovial fluid, Arthr. Rheum. 16: 186–190.

    CAS  Google Scholar 

  • Benz, R., Janko, K., and Läuger, P., 1979, Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli, Biochim. Biophys. Acta 551: 238–247.

    PubMed  CAS  Google Scholar 

  • Benz, G., Schrder, T., Kurz, J., Wunsch, C., Karl, W., Steffens, G., Pfitzner, J., and Schmidt, D., 1982, Konstitution der Desferriform der Albomycine, Angew. Chem. Suppl. 1322–1335.

    Google Scholar 

  • Betke, K., 1981, Eisenprophylaxe beim normalen Säugling? Pädiat. Pädol. 16: 115–119.

    CAS  Google Scholar 

  • Bindereif, A., Braun, V., and Hantke, K., 1982, The cloacin receptor of Co1V-bearing Escherichia coli is part of the Fei+-aerobactin transport system, J. Bacteriol. 150: 1472–1475.

    PubMed  CAS  Google Scholar 

  • Binns, M. M., Davies, D. L., and Hardy, K. G., 1979, Cloned fragments of the CoIV, I-K94 specifying virulence and serum resistance, Nature 279: 778–781.

    PubMed  CAS  Google Scholar 

  • Boesman-Finkelstein, M., and Finkelstein, R. A., 1982, Sequential purification of lactoferrin, lysozyme and secretory immunoglobulin A from human milk, FEBS Lett. 144: 1–5.

    PubMed  CAS  Google Scholar 

  • Boyd, A., and Holland, I. B., 1979, Regulation of the synthesis of surface protein in the cell cycle of E. coli B/r, Cell 18: 287–296.

    PubMed  CAS  Google Scholar 

  • Braun, V., 1978, Structure—function relationships of the gram-negative bacterial cell envelope, in: Relations between Structure and Function in the Prokaryotic Cell (R. Y. Stanier, H. J. Rogers, and B. J. Ward, eds. ), Cambridge University Press, pp. 111–138.

    Google Scholar 

  • Braun, V., 1981, Escherichia coli cells containing the plasmid Co1V produce the iron ionophore aerobactin, FEMS Microbiol. Lett. 11: 225–228.

    CAS  Google Scholar 

  • Braun, V., and Burkhardt, R., 1982, Regulation of the CoIV plasmid-determined iron(III)-aerobactin transport system in Escherichia coli, J. Bacteriol. 152: 223–231.

    PubMed  CAS  Google Scholar 

  • Braun, V., and Hantke, K., 1977, Bacterial receptors for phages and colicins as constituents of specific transport systems, in: Microbial Interactions: Receptors and Recognition, Series B, Vol. 3 ( J. L. Reissig, ed.), Chapman and Hall, London, pp. 101–130.

    Google Scholar 

  • Braun, V., and Hantke, K., 1981, Bacterial cell surface receptors, in: Organization of Prokaryotic Cell Membranes, Vol. II ( B. K. Ghosh, ed.), CRC Press, Boca Raton, pp. 1–74.

    Google Scholar 

  • Braun, V., and Hantke, K., 1982, Receptor-dependent transport systems in Escherichia coli for iron complexes and vitamin B12, in: Membranes and Transport, Vol. 2 ( A. N. Martonosi, ed.), Plenum Press, New York and London, pp. 107–113.

    Google Scholar 

  • Braun, V., and Krieger-Brauer, H. J., 1977, Interrelationship of the phage X receptor protein and maltose transport in mutants of Escherichia colt K12, Biochim. Biophys. Acta 469: 89–98.

    PubMed  CAS  Google Scholar 

  • Braun, V., Schaller, K., and Wolff, H., 1973, A common receptor protein for phage T5 and colicin M in the outer membrane of Escherichia coli, Biochim. Biophys. Acta 328: 87–97.

    Google Scholar 

  • Braun, V., Hancock, R. E. W., Hantke, K., and 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.

    PubMed  CAS  Google Scholar 

  • Braun, V., Frenz, S., Hantke, K., and Schaller, K., 1980, Penetration of colicin M into cells of Escherichia coli, J. Bacteriol. 142: 162–168.

    PubMed  CAS  Google Scholar 

  • Braun, V., Burkhardt, R., Schneider, R., and Zimmermann, L., 1982, Chromosomal genes for Co1V plasmid-determined Fei+-aerobactin transport in Escherichia coli, J. Bacteriol. 152: 553–559.

    Google Scholar 

  • Bremer, E., Cole, S. T., Hindennach, I., Henning, U., Beck, E., Kurz, C., and Schaller, K., 1982, Export of a protein into the outer membrane of Escherichia coli K12. Stable incorporation of the OmpA protein requires less than 193 amino-terminal amino acid residues, Eur. J. Biochem. 122: 220–231.

