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Translational Regulation of Bioiron

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Metal Ions in Gene Regulation

Part of the book series: Chapman & Hall Microbiology Series ((CHMBS))

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Abstract

Iron is central to respiration, photosynthesis, nitrogen fixation, and, in most organisms, the reduction of ribose to deoxyribose, rate limiting in DNA synthesis. Dioxygen, which allows high-efficiency bioenergetics, at the same time converts soluble ferrous ions to insoluble ferric ions; iron concentrations in cells are almost a trillion times the solubility of the free ferric ion under physiological conditions. Ferritin is the protein that concentrates ferric iron in all known organisms [reviewed in Theil (1987, 1990) Waldo and Theil (1996) Harrison and Lilley (1990)]. Induction of ferritin synthesis by iron also protects cells from oxidant stress (Balla et al. 1992). Gene regulation of ferritin synthesis is precise and complex and, in animals, is coordinately regulated with transferrin receptor (TfR) synthesis [reviewed in Theil (1990, 1993, 1994, 1997) Hentze and Kuhn (1996) Rouault and Klausner (1996) Klausner et al. (1993) Munro (1990)]. The problem of acquiring and concentrating iron is solved by the use of environmental iron to regulate expression of both iron-storage (ferritin) and iron-uptake (TfR) genes; changes in expression of ferritin and TfR are also regulated by growth factors and hormones and during cell differentiation.

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References

  • Aziz, N. and H. N. Munro. 1987. Iron regulates ferritin mRNA translation through a segment of its 5’-untranslated region. Proc. Natl. Acad. Sci. U.S.A. 84:8478–8482.

    Article  PubMed  CAS  Google Scholar 

  • Balla G., H. S. Jacob, J. Balla, M. Rosenberg, K. Nath, F. Apple, J. W. Eaton, and G. M. Vercellotti. 1992. Ferritin: A cytoprotective antioxidant stratagem of endothelium. J. Biol. Chem. 267:18148–18153.

    PubMed  CAS  Google Scholar 

  • Beelman C. A., and R. Parker. 1995. Degradation of RNA in eukaryotes. Cell 81:179–183.

    Article  PubMed  CAS  Google Scholar 

  • Beinert H., and M. C. Kennedy. 1989. Engineering of protein bound iron-sulfur clusters. Eur. J. Biochem. 186:5–15.

    Article  PubMed  CAS  Google Scholar 

  • Bhasker C. R., G. Burgil, B. Neupert, A. Emery-Goodman, L. C. Kuhn, and B. K. May. 1993. The putative iron-responsive element in the human erythroid 5-aminolevulinate synthase mRNA mediates translational control. J Biol. Chem. 268:12669–12705.

    Google Scholar 

  • Binder R., J. A. Horowitz, J. B. Basilion, D. M. Koeller, R. D. Klausner, and J. B. Harford. 1994. Evidence that the pathway of transferrin receptor mRNA degradation involves an endonucleolytic cleavage within the 3’ UTR and does not involve polyA tail shortening. EMBO J. 18:1969–1980.

    Google Scholar 

  • Brown J. E., and E. C. Theil. 1977. Red cells, ferritin and iron storage during amphibian development. J. Biol Chem. 253:2673–2678.

    Google Scholar 

  • Butts J., H.-Y. Kim, J. P. Basilion, S. Cihenm, K. Iwai, C. C. Philpott, S. Altschul, R. D. Klausner, T. A. Rousault. 1996. Differences in the RNA binding sites of iron regulatory proteins and potential target diversity. Proc. Natl. Acad. Sci. 93:4345–4349.

    Article  Google Scholar 

  • Carter B. J., E. deVroom, E. C. Long, G. A. Van der Marl, J. H. Van Boom, and S. M. Hecht. 1990. Site-specific cleavage of RNA by Fe(II) bleomycin. Proc. Natl Acad. Sci. U.S.A. 87:9373–9377.

    Article  PubMed  CAS  Google Scholar 

  • Casey J. L., M. W. Hentze, D. M. Koeller, S. W. Caughman, T. A. Rouault, R. D. Klausner, and J. B. Harford. 1988. Iron responsive elements: Regulatory RNA sequences that control mRNA levels and translation. Science 240:924–928.

