Abstract
Iron is perhaps the most essential inorganic element necessary for cell growth, and, acting as both donor and acceptor of electrons, has evolved as an integral cofactor and component of many proteins (Crichton and Ward 1992; Aisen 1994). Indeed, variability in the protein ligands coordinating iron can evoke a wide-ranging flexibility in redox potentials. Regulation of the amount of free intracellular iron is critical, and in mammals is mediated at several steps, including the uptake of iron by endocytosis of receptor-bound transferrin, and the storage of iron by ferritin within the cell (Baker and Morgan 1994). Insufficient iron will prevent cell division, whereas iron overload is toxic, due in large part to the potential for oxidative damage (Crichton 1991).
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References
Aisen P (1994) Iron metabolism: an evolutionary perspective. In: Brock JH, Halliday JW, Pippard MJ, Powell LW (ed) Iron metabolism in health and disease. Saunders, London, p 1
Aziz N, Munro HN (1987) Iron regulates ferritin mRNA translation through a segment of its 5´ untranslated region. Proc Natl Acad Sci USA 89: 8478–8482
Baker E, Morgan EH (1994) Iron transport. In: Brock JH, Halliday JW, Pippard MJ, Powell LW (ed) Iron metabolism in health and disease. Saunders, London, p 63
Barton HA, Eisenstein RS, Bomford A, Munro HN (1990) Determinants of the interaction between the iron-responsive element-binding protein and its binding site in rat L-ferritin mRNA. J Biol Chem 265: 7000–7008
Basilion JP, Rouault TA, Massinople CM, Klausner RD, Burgess WH (1994a) The iron-responsive element-binding protein: localization of the RNA-binding site to the aconitase active-site cleft. Proc Natl Acad Sci USA 91: 574–578
Basilion JP, Kennedy MC, Beinert H, Massinople CM, Klausner RD, Rouault TA (1994b) Overexpression of iron-responsive element-binding protein and its analytical characterization as the RNA-binding form, devoid of an iron-sulfur cluster. Arch Biochem Biophys 311: 517–522
Battiste JL, Tan R, Frankel AD, Williamson JR (1994) Binding of an HIV rev peptide to rev responsive element RNA induces formation of purine-purine base pairs. Biochemistry 33: 2741–2747
Beaumont C, Leneuve P, Devaux I, Scoazec J-Y, Berthier M, Loiseau M-N, Grandchamp B, Bonneau D (1995) Mutation in the iron responsive element of the L Ferritin mRNA in a family with dominant hyperferritinaemia and cataract. Nature Genet 11: 444–446
Beinert H, Kennedy MC (1993) Aconitase, a two-faced protein: enzyme and iron regulatory factor. FASEB J 7: 1442–1449
Bettany AJE, Eisenstein RS, Munro HN (1992) Mutagenesis of the iron-regulatory element further defines a role for RNA secondary structure in the regulation of ferritin and transferrin receptor expression. J Biol Chem 267: 16531–16537
Burd CG, Drey fuss G (1994) Conserved structures and diversity of functions of RNA-binding proteins. Science 265: 615–621
Cairo G, Pietrangelo A (1994) Transferrin receptor gene expression during rat liver regeneration: evidence for post-transcriptional regulation by iron regulatory factorB, a second iron-responsive element binding protein. J Biol Chem 269: 6405–6409
Cairo G, Tacchini L, Pogliaghi G, Anzon E, Tornasi A, Bernelli-Zazzera A (1995) Induction of ferritin synthesis by oxidative stress: transcriptional and post-transcriptional regulation by expansion of the free iron pool. J Biol Chem 270: 700–703
Casey JL, Hentze MW, Koeller DM, Caughman SW, Rouault TA, Klausner RD, Harford JB (1988) Iron-responsive elements: regulatory RNA sequences that control mRNA levels and translation. Science 240: 924–928
Casey JL, Koeller DM, Ramin VC, Klausner RD, Harford JB (1989) Iron regulation of transferrin receptor mRNA levels requires iron-responsive elements and a rapid turnover determinant in the 3´ untranslated region of the mRNA. EMBO J 8: 3693–3699