    Google Scholar 

  • Bryce, G. F., and Brot, N., 1971, Iron transport in Escherichia coli and its relation to the repression of 2,3-dihydroxy-N-benzoyl-L-serine synthetase, Arch. Biochem. Biophys. 142: 399–406.

    PubMed  CAS  Google Scholar 

  • Buck, M., and Griffith, E., 1982, Iron mediated methylthiolation of tRNA as a regulator of operon expression in Escherichia coli, Nucleic Acids Res. 10: 2609–2623.

    PubMed  CAS  Google Scholar 

  • Bullen, J. J., 1976, Iron-binding proteins and other factors in milk responsible for resistance to Escherichia colt, in: Acute Diarrhoea in Childhood, Ciba Foundation Symposium 42, Elsevier/Excerpta Medical North-Holland, Amsterdam, pp. 149–169.

    Google Scholar 

  • Bullen, J. J., Leigh, L. C., and Rogers, H. J., 1968, The effect of iron compounds on the virulence of Escherichia coli for guinea pigs, Immunology 15: 581–588.

    PubMed  CAS  Google Scholar 

  • Casadaban, M. J., and Cohen, S. N., 1979, Lactose genes fused to exogenous promoters in one step using a Mu-lac bacteriophage: In vivo probe for transcriptional control sequences, Proc. Natl. Acad. Sci. USA 76: 4530–4533.

    PubMed  CAS  Google Scholar 

  • Clancy, J., and Savage, D. C., 1981, Another colicin V phenotype: In vitro adhesion of Escherichia coli to mouse intestinal epithelium, J. Infect. Immunol. 32: 343–352.

    CAS  Google Scholar 

  • Coulton, J. W., and Braun, V., 1979, Protein II* influences ferrichrome-iron transport in Escherichia coli K12, J. Gen. Microbiol. 110: 211–220.

    PubMed  CAS  Google Scholar 

  • Coulton, J. W., Naegeli, H.-U., and Braun, V., 1979, Iron supply of Escherichia coli with polymer-bound ferricrocin, Eur. J. Biochem. 99: 39–47.

    PubMed  CAS  Google Scholar 

  • Dietz, G. W., Jr., 1976, The hexose phosphate transport system of Escherichia colt, in: Advances in Enzymology, Vol. 44 ( A. Meister, ed.), John Wiley, New York, pp. 237–259.

    Google Scholar 

  • DiRienzo, J. M., Nakamura, K., and Inouye, M., 1978, The outer membrane proteins of gram-negative bacteria: Biosynthesis, assembly and functions, Annu. Rev. Biochem. 47: 481–532.

    PubMed  CAS  Google Scholar 

  • Eaton, J. W., Brandt, P., Mahoney, J. R., and Lee, J. T., Jr., 1982, Haptoglobin: A natural bacteriostat, Science 215: 691–693.

    PubMed  CAS  Google Scholar 

  • Ernst, J. F., Bennett, R. L., and Rothfield, L. I., 1978, Constitutive expression of the iron-enterochelin and ferrichrome uptake systems in a mutant strain of Salmonella typhimurium, J. Bacteriol. 135: 928–934.

    PubMed  CAS  Google Scholar 

  • Ferenci, T., 1980, The recognition of maltodextrins by Escherichia coli, Eur. J. Biochem. 108: 631–636.

    PubMed  CAS  Google Scholar 

  • Ferenci, T., and Boos, W., 1980, The role of the Escherichia coli X receptor in the transport of maltose and maltodextrins, J. Supramol. Struct. 13: 101–116.

    PubMed  CAS  Google Scholar 

  • Ferenci, T., Schwentorat, M., Ullrich, S., and Vilmart, J., 1980, Lambda receptor in the outer membrane of Escherichia coli as a binding protein for maltodextrins and starch polysaccharides, J. Bacteriol. 142: 521–526.

    PubMed  CAS  Google Scholar 

  • Fitzgerald, S. P., and Rogers, H. J., 1980, Bacteriostatic effect of serum: Role of antibody to lipopolysaccharide, Infect. Immunol. 27: 302–308.

    CAS  Google Scholar 

  • Fletcher, J., and Goldstein, E., 1970, The effect of parenteral iron preparations on experimental pyelonephritis, Arch. J. Exp. Pathol. 51: 280–285.

    CAS  Google Scholar 

  • Franklin, N. C., Dove, W. F., and Yanofsky, C., 1965, The linear insertion of a prophage into the chromosome of E. coli shown by deletion mapping, Biochem. Biophys. Res. Commun. 18: 910–923.

    Google Scholar 

  • Frost, G. E., and Rosenberg, H., 1973, The inducible citrate-dependent iron transport system in Escherichia coli K12, Biochim. Biophys. Acta 330: 90–101.