    Article  PubMed  CAS  Google Scholar 

  • Casey J. L., D. M. Koeller, V. C. Ramin, R. D. Klausner, and J. B. Harford. 1989. Iron regulation of transferrin receptor levels requires iron-responsive elements and a rapid turnover in the 3'-untranslated region of the mRNA. EMBO J. 8:3693–3699.

    PubMed  CAS  Google Scholar 

  • Cox, T. C, M. J. Bawden, A. Martin, and B. K. May. 1991. Human erythroid 5-aminolevul-nate synthase: Promoter analysis and identification of an iron-responsive element in the mRNA. EMBO J. 10:1891–1902.

    PubMed  CAS  Google Scholar 

  • Dandekar T., R. Stripecke, N. K. Gray, B. Goossen, A. Constable, H. E. Johansson, and M. W. Hentze. 1991. Identification of a novel iron-responsive element in murine and human erythroid delta aminolevulinic acid synthease mRNA. EMBO J. 10:1903–1909.

    PubMed  CAS  Google Scholar 

  • Diamond M. I., J. N. Miner, S. K. Yoshinagu, and K. R. Yamamato. 1990. Transcription factor interactions: Selectors of positive or negative regulation from a single DNA element. Science 249:1266–1272.

    Article  PubMed  CAS  Google Scholar 

  • Dickey L. F., Y.-H. Wang, G. E. Shull, I. A. Wortmann III, and E. C. Theil. 1988. The importance of the 3/-untranslated region in the translational control of ferritin mRNA. J. Biol. Chem. 263:3071–3074.

    PubMed  CAS  Google Scholar 

  • Didsbury J. R., E. C. Theil, R. E. Kaufman, and L. F. Dickey. 1986. Multiple red cell ferritin mRNAs, which code for an abundant protein in the embryonic cell type, analyzed by cDNA sequence and by primer extension of the 5’-untranslated regions. J. Biol Chem. 261:949–95

    PubMed  CAS  Google Scholar 

  • Dix D. J., P. N. Lin, Y. Kimata, and E. C. Theil. 1992. The iron regulatory region (IRE) of ferritin mRNA is also a positive control element for iron-independent translation. Biochem. 31:2818–2822.

    Article  CAS  Google Scholar 

  • Dix D. J., P. N. Lin, A. R. McKenzie, W. E. Walden, and E. C. Theil. 1993. The influence of the base-paired flanking region (FL) on structure and function of the ferritin mRNA iron regulatory element (IRE). J. Mol. Biol. 231:230–240.

    Article  PubMed  CAS  Google Scholar 

  • Eisenstein R. S., P. T. Tuazon, K. L. Schalinske, S. A. Anderson, and J. A. Traugh. 1993. Iron-responsive element-binding protein. J. Biol. Chem. 268:27363–27370.

    PubMed  CAS  Google Scholar 

  • Gallie D. R., and R. Tanquay. 1994. Poly(a) binds to initiation factors and increases cap-dependent translation in vitro. J. Biol. Chem. 269:17166–17173.

    PubMed  CAS  Google Scholar 

  • Goessling L. S., S. Daniels-McQueen, M. Chattaacharayya-Pakrasi, J.-J. Lin, and R. E. Thach. 1992. Enhanced degradation of the ferritin repressor protein during induction of ferritin repressor protein during induction of ferritin messenger RNA translation. Science 256:670–673.

    Article  PubMed  CAS  Google Scholar 

  • Green, P. J. 1993. Control of mRNA stability in higher plants. Plant Physiol. 102:1065–1070.

    PubMed  CAS  Google Scholar 

  • Guo B., Y. Yu, and E. A. Leibold. 1994. Iron regulates cytoplasmic levels of a novel iron-responsive element-binding protein without aconitase activity. J. Biol. Chem. 268:24252–2426

    Google Scholar 

  • Haile D. J., T. A. Rouault, J. B. Harford, M. C. Kennedy, G. A. Blondin, H. Beinert, and R. D. Klausner. 1992. Cellular recognition of the iron-responsive element binding protein: Dissembly of the cubane iron-sulfur cluster results in high affinity RNA binding. Proc. Natl. Acad. Sci. 89:11735–11739.