Cavarelli J, Rees B, Ruif M, Thierry J-C, Moras D (1993) Yeast tRNAAsp recognition by its cognate class II aminoacyl-tRNA synthetase. Nature 362: 181–184
Chu E, Koeller DM, Casey JL, Drake JC, Chabner BA, Elwood PC, Zinn S, Allegra CJ (1991) Autoregulation of human thymidylate synthase messenger RNA translation by thymidylate synthase. Proc Natl Acad Sci USA 88: 8977–8981
Chu E, Takimoto CH, Voeller D, Grem JL, Allegra CJ (1993) Specific binding of human dihy-dofolate reductase protein to dihydrofolate reductase messenger RNA in vitro. Biochemistry 32: 4756–4760
Chu E, Voeller DM, Morrison PF, Jones KL, Takechi T, Maley GF, Maley F, Allegra CJ (1994) The effect of reducing reagents on binding of thymidylate synthase protein to thymidylate synthase messenger RNA. J Biol Chem 269: 20289–20293
Chu E, Takechi T, Jones KL, Voeller DM, Copur SM, Maley GF, Maley FM, Segal S, Allegra CJ (1995) Thymidylate synthase binds to c-myc RNA in human colon cancer cells and in vitro. Mol Cell Biol 15: 179–185
Colvin RA, Garcia-Blanco MA (1992) Unusual structure of the human immunodeficiency virus type 1 trans -activation response element. J Virol 66: 930–935
Colvin RA, White SW, Garcia-Blanco MA, Hoffman DW (1993) Structural features of an RNA containing the CUGGGA loop of the human immunodeficiency virus type 1 trans -activation response element. Biochemistry 32: 1105–1112
Constable A, Quick S, Gray NK, Hentze MW (1992) Modulation of the RNA-binding activity of a regulatory protein by iron in vitro: switching between enzymatic and genetic function? Proc Natl Acad Sci USA 89: 4554–4558
Cox TC, Bawden MJ, Martin A, May BK (1991) Human erythroid 5-aminolevulinate synthase: promoter analysis and identification of an iron-responsive element in the mRNA. EMBO J 10: 1891–1902
Crichton RR (1991) Iron homeostasis and cellular iron release. In: Crichton RR (ed) Inorganic biochemistry of iron metabolism. Horwood, New York, p 163
Crichton RR, Ward RJ (1992) Iron metabolism — new perspectives in view. Biochemistry 31: 11255–11264
Dandekar T, Stripecke R, Gray NK, Goossen B, Constable A, Johansson HE, Hentze MW (1991) Identification of a novel iron-responsive element in murine and human erythroid 5-aminole-vulinic acid synthase mRNA. EMBO J 10: 1903–1909
DeRusso P, Philpott CC, Iwai K, Mostowski HS, Klausner RD, Rouault TA (1995) Expression of a constitutive mutant of iron regulatory protein 1 abolishes iron homeostasis in mammalian cells. J Biol Chem 270: 15451–15454
Dix DJ, Lin PN, McKenzie AR, Walden WE, Theil EC (1993) The influence of the base-paired flanking region on structure and function of the ferritin mRNA iron regulatory element. J Mol Biol 231: 230–240
Drapier J-C, Hiding H, Wietzerbin J, Kaldy P, Kühn LC (1993) Biosynthesis of nitric oxide activates iron regulatory factor in macrophages. EMBO J 12: 3643–3649
Eisenstein RS, Tuazon PT, Schalinske KL, Anderson SA, Traugh JA (1993) Iron-responsive element binding protein: phosphorylation by protein kinase C. J. Biol Chem 268: 27363–27370
Emery-Goodman A, Hiding H, Scarpellino L, Henderson B, Kühn LC (1993) Iron regulatory factor expressed from recombinant baculovirus: conversion between the RNA-binding apo-protein and Fe-S cluster containing aconitase. Nucl Acids Res 21: 1457–1461
Gait MJ, Karn J (1993) RNA recognition by the human immunodeficiency virus Tat and Rev proteins. Trends Biochem Sci 18: 255–259
Goessling LS, Daniels-McQueen S, Bhattacharyya-Pakrasi M, Lin JJ, Thach RE (1992) Enhanced degradation of the ferritin repressor protein during induction of ferritin messenger RNA translation. Science 256: 670–673