    PubMed  CAS  Google Scholar 

  • Frost, G. E., and Rosenberg, H., 1975, Relationship between the tonB locus and iron transport in Escherichia coli, J. Bacteriol. 124: 704–712.

    PubMed  CAS  Google Scholar 

  • Funakoshi, S., Doi, T., Nakajima, T., Suyama, T., and Tokuda, M., 1982, Antimicrobial effect of human serum IgA, Microbiol. Immunol. 26: 227–239.

    PubMed  CAS  Google Scholar 

  • Ganzoni, A. M., and Puschmann, M., 1977, Iron status and host defense, in: Proteins of Iron Metabolism ( E. B. Brown, P. Aisen, J. Fielding, and R. C. Crichton, eds.), Grune & Stratton, New York, pp. 427–432.

    Google Scholar 

  • Gibson, F., and Magrath, D. J., 1969, The isolation and characterization of a hydroxamic acid (aerobactin) formed by Aerobacter aerogenes 62–1, Biochim. Biophys. Acta 192: 175–184.

    PubMed  CAS  Google Scholar 

  • Glusker, J. P., 1980, Citrate conformation and chelation: Enzymatic implications, Acc. Chem. Res. 13: 345–352.

    CAS  Google Scholar 

  • Goebel, W., and Hedgpeth, J., 1982, Cloning and functional characterization of the plasmid-encoded hemolysin determinant of Escherichia coli, J. Bacteriol. 151: 1290–1298.

    PubMed  CAS  Google Scholar 

  • Gratia, J.-P., 1964, Résistance â la colicine B chez Eschérichia coli. Relations de spécificité entre colicine B, I, et phage Tl. Etude génétique, Ann. Inst. Pasteur (Paris) 107: 132–151.

    Google Scholar 

  • Greenwood, K. T., and Luke, R. K. J., 1976, Studies on the enzymatic synthesis of enterochelin in Escherichia coli K-12. Four polypeptides involved in the conversion of 2,3-dihydroxy-benzoate to enterochelin, Biochim. Biophys. Acta 454: 285–287.

    PubMed  CAS  Google Scholar 

  • Greenwood, K. T., and Luke, R. K. J., 1978, Enzymatic hydrolysis of enterochelin and its iron complex in Escherichia coli K-12. Properties of enterochelin esterase, Biochim. Biophys. Acta 525: 209–218.

    PubMed  CAS  Google Scholar 

  • Grevai, K. K., Warner, P. J., and Williams, P. H., 1982, An inducible outer membrane protein involved in aerobactin-mediated iron transport by CoIV strains of Escherichia coli, FEBS Lett. 140: 27–30.

    Google Scholar 

  • Griffith, E., and Humphreys, J., 1980, Isolation of enterochelin from the peritoneal washings of guinea pigs lethally infected with Escherichia coli, Infect. Immunol. 28: 286–289.

    Google Scholar 

  • Griffith, E., Stevenson, P., and Joyce, P., 1983, Pathogenic Escherichia coli express new outer membrane proteins when growing in vivo, FEMS Microbiol. Lett. 16: 95–99.

    Google Scholar 

  • Guterman, S. K., 1971, Inhibition of colicin B by enterochelin, Biochem. Biophys. Res. Commun. 44: 1149–1155.

    PubMed  CAS  Google Scholar 

  • Guterman, S., and Luria, S., 1969, Escherichia coli: Strains that excrete an inhibitor of colicin B, Science 164: 1414.

    CAS  Google Scholar 

  • Hall, B., 1982, Chromosomal mutation for citrate utilization by Escherichia coli K-12, J. Bacteriol. 151: 269–273.

    PubMed  CAS  Google Scholar 

  • Hamed, M. Y., Hider, R. C., and Silver, J., 1982, The competition between enterobactin and glutathione for iron, Inorg. Chim. Acta 66: 13–18.

    CAS  Google Scholar 

  • Hancock, R. E. W., and Braun, V., 1976, Nature of the energy requirement for the irreversible adsorption of bacteriophages TI and 080 to Escherichia coil K-12, J. Bacteriol. 125: 409–415.

    PubMed  CAS  Google Scholar 

  • Hancock, R. E. W., Hantke, K., and Braun, V., 1976, Iron transport in Escherichia coli K-12: Involvement of the colicin B receptor and of a citrate-inducible protein, J. Bacteriol. 127: 1370–1375.

    PubMed  CAS  Google Scholar 

  • Hancock, R. E. W., Hantke, K., and Braun, V., 1977, Iron transport in Escherichia coli K-12. 2,3-dihydroxybenzoate-promoted iron uptake, Arch. Microbiol. 114: 231–239.

    PubMed  CAS  Google Scholar 

  • Hantke, K., 1976, Phage T6-colicin K receptor and nucleoside transport in Escherichia coli, FEBS Lett. 70: 109–112.