    Article  PubMed  CAS  Google Scholar 

  • Harrell C. M., A. R. McKenzie, M. M. Patino, W. E. Walden, and E. C. Theil. 1991. Ferritin mRNA: Interactions of iron regulatory element (IRE) with the translational regulatory protein (P-90) and the effect on base-paired flanking regions. Proc. Natl. Acad. Sci. U.S.A. 88:4166–4170.

    Article  PubMed  CAS  Google Scholar 

  • Harrison P. M., and T. H. Lilley. 1990. Ferritin. In Iron Carriers and Iron Proteins,ed. T. M. Loller. pp. 353–452. VCH Weinheim, New York.

    Google Scholar 

  • Hecht, S. M. 1994. RNA degradation by bleomycin, a naturally occurring bioconjugate. Bioconjugate Chemistry 5:513–526.

    Article  PubMed  CAS  Google Scholar 

  • Henderson B. R., E. Menotti, C. Bonnard, and L. C. Kuhn. 1994. Optimal sequence and structure of iron responsive elements. J. Biol. Chem. 269:17481–17489.

    PubMed  CAS  Google Scholar 

  • Hentze M. W., S. W. Caughman, T. A. Rouault, J. G. Barriocanal, A. Dancis, J. B. Harford, and R. D. Klausner. 1987. Identification of the iron-responsive element for the translational regulation of human ferritin mRNA. Science 238:1570–1573.

    Article  PubMed  CAS  Google Scholar 

  • Hentze M. W., and L. C. Kuhn. 1996. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide and oxidative stress. Proc. Natl. Acad. Sci. 93:8175–8182.

    Article  PubMed  CAS  Google Scholar 

  • Herrick D. J., and J. Ross. 1994. The half-life of c-myc mRNA in growing and serum-stimulated cells: Influence of the coding and 3’ untranslated regions and role of ribosome translocation. Mol. Cell. Biol. 14:2119–2128.

    PubMed  CAS  Google Scholar 

  • Iwai K., R. D. Klausner, and T. A. Rouault. 1995. Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein-2. EMBO J. 14:5350–5367.

    PubMed  CAS  Google Scholar 

  • Kaptain S., W. E. Downey, C. Tang, C. Philpott, D. Haile, D. Orloff, J. B. Harford, T. A. Rouault, and R. D. Klausner. 1991. A regulated RNA binding protein also possesses aconitase activity. Proc. Natl. Acad. Sci. U.S.A. 88:10109–10113.

    Article  PubMed  CAS  Google Scholar 

  • Kennedy M. C., L. Mend-Mueller, G. A. Blondin, and H. Beinert. 1992. Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein. Proc. Natl. Acad. Sci. 89:11730–11734.

    Article  PubMed  CAS  Google Scholar 

  • Kimata Y., and E. C. Theil. 1994. Posttranslational regulation of ferritin during nodule development in soybean. Plant Physiol. 104:263–270.

    Article  PubMed  CAS  Google Scholar 

  • Klausner R. D., T. A. Rouault, and J. B. Harford. 1993. Regulating the rate of mRNA: The control of cellular iron metabolism. Cell 72:19–29.

    Article  PubMed  CAS  Google Scholar 

  • Koeller D. M., J. A. Horowitz, J. L. Casey, R. D. Klausner, and J. B. Harford. 1991. Translation and the stability of mRNAs encoding the transferrin receptor and c-fos. Proc. Natl. Acad. Sci. U.S.A. 88:7778–7782.

    Article  PubMed  CAS  Google Scholar 

  • Kohler S. A., B. R. Henderson, and L. C. Kuhn. 1995. Succinic dehydrogenase b mRNA of Drosophila melanogaster has a functional iron-responsive element of the 5’ untranslated region. J. Biol. Chem. 270:30781–30786.

    Article  PubMed  CAS  Google Scholar 

  • Kohler S. A., B. R. Henderson, and L. C. Kuhn. 1996. Translational regulation of mammalilan and Drosophila citric acid cycle enzymes via iron-responsive elements. Proc. Natl. Acad. Sci. U.S.A.

    Google Scholar 

  • Lescure A. M., D. Proudhon, H. Pesey, M. Ragland, E. C. Theil, and J. F. Briat. 1991. Ferritin gene transcription is regulated by iron in soybean cell cultures. Proc. Natl. Acad. Sci. U.S.A. 88:8222–8226.