Goessling LS, Mascotti DP, Bhattacharyya-Pakrasi M, Gang H, Thach RE (1994) Irreversible steps in the ferritin synthesis induction pathway. J Biol Chem 269: 4343–4348
Goossen B, Hentze MW (1992) Position is the critical determinant for function of iron-responsive elements as translational regulators. Mol Cell Biol 12: 1959–1966
Goossen B, Caughman SW, Harford JB, Klausner RD, Hentze MW (1990) Translational repression by a complex between the iron-responsive element of ferritin mRNA and its specific cytoplasmic binding protein is position-dependent in vivo. EMBO J 9: 4127–4133
Guo B, Yu Y, Leibold EA (1994) Iron regulates cytoplasmic levels of a novel iron-responsive element-binding protein without aconitase activity. J Biol Chem 269: 24252–24260
Guo B, Brown FM, Phillips JD, Yu Y, Leibold EA (1995a) Characterization and expression of iron regulatory protein 2 (IRP2): presence of multiple IRP2 transcripts regulated by intracellular iron levels. J Biol Chem 270: 16529–16535
Guo B, Phillips JD, Yu Y, Leibold EA (1995b) Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome. J Biol Chem 270: 21645–21651
Haile DJ, Hentze MW, Rouault TA, Harford JB, Klausner RD (1989) Regulation of interaction of the iron-responsive element binding protein with iron-responsive elements. Mol Cell Biol 9: 5055–5061
Haile DJ, Rouault TA, Harford JB, Klausner RD (1990) The inhibition of the iron responsive element RNA-protein interaction by heme does not mimic in vivo iron regulation. J Biol Chem 265: 12786–12789
Haile DJ, Rouault TA, Tang CK, Chin J, Harford JB, Klausner RD (1992a) Reciprocal control of RNA-binding and aconitase activity in the regulation of the iron-responsive element binding protein: role of the iron-sulfur cluster. Proc Natl Acad Sci USA 89: 7536–7540
Haile DJ, Rouault TA, Harford JB, Kennedy MC, Blondin GA, Beinert H, Klausner RD (1992b) Cellular regulation of the iron-responsive element binding protein: disassembly of the cubane iron-sulfur cluster results in high-affinity RNA binding. Proc Natl Acad Sci USA 89: 11735–11739
Harrell CM, McKenzie AR, Patino MM, Walden WE, Theil EC (1991) Ferritin mRNA: Interactions of iron regulatory element with translational regulatory protein P-90 and the effect on base-paired flanking regions. Proc Natl Acad Sci USA 88: 4166–4170
Henderson BR, Kühn LC (1995) Differential modulation of the RNA-binding proteins IRP-1 and IRP-2 in response to iron: IRP-2 inactivation requires translation of another protein. J Biol Chem 270: 20509–20515
Henderson BR, Seiser C, Kühn LC (1993) Characterisation of a second RNA-binding protein in rodents with specificity for iron-responsive elements. J Biol Chem 268: 27327–27334
Henderson BR, Menotti E, Bonnard C, Kühn LC (1994) Optimal sequence and structure of iron responsive elements: selection of RNA stem-loops with high affinity for iron regulatory factor. J Biol Chem 269: 17481–17489
Henderson BR, Menotti E, Kühn LC (1996) Iron regulatory proteins -1 and -2 bind distinct sets of RNA target sequences. J Biol Chem 271: 4900–4908
Henry Y, Lepoivre M, Drapier J-C, Ducrocq C, Boucher J-L, Guissani A (1993) EPR characterization of molecular targets for NO in mammalian cells and organelles. FASEB J 7: 1124–1134
Hentze MW (1994) Enzymes as RNA-binding proteins: a role for (di)nucleotide-binding domains? Trends Biochem Sci 19: 101–103
Hentze MW, Argos P (1991) Homology between IRE-BP, a regulatory RNA-binding protein, aconitase, and isopropylmalate isomerase. Nucl Acids Res 19: 1739–1740
Hentze MW, Rouault TA, Caughman SW, Dancis A, Harford JB, Klausner RD (1987a) A cis -acting element is necessary for translational regulation of human ferritin expression in response to iron. Proc Natl Acad Sci USA 84: 6730–6734
