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Bacterioferritin: A Hemoprotein Member of the Ferritin Family

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 356))

Abstract

Ferritin has been known in eukaryotic cells for over 50 years1 but only in the last 15 years has a ferritin-like molecule been recognized in bacterial systems. In 1979 2 the hemoprotein originally designated3 as Azotobacter vinelandii cytochrome b557.5 was shown to be ferritin-like in character on the basis of subunit size and composition, electron microscopy of the holoprotein, and physical characterization of the core iron. 2 Since this initial identification of bacterioferritin its presence has been established in a wide variety of prokaryotic organisms including Escherichia coli, 4 Pseudomonas aeruginosa 5 Nitrobacter winogradskii 5 Mycobacterium paratuberculosis, 7 Synechocystis P.C.C. 6803, 8 Yersinia pestis 9 and Rhodobacter capsulatus. 10 In each of the above species heme in the form of extractable protoporphyrin IX is intimately associated with the protein.

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References

  1. R.R. Chrichton, “Inorganic Biochemistry of Iron Metabolism,” Ellis Horwood, New York (1991).

    Google Scholar 

  2. E. I. Stiefel and G. D. Watt, Azotobacter cytochrome b557.5 is a bacterioferritin, Nature (London) 279: 81 (1979).

    Article  CAS  Google Scholar 

  3. W.A. Bulen, J.R. Lecomte, and S. Lough, A hemoprotein from azotobacter containing non-heme iron: isolation and crystallization, Biochem. Biophys. Res. Commun. 54: 1274 (1974).

    Article  Google Scholar 

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

    PubMed  CAS  Google Scholar 

  5. G.R. Moore, S. Mann, and J.V. Bannister, Isolation and properties of the complex nonheme-iron-containing cytochrome b557.5 (bacterioferritin) from Pseudomonas aeruginosa, J. Inorg. Biochem. 28: 329 (1986).

    Article  PubMed  CAS  Google Scholar 

  6. B.W. Brooks, N.M. Young, D.C. Watson, R.H. Robertson, E.A. Sugden, K.H. Nielsen, and S.A.W.E. Becker, Mycobacterium paratuberculosis antigen D: characterization and evidence that it is a bacterioferritin, J. Clin. Micro. 29: 1652 (1991).

    CAS  Google Scholar 

  7. T. Kurokawa, Y. Fukumori, and T. Yamanaka, Nitrobacter winogradskyi cytochrome b-559: a nonhaem iron-containing cytochrome related to bacterioferritin , Biochem. Biophys. Acta 976: 135 (1989).

    Article  CAS  Google Scholar 

  8. J.-P. Laulhere, A.-M. Labouré, O. Van Wuytswinkel, J. Gagnon, J.-F. Briat, Purification, characterization and function of bacterioferritin from the cyanobacterium Synechocystis P.C.C. 6803, Biochem. J. 281: 783 (1992).

    Google Scholar 

  9. R.D. Perry, T.S. Lucher, D.J. Sikkema, and R.R. Brubaker, Storage reservoirs of hemin and inorganic iron in Yersinia pestis, Infect. Immun. 66: 32 (1993).

    Google Scholar 

  10. P.L. Ringeling, A.G. McEwan, and G.R. Moore, Bacterioferritin from the photosynthetic bacterium Rhodobacter capsulatus, Abstracts: 11th International Conference on Iron and Iron Proteins, Jerusalem, Israel (1993)

    Google Scholar 

  11. M. Izuhara, K. Takamune, and R. Takata, Cloning and sequencing of the Escherichia coli K12 gene which encodes a polypeptide having similarity to human ferritin H subunit, Mol. Gen. Genet. 225: 510 (1991).

    Article  PubMed  CAS  Google Scholar 

  12. E.D. Rocha, S.C. Andrews, J.N. Keen, and J.H. Brock, Isolation of a ferritin from Bacteroides fragilis, FEMS Microbiol. Lett. 95: 207 (1992).