    Article  PubMed  CAS  Google Scholar 

  • Lin, J.-J., M. M. Patino, L. Gaffield, W. E. Walden, A. Smith, and R. E. Thach. 1991. Crosslinking of hemin to a specific site on the 90-kDa ferritin repressor protein. Proc. Natl. Acad. Sci. U.S.A. 88:6068–6071.

    Article  PubMed  CAS  Google Scholar 

  • Mascotti D. P., Rup D., and Thach, R. E. Regulation of Iron Metabolism: Translational Effects Mediated by Iron, Heme, and Cytokines. Annu. Rev. Nutr., 1995. 15. p. 239–261.

    Google Scholar 

  • Melefors O., B. Goossen, H. E. Johansson, R. Stripecke, N. K. Gray, and M. W. Hentze. 1993. Translational control of 5-aminolevulinate synthase mRNA by iron-responsive elements in erythroid cells. J. Biol. Chem. 268:5974–5978.

    PubMed  Google Scholar 

  • Mullner E. W., and L. C. Kuhn. 1988. A region in the 3’ untranslated region mediates iron dependent regulation of transferrin receptor mRNA stability in the cytoplasm. Cell 53:815–825.

    Article  PubMed  CAS  Google Scholar 

  • Munro, H. N. 1990. Iron regulation of ferritin gene expression. J. Cell. Biochem. 44:107–115.

    Article  PubMed  CAS  Google Scholar 

  • Murray E. E., T. Rocheleau, M. Eberle, C. Stock, V. Sekar, and M. Adang. 1991. Analysis of unstable RNA transcripts of insecticidal crystal protein genes of Bacillus thuringiensis in transgenic plants and electroporated protoplasts. Plant Mol Biol. 16:1035–1050.

    Article  PubMed  CAS  Google Scholar 

  • Owen D., and L. C. Kuhn. 1987. Noncoding 3’ sequences of the transferrin receptor gene are required for mRNA regulation by iron. EMBO J. 6:1287–1293.

    PubMed  CAS  Google Scholar 

  • Pantopoulos K., and M. W. Hentze. 1995. Nitric oxide signaling to iron-regulatory protein: Direct control of ferritin mRNA translation and transferrin receptor mRNA stability in transfected fibroblasts. Proc. Natl. Acad. Sci. U.S.A. 92:1267–1271.

    Article  PubMed  CAS  Google Scholar 

  • Patino M. M., and W. E. Walden. 1992. Cloning of a functional cDNA for the rabbit ferritin mRNA repressor proteins: Demonstration of a tissue-specific pattern of expression. J. Biol. Chem. 267:19011–19016.

    PubMed  CAS  Google Scholar 

  • Proudhon D., J. Wei, J.-F. Briat, and E. C. Theil. 1996. Ferritin gene organization: Differences between plants and animals suggest possible kingdom-specific selective constraints. J. Mol. Evol. 42:325–336.

    Article  PubMed  CAS  Google Scholar 

  • Ragland M., J.-F. Briat, J. Gagnon, J.-P. Laulhere, O. Massenet, and E. C. Theil. 1990. Evidence for conservation of ferritin sequences among plants and animals and for a transit peptide in soybean. J. Biol. Chem. 263:18339–18344.

    Google Scholar 

  • Ragland, M. and E. C. Theil. 1993. Ferritin and iron are developmentally regulated in nodules. Plant Mol. Biol. 21:555–560.

    Article  PubMed  CAS  Google Scholar 

  • Rothenberger S., E. W. Mullner, and L. C. Kuhn. 1990. The mRNA-binding protein which controls ferritin and transferritin receptor expression is conserved during evolution. Nucl. Acids Res. 18:1175–1179.

    Article  PubMed  CAS  Google Scholar 

  • Rouault T. A., M. A. Hentze, D. J. Haile, J. B. Harford, and R. D. Klausner. 1989. The iron-responsive element binding protein: A method for affinity purification of a regulatory RNA-binding protein. Proc. Natl. Acad. Sci. 86:5718–5722.

    Article  Google Scholar 

  • Rouault T. A., Klausner R. D., Post-transcriptional regulation of genes of iron metabolism in mammalian cells. J. Biol. Inorg. Chem., 1996, 1. p. 494–499.

    Google Scholar 

  • Rouault T. A., C. D. Stout, S. Kaptain, J. B. Harford, R. D. Klausner. 1991. Structural relationship between iron-regulated RNA-binding protein (IRE-BP) and aconitase: Functional implications. Cell 64:881–883.