    PubMed  CAS  Google Scholar 

  • Hantke, K., 1981, Regulation of ferric iron transport in Escherichia coli K-12: Isolation of a constitutive mutant, Mol. Gen. Gen. 182: 288–292.

    CAS  Google Scholar 

  • Hantke, K., 1982, Negative control of iron uptake systems in Escherichia coli, FEMS Microbiol. Lett. 15: 83–86.

    CAS  Google Scholar 

  • Hantke, K., and Braun, V., 1975a, A function common to iron enterochelin transport and actions of colicins B,I,V in Escherichia coli, FEBS Lett. 59: 277–281.

    PubMed  CAS  Google Scholar 

  • Hantke, K., and Braun, V., 1975b, Membrane receptor dependent iron transport in Escherichia coli, FEBS Lett. 49: 301–305.

    PubMed  CAS  Google Scholar 

  • Hantke, K., and Braun, V., 1978, Functional interaction of the tonA/tonB receptor system in Escherichia coli, J. Bacteriol. 135: 190–197.

    PubMed  CAS  Google Scholar 

  • Hantke, K., and Zimmermann, L., 1981, The importance of the exbB gene for vitamin B12 and ferric iron transport, FEMS Microbiol. Lett. 12: 31–35.

    CAS  Google Scholar 

  • Hanis, W. R., Carrano, C. J., and Raymond, K. N., 1979a, Coordination chemistry of microbial iron transport compounds. Isolation, characterization, and formation constants of ferric aerobactin, J. Am. Chem. Soc. 101:2722–2727.

    Google Scholar 

  • Harris, W. R., Carrano, C. J., Cooper, S. R., Sofen, S. R., Avdeef, A. E., McArdle, J. V., and Raymond, K. N., 1979b, Coordination chemistry of microbial iron transport compounds. 19. Stability constants and electrochemical behavior of ferric enterobactin and model complexes, J. Am. Chem. Soc. 101: 6097–6104.

    CAS  Google Scholar 

  • Hartmann, A., and Braun, V., 1979, Uptake and conversion of the antibiotic albomycin by Escherichia coli K-12, Eur. J. Biochem. 99: 517–524.

    PubMed  CAS  Google Scholar 

  • Hartmann, A., and Braun, V., 1980, Iron transport in Escherichia cols: Uptake and modification of ferrichrome, J. Bacteriol. 143: 246–255.

    PubMed  CAS  Google Scholar 

  • Hartmann, A., and Braun, V., 1981, Iron uptake and iron limited growth of Escherichia cols K-12, Arch. Microbiol. 130: 353–356.

    PubMed  CAS  Google Scholar 

  • Hazelbauer, G. L., and Parkinson, J. S., 1977, Bacterial chemotaxis, in: Microbial Interactions: Receptors and Recognition, Series B, Vol. 3 ( J. L. Reissig, ed.), Chapman and Hall, London, pp. 61–98.

    Google Scholar 

  • Heidinger, S., Braun, V., Pecoraro, V. L., and Raymond, K. N., 1983, Iron supply to Escherichia coli by synthetic analogs of enterochelin, J. Bacteriol. 153: 109–115.

    PubMed  CAS  Google Scholar 

  • Heuzenroeder, M. W., and Reeves, P., 1980, Periplasmic maltose-binding protein confers specificity on the outer membrane maltose pore of Escherichia coli, J. Bacteriol. 141: 431–435.

    PubMed  CAS  Google Scholar 

  • Hider, R. C., Silver, J., Neilands, J. B., Morrison, I. E. G., and Rees, L. V. E., 1979, Identification of iron(II) enterobactin and its possible role in Escherichia coli iron transport, FEBS Lett. 102: 325–328.

    PubMed  CAS  Google Scholar 

  • Hollifield, W. C., and Neilands, J. B., 1978, Ferric enterobactin transport system in Escherichia cols K12. Extraction, assay, and specificity of the outer membrane receptor, Biochemistry 17: 1922–1928.

    PubMed  CAS  Google Scholar 

  • Hussein, S., Hantke, K., and Braun, V., 1981, Citrate-dependent iron transport system of Escherichia coil K-12, Eur. J. Biochem. 117: 431–437.

    PubMed  CAS  Google Scholar 

  • Ichihara, S., and Mizushima, S., 1978, Identification of an outer membrane protein responsible for the binding of the Fe-enterochelin complex to Escherichia cols cells, J. Biochem. 83: 137–140.

    PubMed  CAS  Google Scholar 

  • Kadner, R. J., and Bassford, P. J., Jr., 1978, The role of the outer membrane in active transport, in: Bacterial Transport ( B. P. Rosen, ed.), Marcel Dekker, New York, pp. 413–462.