Hentze MW, Caughman SW, Rouault TA, Barriocanal JG, Dancis A, Harford JB, Klausner RD (1987b) Identification of the iron-responsive element for the translational regulation of human ferritin mRNA. Science 238: 1570–1573
Hentze MW, Caughman SW, Casey JL, Koeller DM, Rouault TA, Harford JB, Klausner RD (1988) A model for the structure and functions of iron-responsive elements. Gene 72: 201–208
Hentze MW, Rouault TA, Harford JB, Klausner RD (1989) Oxidation-reduction as a molecular mechanism of a regulatory RNA-protein interaction. Science 244: 357–359
Hirling H, Emery-Goodman A, Thompson N, Neupert B, Seiser C, Kühn LC (1992) Expression of active iron regulatory factor from a full-length human cDNA by in vitro transcription/translation. Nucl Acids Res 20: 33–39
Hirling H, Henderson BR, Kühn LC (1994) Mutational analysis of the [4Fe-4S] cluster converting iron regulatory factor from its RNA-binding form to cytoplasmic aconitase. EMBO J 13: 453–461
Horowitz JA, Harford JB (1992) The secondary structure of the regulatory region of the transferrin receptor mRNA deduced by enzymatic cleavage. New Biol 4: 330–338
Iwai K, Klausner R, Rouault TA (1995) Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2. EMBO J 14: 5350–5357
Jaffrey SR, Haile DJ, Klausner RD, Harford JB (1993) The interaction between the iron-responsive element binding protein and its cognate RNA is highly dependent upon both RNA sequence and structure. Nucl Acids Res 24: 4627–4631
Kaptain S, Downey WE, Tang C, Philpott C, Haile D, Orloff DG, Harford JB, Rouault TA, Klausner RD (1991) A regulated RNA-binding protein also possesses aconitase activity. Proc Natl Acad Sci USA 88: 10109–10113
Kennedy MC, Mende-Mueller L, Blondin GA, Beinert H (1992) Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein. Proc Natl Acad Sci USA 89: 11730–11734
Kim H-Y, Klausner RD, Rouault TA (1995) Translational repressor activity is equivalent and is quantitatively predicted by in vitro RNA binding for two iron-responsive element-binding proteins, IRP1 and IRP2. J Biol Chem 270: 4983–4986
Kjems J, Brown M, Chang DD, Sharp PA (1991) Structural analysis of the interaction between the human immunodeficiency virus rev protein and the rev response element. Proc Natl Acad Sci USA 88: 683–687
Klausner RD, Rouault TA, Harford JB (1993) Regulating the fate of mRNA: the control of cellular iron metabolism. Cell 72: 19–26
Koeller DM, Casey JL, Gerhardt EM, Chan LN, Klausner RD, Harford JB (1989) A cytosolic protein binds to the structural elements within the iron regulatory region of the transferrin receptor mRNA. Proc Natl Acad Sci USA 86: 3574–3578
Kohler SA, Henderson BR, Kühn LC (1995) Succinate dehydrogenase b mRNA of Drosophila melanogaster has a functional iron-responsive element in its 5´-untranslated region. J Biol Chem 270: 30781–30786
Kühn LC (1994) Molecular regulation of iron proteins. In: Hershko C (ed) Baillière’s Clinical Haematology, vol 7. Baillière Tindall, London, pp 763–785
Kühn LC, Hentze MW (1992) Coordination of cellular iron metabolism by post-transcriptional gene regulation. J Inorg Biochem 47: 183–195
Lander HM, Levine DM, Novogrodsky A (1992) Hemin stimulation of cAMP production in human lymphocytes. FEBS Lett 303: 242–246
Leibold EA, Munro HN (1988) Cytoplasmic protein binds in vitro to a highly conserved sequence in the 5´ untranslated region of ferritin heavy and light subunit mRNAs. Proc Natl Acad Sci USA 85: 2171–2175
Leibold EA, Laudano A, Yu Y (1990) Structural requirements of iron-responsive elements for binding the protein involved in both transferrin receptor and ferritin mRNA post-transcriptional regulation. Nucl Acids Res 18: 1819–1824
Levine TD, Gao F-B, King PH, Andrews LG, Keene JD (1993) Hel-N1: an autoimmune RNA-binding protein with specificity for 3´ uridylate-rich untranslated regions of growth factor mRNAs. Mol Cell Biol 13: 3494–3504