    Article  PubMed  CAS  Google Scholar 

  • Rouault T. A., C. K. Tang, S. Kaptain, W. H. Burgeess, D. J. Haile, F. Samniego, O. W. McBride, J. B. Harford, and R. D. Klausner. 1990. Cloning of the cDNA encoding an RNA regulatory proteins—The human iron-responsive element binding protein. Proc. Natl. Acad. Sci. U.S.A. 87:7958–7962.

    Article  PubMed  CAS  Google Scholar 

  • Samaniego F., J. Chin, K. Iwai, T. A. Rouault, and R. D. Klausner. 1994. Molecular characterization of a second iron responsive element binding protein (IRP2): Structure, function and posttranslational regulation. J. Biol. Chem. 269:30904–30910.

    PubMed  CAS  Google Scholar 

  • Schaefer F. V., and E. C. Theil. 1981. The effect of iron on the synthesis and amoun of ferritin in red blood cells during ontogeny. J. Biol. Chem. 256:1711–1715.

    PubMed  CAS  Google Scholar 

  • Schalinske K. L., and R. S. Eisenstein. 1996. Phosphorylation and activation of both iron regulatory proteins 1 and 2 in HL-60 cells. J. Biol. Chem. 271:7168–7176.

    Article  PubMed  CAS  Google Scholar 

  • Shull G. E., and E. C. Theil. 1982. Translational control of ferritin synthesis by iron in embryonic reticulocytes of the bullfrog. J. Biol. Chem. 257:14187–14191.

    PubMed  CAS  Google Scholar 

  • Shull G. E., and E. C. Theil. 1983. Regulation of ferritin mRNA: A possible gene-sparing phenomenon. J. Biol. Chem. 258:7921–7923.

    PubMed  CAS  Google Scholar 

  • Sierzputowska-Gracz H., R. A. McKenzie, and E. C. Theil. 1995. The importance of a single G in the hairpin loop of the iron responsive element (IRE) in ferritin mRNA for structure: An NMR spectroscopy study. Nucl. Acids Res. 23:145–152.

    Article  Google Scholar 

  • Theil, E. C. 1973. Red cell ferritin content during the hemoglobin transition of amphibian metamorphosis. Dev. Biol. 34:282–288.

    Article  PubMed  CAS  Google Scholar 

  • Theil, E. C. 1976. The abundance of ferritin in yolk-sac derived red blood cells of the embryonic mouse. Brit. J. Haem. 33:437–442.

    Article  CAS  Google Scholar 

  • Theil, E. C. 1981. Red cell ferritin and iron storage during the early hemoglobin switch. In Hemoglobins in Development and Differentiation,eds. A. Nienhuis and G. Stamatoyannopoulis. pp. 423–431. Alan R. Liss, New York.

    Google Scholar 

  • Theil, E. C. 1987. Storage and translation of ferritin messenger RNA. In Translational Regulation of Gene Expression,ed. J. Ilan. pp. 141–163. Plenum Press, New York.

    Chapter  Google Scholar 

  • Theil, E. C. 1987. Ferritin: Structure, gene regulation, and cellular function in animals, plants, and microorganisms. Ann. Rev. Biochem. 56:289–315.

    Article  PubMed  CAS  Google Scholar 

  • Theil, E. C. 1990. The ferritin family of iron storage proteins. Adv. Enzymol. 63:421–449.

    PubMed  CAS  Google Scholar 

  • Theil, E. C. 1990. Regulation of ferritin and transferrin receptor (TR) mRNAs. J. Biol. Chem. 265:4771–4774.

    PubMed  CAS  Google Scholar 

  • Theil, E. C. 1993. The IRE (iron regulatory element) family: Structures which regulate mRNA translation and stability. Biofactors 4:87–93.

    PubMed  CAS  Google Scholar 

  • Theil, E. C. 1994. IREs, a family of composite mRNA regulatory elements. Biochem. J. 304:1–11.

    PubMed  Google Scholar 

  • Theil, E. C. 1994. Transition metal coordination complexes as probes of mRNA structure: The IRE (iron regulatory element) of ferritin mRNA as a case study. New J. Chemistry 18:435–441.