    Google Scholar 

  • Kadner, R. J., Heller, K., Coulton, J. W., and Braun, V., 1980, Genetic control of hydroxamate-mediated iron uptake in Escherichia coli, J. Bacteriol. 143: 256–264.

    PubMed  CAS  Google Scholar 

  • Klebba, P. E., McIntosh, M. A., and Neilands, J. B., 1982, Kinetics of biosynthesis of iron-regulated membrane proteins in Escherichia coli, J. Bacteriol. 149: 880–888.

    PubMed  CAS  Google Scholar 

  • Kochan, I., 1973, The role of iron in bacterial infections with special consideration of host-tubercle bacillus interactions, Curr. Top. Microbiol. Immunol. 60: 1–30.

    PubMed  CAS  Google Scholar 

  • Kochan, I., Krach, J. T., and Wiles, T. I., 1977, Virulence-associated acquisition of iron in mammalian serum by Escherichia coli, J. Infect. Dis. 135: 623–632.

    PubMed  CAS  Google Scholar 

  • Konisky, J., 1979, Specific transport systems and receptors for colicins and phages, in: Bacterial Outer Membranes. Biogenesis and Functions ( M. Inouye, ed.), John Wiley & Sons, New York, pp. 319–359.

    Google Scholar 

  • Konisky, J., 1982, Colicins and other bacteriocins with established modes of action, Annu. Rev. Microbiol. 36: 125–144.

    PubMed  CAS  Google Scholar 

  • Krieger-Brauer, H. J., and Braun, V., 1980, Functions related to the receptor protein specified by the tsx gene of Escherichia coli, Arch. Microbiol. 114: 233–242.

    Google Scholar 

  • Laird, A. J., and Young, I. G., 1980, Tn5 mutagenesis of the enterochelin gene cluster of Escherichia coli, Gene 11: 359–366.

    PubMed  CAS  Google Scholar 

  • Laird, A. J., Ribbons, D. W., Woodrow, G. C., and Young, I. G., 1980, Bacteriophage Mu-mediated gene transposition and in vitro cloning of the enterochelin gene cluster of Escherichia coli, Gene 11: 347–357.

    PubMed  CAS  Google Scholar 

  • Langmann, L., Young, I. G., Frost, G. E., Rosenberg, H., and Gibson, F., 1972, Enterochelin system of iron transport in Escherichia coli: Mutations affecting ferric enterochelin esterase, J. Bacteriol. 112: 1142–1149.

    Google Scholar 

  • Lingwood, M. A., and Ingram, P. L., 1982, The role of alpha haemolysin in the virulence of Escherichia coli for mice, J. Med. Microbiol. 15: 23–30.

    Google Scholar 

  • Lodge, J. S., Gaines, C. G., Arceneaux, J. E. L., and Byers, B. R., 1980, Non-hydrolytic release of iron from ferrienterobactin analogs by extracts of Bacillus subtilis, Biochem. Biophys. Res. Commun. 17: 1291–1295.

    Google Scholar 

  • Luckey, M., and Nikaido, H., 1980, Specificity of diffusion channels produced by X phage receptor protein of Escherichia coli, Proc. Natl. Acad. Sci. USA 77: 167–171.

    PubMed  CAS  Google Scholar 

  • Luckey, M., Wayne, R., and Neilands, J. B., 1975, In vitro competition between ferrichrome and phage for the outer membrane T5 receptor complex of Escherichia coli, Biochem. Biophys. Res. Commun. 64: 687–693.

    PubMed  CAS  Google Scholar 

  • Lugtenberg, B., and van Alphen, L., 1983, Molecular architecture and functioning of the outer membrane of Escherichia coli and other gram-negative bacteria, Biochim. Biophys. Acta. 737: 51–115.

    PubMed  CAS  Google Scholar 

  • Lugtenberg, B., Meijers, J., Peters, R., van der Hoek, P., and van Alphen, L., 1975, Electrophoretic resolution of the major outer membrane protein of Escherichia coli K12 into four bands, FEBS Leu. 58: 254–258.

    CAS  Google Scholar 

  • Martonosi, A. N. (ed.), 1982, Membranes and Transport, Plenum Press, New York, London.

    Google Scholar 

  • Masson, P. L., Heremans, J. F., and Dive, C., 1966, An iron-binding protein common to many external excretions, Clin. Chim. Acta 14: 735–739.

    CAS  Google Scholar 

  • McIntosh, M. A., and Earhart, C. F., 1977, Coordinate regulation by iron of the synthesis of phenolate compounds and three outer membrane proteins in Escherichia coli, J. Bacteriol. 131: 331–339.

    PubMed  CAS  Google Scholar 

  • McIntosh, M. A., Chenault, S. S., and Earhart, C. F., 1979, Genetic and physiological studies on the relationship between colicin B resistance and ferrienterochelin uptake in Escherichia coli K-12. J. Bacteriol. 137: 653–657.