Liau G, Chan LM, Feng P (1991) Increased ferritin gene expression is both promoted by cAMP and a marker of growth arrest in rabbit vascular smooth muscle cells. J Biol Chem 266: 18819–18826
Lim F, Spingola M, Peabody DS (1994) Altering the RNA binding specificity of a translational repressor. J Biol Chem 269: 9006–9010
Lin JJ, Patino MM, Gaffield L, Walden WE, Smith A, Thach RE (1991) Crosslinking of hemin to a specific site on the 90-kDa ferritin repressor protein. Proc Natl Acad Sci USA 88: 6068–6071
Malter JS, Hong Y (1991) A redox switch and phosphorylation are involved in the post-transcriptional up-regulation of the adenosine-uridine binding factor by phorbol ester and ionophore. J Biol Chem 266: 3167–3171
Müllner EW, Kühn LC (1988) A stem-loop in the 3´ untranslated region mediates iron-dependent regulation of transferrin receptor mRNA stability in the cytoplasm. Cell 58: 373–382
Müllner EW, Neupert B, Kühn LC (1989) A specific mRNA binding factor regulates the iron-dependent stability of cytoplasmic transferrin receptor mRNA. Cell 58: 373–382
Müllner EW, Rothenberger S, Müller AM, Kühn LC (1992) In vivo and in vitro modulation of the mRNA-binding activity of iron-regulatory factor: tissue distribution and effects of cell proliferation, iron levels and redox state. Eur J Biochem 208: 597–605
Nakagawa J, Waldner H, Meyer-Monard S, Hofsteenge J, Jeno P, Moroni C (1995) AUH, a gene encoding an AU-specific RNA binding protein with intrinsic enoyl-CoA hydratase activity. Proc Natl Acad Sci USA 92: 2051–2055
Neupert B, Thompson NA, Meyer C, Kühn LC (1990) A high affinity purification method for specific RNA-binding proteins: isolation of the iron regulatory factor from human placenta. Nucl Acids Res 18: 51–55
Neupert B, Menotti E, Kühn LC (1995) A novel method to identify nucleic acid-binding sites in proteins by scanning mutagenesis: application to iron regulatory protein. Nucl Acids Res 23: 2579–2583
Oubridge C, Ito N, Evans PR, Teo C-H, Nagai K (1994) Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature 372: 432–438
Pantopoulos K, Hentze MW (1995) Rapid responses to oxidative stress mediated by iron regulatory protein. EMBO J 14: 2917–2924
Pantopoulos K, Gray NK, Hentze MW (1995) Differential regulation of two related RNA-binding proteins, iron regulatory protein (IRP) and IRPB- RNA 1: 155–163
Patino MM, Walden WE (1992) Cloning of a functional cDNA for the rabbit ferritin mRNA repressor protein: demonstration of a tissue-specific pattern of expression. J Biol Chem 267: 19011–19016
Philpott CC, Rouault TA, Klausner RD (1991) Sequence and expression of the murine iron-responsive element binding protein. Nucl Acids Res 19: 6333
Philpott CC, Haile D, Rouault TA, Klausner RD (1993) Modification of a free Fe-S cluster cysteine residue in the active iron-responsive element binding protein prevents RNA binding. J Biol Chem 268: 17655–17658
Philpott CC, Klausner RD, Rouault TA (1994) The bifunctional iron-responsive element binding protein/cytosolic aconitase: the role of active site residues in ligand binding and regulation. Proc Natl Acad Sci USA 91: 7321–7325
Prodromou C, Artymiuk PJ, Guest JR (1992) The aconitase of Escherichia coli: nucleotide sequence of the aconitase gene and amino acid sequence similarity with mitochondrial aconitases, the iron-responsive element-binding protein and isopropylmalate isomerases. Eur J Biochem 204: 599–609
Robbins AH, Stout CD (1989) The structure of aconitase. Proteins 5: 289–312
Rogers JT, Andriotakis JL, Lacroix L, Durmowicz GP, Kasschau KD, Bridges KR (1994) Translational enhancement of H-ferritin mRNA by interleukin-lB acts through 5´ leader sequences distinct from the iron responsive element. Nucl Acids Res 22: 2678–2686