    CAS  Google Scholar 

  • Theil, E. C. 1998. The Iron Responsive Element (IRE) family of mRNA Regulators in Sigel, E. and Sigel H., eds. Metal Ions in Biological Systems, Volume 35: Iron Transport and Storage in Microorganisms, Plants and Animals. Marcel Dekker, New York, (in press).

    Google Scholar 

  • Theil, E. C, and W. E. Brenner. 1981. The ferritin content of human red blood cells during the replacement of embryonic cells by fetal cells. Dev. Biol. 84:481–484.

    Article  PubMed  CAS  Google Scholar 

  • Theil, E. C, and G. M. Tosky. 1979. Red cell ferritin and iron storage during chick embryonic development. Dev. Biol. 69:666–672.

    Article  PubMed  CAS  Google Scholar 

  • Thorp H. H., R. A. McKenzie, P.-N. Lin, W. E. Walden, and E. C. Theil. 1996. Cleavage of functionally relevant sites in ferritin mRNA by oxidizing metal complexes. Inorg. Chem. 35:2773–2779.

    Article  CAS  Google Scholar 

  • Vogel W., D. A. Richert, B. Q. Pixley, and M. P. Schulman. 1960. Heme synthesis in iron-deficient duck blood. J. Biol. Chem. 235:1769–1775.

    CAS  Google Scholar 

  • Von Darl M., P. M. Harrison, W. Bottke. 1994. cDNA cloning and deduced amino acid sequence of two ferritins: soma ferritin and yolk ferritin, from the snail Lymnaea stagnalisL. Eur. J. Biochem. 222:353–366.

    Article  Google Scholar 

  • Walden W. E., M. H. Patino, and L. Gaffield. 1989. Purification of a specific repressor of ferritin mRNA translation from rabbit liver. J. Biol. Chem. 264:13765–13769.

    PubMed  CAS  Google Scholar 

  • Walden W. E., and R. E. Thach. 1986. Translational control of gene expression in a normal fibroblast characterization of a subclass of mRNAs with unusual kinetic properties. Biochem. 25:2003–2041.

    Article  Google Scholar 

  • Waldo G. S., and E. C. Theil. 1996. Ferritin and iron biomineralization. In Comprehensive Supramolecular Chemistry, Vol. 5, Bioinorganic Systems,vol. ed. K. S. Suslick. pp. 65–89. Pergamon Press, Oxford, U.K.

    Google Scholar 

  • Wang, Y.-H., P.-N. Lin, S. R. Sczekan, R. A. McKenzie, and E. C. Theil. 1991. Ferritin mRNA probed, near the iron regulatory region (IRE), with protein and chemical (1,10-penanathroline-Cu) nucleases: A possible role for base-paired flanking regions. Biol. Metals 4:56–61.

    Article  CAS  Google Scholar 

  • Wang, Y.-H., S. R. Sczekan, and E. C. Theil. 1990. Structure of the 5’ untranslated regulatory region of ferritin mRNA studies in solution. Nucl Acids Res. 18:4463–4468.

    Article  PubMed  CAS  Google Scholar 

  • Weiss G., B. Goossen, W. Dopple, D. Fuchs, K. Pantopoulos, G. Werner-Felmayer, H. Wachter, and M. W. Hentze. 1993. Translational regulation via iron-responsive elements by the nitric oxide/NO-synthase pathway. EMBO J. 12:3651–3657.

    PubMed  CAS  Google Scholar 

  • Yu Y., E. Radisky, and E. A. Leibold. 1992. The iron-responsive element binding protein: Purification, cloning and regulation in rat. J. Biol Chem. 267:19005–19010.

    PubMed  CAS  Google Scholar 

  • Zahringer J., B. S. Baliga, and H. N. Munro. 1976. Novel mechanisms for translational control in regulation of ferritin synthesis by iron. Proc. Natl. Acad. Sci. 73:857–861.

    Article  PubMed  CAS  Google Scholar 

  • Zheng L., M. C. Kennedy, G. A. Blondin, H. Beinert, and H. Zalkin. 1992. Arch. Biochem. Biophys. 299:356–360.

    Article  PubMed  CAS  Google Scholar 

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Theil, E.C. (1998). Translational Regulation of Bioiron. In: Silver, S., Walden, W. (eds) Metal Ions in Gene Regulation. Chapman & Hall Microbiology Series. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5993-1_6

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