    PubMed  CAS  Google Scholar 

  • Mellencamp, M. W., McCabe, M. A., and Kochan, I., 1981, The growth-promoting effect of bacterial iron for serum-exposed bacteria, Immunology 43: 483–491.

    PubMed  CAS  Google Scholar 

  • Michaelis, S., and Beckwith, J., 1982, Mechanism of incorporation of cell envelope proteins in Escherichia coli, Annu. Rev. Microbiol. 36: 435–465.

    PubMed  CAS  Google Scholar 

  • Moore, D. G., and Earhart, C. F., 1981, Specific inhibition of Escherichia coli ferrienterochelin uptake by a normal human serum immunoglobulin, Infect. Immunol. 31: 631–635.

    CAS  Google Scholar 

  • Moore, D. G., Yancey, J., Lankford, C. E., and Earhard, C. F., 1980, Bacteriostatic enterochelin-specific immunoglobulin from human serum, Infect. Immunol. 27: 418–423.

    CAS  Google Scholar 

  • Murray, G. J., Clark, G. E. D., Parniak, M. A., and Viswanatha, T., 1977, Effect of metabolites on EN-hydroxylysine formation in cell-free extracts of Aerobacter aerogenes 62–1, Can. J. Biochem. 55: 625–629.

    PubMed  CAS  Google Scholar 

  • Neilands, J. B., 1981, Microbial iron compounds, Annu. Rev. Biochem. 50: 715–731.

    PubMed  CAS  Google Scholar 

  • Neilands, J. B., 1982, Microbial envelope proteins related to iron, Annu. Rev. Microbiol. 36: 285–309.

    PubMed  CAS  Google Scholar 

  • Nikaido, H., 1982, Proteins forming large channels in biological membranes, in: Membranes and Transport, Vol. 2 ( A. N. Martonosi, ed.), Plenum Press, New York and London, pp. 265–270.

    Google Scholar 

  • Nikaido, H., and Nakae, T., 1979, The outer membrane of gram-negative bacteria, in: Advances in Microbial Physiology, Vol. 20 ( A. H. Rose and J. G. Morris, eds.), Academic Press, London, pp. 163–250.

    Google Scholar 

  • Norrestam, R., Stensland, B., and Bränden, C.-J., 1975, On the conformation of cyclic iron-containing hexapeptides: The crystal structure and molecular structure of ferrichrysin, J. Mol. Biol. 99: 501–506.

    PubMed  CAS  Google Scholar 

  • Osborn, M. J., and Wu, H., 1980, Proteins of the outer membrane of gram-negative bacteria, Annu. Rev. Microbiol. 34: 369–422.

    PubMed  CAS  Google Scholar 

  • Overbeeke, N., and Lugtenberg, B., 1982, Recognition site for phosphorus-containing compounds and other negatively charged solutes on the PhoE protein pore of the outer membrane of Escherichia coli K-12, Eur. J. Biochem. 126: 113–118.

    PubMed  CAS  Google Scholar 

  • Pappenheimer, A. M., 1977, Diphtheria toxin, Annu. Rev. Biochem. 46: 69–94.

    PubMed  CAS  Google Scholar 

  • Pamiak, M. A., Jackson, G. E. D., Murray, G. J., and Viswanatha, T., 1979, Studies on the formation ofN -hydroxylysine in cell-free extracts of Aerobacteraerogenes 62–1, Biochim. Biophys. Acta 569: 99–108.

    Google Scholar 

  • Payne, S. M., 1980, Synthesis and utilization of siderophore by Shigella fiexneri, J. Bacteriol. 143: 1420–1424.

    PubMed  CAS  Google Scholar 

  • Perry, R. D., and San Clemente, C. L., 1979, Siderophore synthesis in Klebsiella pneumoniae and Shigella sonnei during iron deficiency, J. Bacteriol. 140: 1129–1132.

    PubMed  CAS  Google Scholar 

  • Plastow, G. S., and Holland, I. B., 1979, Identification of an Escherichia coil inner membrane polypeptide specified by a X-tonB transducing bacteriophage, Biochem. Biophys. Res. Commun. 90: 1007–1014.

    PubMed  CAS  Google Scholar 

  • Postle, K., and Reznikoff, W., 1979, Identification of the Escherichia coli tonB gene product in minicells containing tonB hybrid plasmids, J. Mol. Biol. 131: 619–636.

    PubMed  CAS  Google Scholar 

  • Pugsley, A. P., 1977, Map location of the cbr gene coding for production of the outer membrane receptor for ferrienterochelin and colicins B and D in Escherichia coil K-12, FEMS Microbiol. Letts. 2: 275–277.