    Article  CAS  Google Scholar 

  13. B.A. Frazier, J.D. Pfeifer, D.G. Russell, P. Falk, A.N. Olsen, M. Hammar, T.U. Westblom, and S.J. Normark, Paracrystalline inclusions of a novel ferritin containing nonheme iron produced by the human gastric pathogen Helicobactor pylori: evidence for a third class of ferritins, J. Bacteriol. 175: 966 (1993).

    PubMed  CAS  Google Scholar 

  14. P.M. Harrison, S.C. Andrews, P.T. Artymiuk, G.C. Ford, D.M. Lawson, J.M.A. Smith, A. Treffry, and J.L. White, Ferritin, in: “Iron Transport and Storage,” P. Ponka, H. M. Schulman, R.C. Woodworth, eds., CRC Press, Boca Raton (1990) p. 83.

    Google Scholar 

  15. M.J. Grosssman, S.M. Hinton, V. Minak-Bernero, C. Slaughter, and E.I. Stiefel, Unification of the ferritin family of proteins, Proc. Natl. Acad. Sci. USA 89: 2419 (1992).

    Article  Google Scholar 

  16. S.C. Andrews, J.M.A. Smith, S.J. Yewdall, J.R. Guest, and P.M. Harrison, Bacterio-ferritins and ferritins are distantly related in evolution: conservation of ferroxidase-center residues, FEBS Letters 293: 164 (1991).

    Article  PubMed  CAS  Google Scholar 

  17. G.R. Moore, Comparison of amino acid compositions suggest there may be sequence similarities between bacterial cytochromes b557.5 and eukaryotic ferritins, J Inorg. Biochem. 26: 143 (1986).

    Article  CAS  Google Scholar 

  18. D.L. Brutlag, J.P. Dautricourt, S. Maulik, J. Relph, Improved sensitivity of biological sequence database searches, Comp. App. Bio. Sci. 6: 237 (1990).

    CAS  Google Scholar 

  19. D.M. Lawson, A. Treffry, P.J. Artymiuk, P.M. Harrison, S.J. Yewdall, A. Luzzago, G. Cesareni, L Levi and P. Arosio, Identification of the ferroxidase centre in ferritin, FEBS Lett. 254: 207 (1989).

    Article  PubMed  CAS  Google Scholar 

  20. S.C. Andrews, P. Arosio, W. Bottke, J.-F. Briat, M. von Darl, P.M. Harrison, J.-P. Laulhère, S. Levi, S. Lobreaux, and S.J. Yewdall, Structure, function, and evolution of ferritins, J. Inorg. Biochem. 47: 161 (1992).

    Article  PubMed  CAS  Google Scholar 

  21. S.C. Andrews, P.M. Harrison, and J.R. Guest, Cloning, sequencing and mapping of the bacterioferritin gene of Escherichia coli K-12, J. Bacteriol. 171: 3940 (1989).

    PubMed  CAS  Google Scholar 

  22. J. Dietzel, J. Hirzmann, D. Preis, P Symmons, and W. Kunz, Ferritins of Schistosoma mansoni: sequence comparison and expression in female and male worms, Mol. Biochem. Parasitol. 50: 245 (1992).

    Article  PubMed  CAS  Google Scholar 

  23. A.M. Lescure, D. Proudhon, H. Pesey, M. Ragland, E.C. Theil, J.-F. Briat, Ferritin gene transcription is regulated by iron in soybean cell cultures, Proc. Natl. Acad. Sci. USA 88: 8222 (1991).

    Article  PubMed  CAS  Google Scholar 

  24. M.J. Spence, M.T. Henzel, and P.J. Lammers, The structure of Phaseolus vulgaris cDNA encoding the iron storage protein ferritin, Plant Mol. Biol. 17: 499 (1991).

    Article  PubMed  CAS  Google Scholar 

  25. D. Boyd, C. Vecoli, D.M. Belcher, W. K. Jain, and J. W. Drysdale, Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones, J. Biol. Chem. 260: 11755 (1985).

    PubMed  CAS  Google Scholar 

  26. Y. Miyazaki, M. Setoguchi, Y. Higuchi, S. Yoshida, S. Akizuke, and S. Yamamoto, Nucleotide sequence of cDNA encoding the heavy subunit of mouse macrophage ferritin, Nucleic Acids Res. 16: 10373 (1988).