    CAS  Google Scholar 

  • Pugsley, A. P., and Reeves, P., 1976, Characterization of colicin B-resistant mutants of Escherichia coli K-12: Colicin resistance and the role of enterochelin, J. Bacteriol. 127: 218–228.

    PubMed  CAS  Google Scholar 

  • Pugsley, A. P., and Reeves, P., 1977, The role of colicin receptors in the uptake of ferrienterochelin by Escherichia coli K-12, Biochem. Biophys. Res. Commun. 74: 903–911.

    PubMed  CAS  Google Scholar 

  • Raymond, K. N., Harris, W. R., Carrano, C. J., and Weitl, F. L., 1982, The synthesis, thermodynamic behaviour, and biological properties of metal-iron-specific sequestering agents for iron and the actinides, in: The Biological Chemistry of Iron ( H. B. Dunford, D. Dolphin, K. N. Raymond, and L. Sieker, eds.), D. Reidel, Dortrecht, Boston, London, pp. 85–105.

    Google Scholar 

  • Reuser, A. J. J., and Postma, P. W., 1973, The induction of translocators for di-and tricarboxylic-acid anions in Azotobacter vinelandii, Eur. J. Biochem. 33: 584–592.

    PubMed  CAS  Google Scholar 

  • Reynolds, P. R., Mottur, G. P., and Bradbeer, C., 1980, Transport of vitamin B12 in Escherichia coli. Some observations of the roles of the gene products of btuC and tonB, J. Biol. Chem. 255: 4313–4319.

    PubMed  CAS  Google Scholar 

  • Rogers, H. J., 1973, Iron binding catechols and virulence in Escherichia coli, Infect. Immunol. 7:445–456.

    Google Scholar 

  • Rogers, H. J., and Synge, C., 1978, Bacteriostatic effect of human milk on Escherichia coli: The role of IgA, Immunology 34: 19–28.

    Google Scholar 

  • Rosenberg, H., and Young, I. G., 1974, Iron transport in the enteric bacteria, in: Microbial Iron Metabolism (J. B. Neilands, ed.), Academic Press, New York, London, pp. 67–82.

    Google Scholar 

  • Schneider, R., Hartmann, A., and Braun, V., 1981, Transport of the iron ionophore ferrichrome in Escherichia coli and Salmonella typhimurium LT2, FEMS Microbiol. Lett. 11: 115–119.

    CAS  Google Scholar 

  • Sillen, L. G., and Martell, A. E., 1964, Stability Constants of Metal—Ion Complexes, The Chemical Society, London.

    Google Scholar 

  • Spiro, T. G., Pape, L., and Saltman, P., 1967, The hydrolytic polymerization of ferric citrate. I. The chemistry of the polymer, J. Am. Chem. Soc. 89: 5555–5559.

    CAS  Google Scholar 

  • Stephens, S., Dolby, J. M., Montreuil, J., and Spik, G., 1980, Differences in inhibition of the growth of commensal and enteropathogenic strains of Escherichia coli by lactotransferrin and secretory immunoglobulin A isolated from human milk, Immunology 41: 597–603.

    PubMed  CAS  Google Scholar 

  • Stuart, S. J., Greenwood, K. T., and Luke, R. K. J., 1980, Hydroxamate-mediated transport of iron controlled by Co1V plasmids, J. Bacteriol. 143: 35–42.

    PubMed  CAS  Google Scholar 

  • Szmelcman, S., and Hofnung, M., 1975, Maltose transport in Escherichia coli K-12. Involvement of the bacteriophage lambda receptor, J. Bacteriol. 124: 112–118.

    PubMed  CAS  Google Scholar 

  • Szmelcman, S., Schwartz, M., Silhavy, T. J., and Boos, W., 1976, Maltose transport in Escherichia coli K-12. A comparison of transport kinetics in wild-type and X-resistant mutants with the dissociation constants of the maltose-binding protein as measured by fluorescence quenching, Eur. J. Biochem. 65: 13–19.

    PubMed  CAS  Google Scholar 

  • Tidmarsh, G. F., and Rosenberg, L. T., 1981, Acquisition of iron from transferrin by Salmonella paratyphi B, Curr. Microbiol. 6: 217–220.

    CAS  Google Scholar 

  • van der Helm, D., Baker, J. R., Eng-Wilmot, D. L., Hossain, M. B., and Loghry, R. A., 1980, Crystal structure of ferrichrome and a comparison with the structure of ferrichrome A, J. Am. Chem. Soc. 104: 4224–4231.

    Google Scholar 

  • van Tiel-Menkveld, G. J., Mentjox-Vervuurt, J. M., Oudega, B., and de Graaf, F., 1982, Siderophore production by Enterobacter cloacae and a common receptor protein for the uptake of aerobactin and cloacin DF13, J. Bacteriol. 150: 490–497.

    PubMed  Google Scholar 

  • Wagegg, W., and Braun, V., 1981, Ferric citrate transport in Escherichia coil requires outer membrane receptor protein FecA, J. Bacteriol. 145: 156–163.

    PubMed  CAS  Google Scholar 

  • Wandersman, C., Schwartz, M., and Ferenci, T., 1979, Escherichia coli mutants impaired in maltodextrin transport, J. Bacteriol. 140: 1–13.

    CAS  Google Scholar 

  • Wang, C. C., and Newton, A., 1971, An additional step in the transport of iron defined by the tonB locus of Escherichia coli, J. Biol. Chem. 246: 2147–2151.

    PubMed  CAS  Google Scholar 

  • Warner, P. J., Williams, P. H., Bindereif, A., and Neilands, J. B., 1981, CoIV plasmid-specified aerobactin synthesis by invasive strains of Escherichia coli, Infect. Immunol. 33: 540–545.

    CAS  Google Scholar 

  • Weinberg, E. D., 1974, Iron and susceptibility to infectious disease, Science 184:952–956. Weinberg, E. D., 1978, Iron and infection, Microbiol. Rev. 42: 45–66.

    Google Scholar 

  • Welch, R. A., Dellinger, E. P., Minshew, A., and Falkow, S., 1981, Haemolysin contributes to virulence of extraintestinal E. coli infections, Nature 294: 665–667.

    PubMed  CAS  Google Scholar 

  • Williams, P., 1979, Novel iron uptake system specified by ColV plasmids: An important component in the virulence of invasive strains of Escherichia coli, Infect. Immunol. 26: 925–932.

    CAS  Google Scholar 

  • Williams, P., and Warner, P. J., 1980, CoIV plasmid-mediated, colicin V-independent iron uptake system of invasive strains of Escherichia coli, Infect. Immunol. 29: 411–416.

    CAS  Google Scholar 

  • Woodrow, G. C., Langman, L., Young, I. G., and Gibson, F., 1978, Mutations affecting the citrate-dependent iron uptake system in Escherichia coli, J. Bacteriol. 133: 1524–1526.

    PubMed  CAS  Google Scholar 

  • Woodrow, C. W., Young, I. G., and Gibson, F., 1979, Biosynthesis of enterochelin in Escherichia coli K-12. Separation of the polypeptides coded by the entD, E, F and G genes, Biochim. Biophys. Acta 582: 145–153.

    PubMed  CAS  Google Scholar 

  • Wookey, P., 1982, The tonB gene product in Escherichia coli. Energy-coupling or molecular processing of permeases, FEBS Lett. 139: 145–154.

    PubMed  CAS  Google Scholar 

  • Wookey, P., and Rosenberg, H., 1978, Involvement of inner and outer membrane components in the transport of iron and in colicin B action in Escherichia coli, J. Bacteriol. 133: 661–666.

    PubMed  CAS  Google Scholar 

  • Wookey, P., Hussein, S., and Braun, V., 1981, Functions in outer and inner membranes of Escherichia coli for femchrome transport, J. Bacteriol. 146: 1158–1161.

    PubMed  CAS  Google Scholar 

  • Worsham, P. L., and Konisky, J., 1981, Use of cir-lac operon fusions to study transcriptional regulation of the colicin la receptor in Escherichia coli K-12, J. Bacteriol. 145: 647–650.

    PubMed  CAS  Google Scholar 

  • Yancey, R. J., Breeding, S. A. L., and Lankford, C., 1979, Enterochelin (enterobactin): Virulence factor for Salmonella typhimurium, Infect. Immunol. 24: 174–180.

    CAS  Google Scholar 

  • Yariv, J., Kalb, J. A., Sperling, R., Bauminger, E. R., Cohen, S. G., and Ofer, S., 1981, The composition and the structure of bacterioferritin of Escherichia coli, Biochem. J. 197: 171–175.

    PubMed  CAS  Google Scholar 

  • Young, I. G., 1976, Preparation of enterochelin from Escherichia coli, Prep. Biochem. 6: 123–131.

    PubMed  CAS  Google Scholar 

  • Zähner, H., Keller-Schierlein, W., Hütter, R., Hess-Leisinger, K., and Deér, A., 1963, Sideramine von Mikroorganismen. Sideramine aus Aspergillaceen, Arch. Microbiol. 45: 119–135.

    Google Scholar 

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  1. Mikrobiologie II, Universität Tübingen, D-7400, Tübingen, West Germany

    Volkmar Braun

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  1. State University of New York, Syracuse, New York, USA

    Anthony N. Martonosi

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Braun, V. (1985). The Iron-Transport Systems of Escherichia coli. In: Martonosi, A.N. (eds) The Enzymes of Biological Membranes. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-4601-2_18

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  • DOI: https://doi.org/10.1007/978-1-4684-4601-2_18

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