    Article  PubMed  CAS  Google Scholar 

  27. P.W. Stevens, J.B. Dodgson, and J.D. Engel, Structure and expression of the chicken ferritin H-subunit gene, Molec. Cell Biol. 7: 1751 (1987).

    PubMed  CAS  Google Scholar 

  28. E.A. Leipold, N. Aziz, A.J.P. Brown, H.N. Munro, Conservation in rat liver of light and heavy subunit sequences of mammalian ferritin: presence of unique octapeptide in the light subunit, J. Biol. Chem. 259: 4327 (1984).

    Google Scholar 

  29. S. Daniels-McQueen, A. Ray, W.E. Walden, B.K. Ray, P.H. Brown, and R. H. Thach, Nucleotide sequence of cDNA encoding rabbit ferritin L chain, Nucl. Acids Res. 16: 7741 (1988).

    Article  PubMed  CAS  Google Scholar 

  30. M. Heusterspreute and R. R. Chrichton, Amino acid sequence of horse spleen apoferritin, FEBS Lett. 129: 322 (1981).

    Article  PubMed  CAS  Google Scholar 

  31. L.F. Dickey, S. Sreedharan, E.C. Theil, J.R. Didsbury, Y.-H. Wang, and R.E. Kaufman, Differences in the regulation of messenger RNA for housekeeping and specialized-cell ferritin: a comparison of three distinct ferritin complementary DNAs, the corresponding subunits, and identification of the first processed pseudogenes in amphibia, J. Biol. Chem. 262: 7901 (1987).

    PubMed  Google Scholar 

  32. J. Felsenstein, PHYLIP-Phylogeny Inference Package (Version 3.2), Cladistics 5: 164 (1989).

    Google Scholar 

  33. M.R. Cheesman, A.J. Thompson, C. Greenwood, G.R. Moore, and F.H.A. Kadir, Bis-methionine axial ligation of heme in bacterioferritin from Pseudomonas aeruginosa, Nature (London) 286: 361 (1990).

    Google Scholar 

  34. M.R. Cheesman, F.H.A. Kadir, J. Al-Basseet, F. Al Massad, J. Farrar, C. Greenwood, A.J. Thompson, and G.R. Moore, E.p.r. and magnetic circular dichroism spectroscopic characterization of bacterioferritin from Pseudomonas aeruginosa and Azotobacter vinelandii, Biochem. J. 286: 361 (1992

    PubMed  CAS  Google Scholar 

  35. G.N. George, T. Richards, R.E. Bare, Y. Gea, R.C. Prince, E.I. Stiefel, and G.D. Watt, Direct observation of bis-sulfur ligation to the heme of bacterioferritin, J. Am. Chem. Soc. in press.

    Google Scholar 

  36. J.M.A. Smith, G.C. Ford, P.M. Harrison, J. Yariv, A.J. Kalb (Gilboa) Molecular size and symmetry of the bacterioferritin of Escherichia coli: x-ray crystallographic characrterization of four crystal forms, J. Mol. Biol. 205: 465 (1989).

    Article  PubMed  CAS  Google Scholar 

  37. G.D. Watt, J.W. McDonald, C.-H. Chiu, and K.R. N. Reddy, Further characterization of the redox and spectroscopic properties of Azotobacter vinelandii ferritin, J. Inorg. Biochem. (1993) in press.

    Google Scholar 

  38. F.H.A. Kadir and G.R. Moore, Bacterial ferritin contains 24 heme groups, FEBS Lett. 271: 141 (1990).

    Article  PubMed  CAS  Google Scholar 

  39. K.M. Towe, Aerobic respiration in the archaean?, Nature (London) 348: 54 (1990).

    Article  CAS  Google Scholar 

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Stiefel, E.I. et al. (1994). Bacterioferritin: A Hemoprotein Member of the Ferritin Family. In: Hershko, C., Konijn, A.M., Aisen, P. (eds) Progress in Iron Research. Advances in Experimental Medicine and Biology, vol 356. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2554-7_18

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  • DOI: https://doi.org/10.1007/978-1-4615-2554-7_18

  • Publisher Name: Springer, Boston, MA

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