Rothenberger S, Müllner EW, Kühn LC (1990) The mRNA-binding protein which controls ferritin and transferrin receptor expression is conserved during evolution. Nucl Acids Res 18: 1175–1179
Rouault TA, Hentze MW, Caughman SW, Harford JB, Klausner RD (1988) Binding of a cytosolic protein to the iron-responsive element of human ferritin messenger RNA. Science 241: 1207–1210
Rouault TA, Tang CK, Kaptain S, Burgess WH, Haile DJ, Samaniego G, McBride OW, Harford JB, Klausner RD (1990) Cloning of the cDNA encoding an RNA regulatory protein — the human iron-responsive element-binding protein. Proc Natl Acad Sci USA 87: 7958–7962
Rouault TA, Stout CD, Kaptain S, Harford JB, Klausner RD (1991) Structural relationship between an iron-regulated RNA-binding protein (IRE-BP) and aconitase: functional implications. Cell 64: 881–883
Rouault TA, Haile DJ, Downey WE, Philpott CC, Tang C, Samaniego F, Chin J, Orloff D, Harford JB, Klausner RD (1992) An iron-sulfur cluster plays a novel regulatory role in the iron-responsive element binding protein. Biometals 5: 131–140
Rould MA, Perona JJ, Steitz TA (1991) Structural basis of anticodon loop recognition by gluta-minyl-tRNA synthetase. Nature 352: 213–218
Samaniego F, Chin J, Iwai K, Rouault T, Klausner RD (1994) Molecular characterization of a second iron-responsive element binding protein, iron regulatory protein 2: structure, function, and post-translational regulation. J Biol Chem 269: 30904–30910
Seiser C, Teixeira S, Kühn LC (1993) Interleukin-2-dependent transcriptional and post-transcriptional regulation of transferrin receptor mRNA. J Biol Chem 268: 13074–13080
Shaw G, Kamen R (1986) A conserved AU sequence from the 3´ untranslated region of GM-CSF mRNA mediates selective mRNA degradation. Cell 46: 659–667
Sierzputowska-Gracz H, McKenzie RA, Theil EC (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: 146–153
Swenson GR, Walden WE (1994) Localization of an RNA binding element of the iron responsive element binding protein within a proteolytic fragment containing iron coordination ligands. Nucl Acids Res 22: 2627–2633
Szewczak AA, Moore PB, Chan Y-L, Wool IG (1993) The conformation of the sarcin/ricin loop from 28S ribosomal RNA. Proc Natl Acad Sci USA 90: 9581–9585
Tang CK, Chin J, Harford JB, Klausner RD, Rouault TA (1992) Iron regulates the activity of the iron-responsive element binding protein without changing its rate of synthesis or degradation. J Biol Chem 267: 24466–24470
Teixeira S, Kühn LC (1991) Post-transcriptional regulation of the transferrin receptor and 4F2 antigen heavy chain mRNA during growth activation of spleen cells. Eur J Biochem 202: 819–826
Testa U, Kühn L, Petrin M, Quaranta MT, Pelosi E, Peschle C (1991) Differential regulation of iron regulatory element-binding protein(s) in cell extracts of activated lymphocytes versus monocytes-macrophages. J Biol Chem 266: 13925–13930
Theil EC (1994) Iron regulatory elements (IREs): a family of mRNA non-coding sequences. Biochem J 304: 1–11
Valegard K, Murray JB, Stockley PG, Stonehouse NJ, Liljas L (1994) Crystal structure of an RNA bacteriophage coat protein-operator complex. Nature 371: 623–626
Walden WE, Daniels-McQueen S, Brown PH, Gaffield L, Russell DA, Bielser D, Bailey LC, Thach RE (1988) Translational repression in eukaryotes: partial purification and characterisation of a repressor of ferritin mRNA translation. Proc Natl Acad Sci USA 85: 9503–9507
Wang Y-H, Sczekan SR, Theil EC (1990) Structure of the 5´ untranslated regulatory region of ferritin mRNA studied in solution. Nucl Acids Res 18: 4463–4468
Weiss G, Goossen B, Doppler W, Fuchs D, Pantopoulos K, Werner-Felmayer G, Wachter H, Hentze MW (1993) Translation regulation via iron-responsive elements by the nitric oxide/NO-synthase pathway. EMBO J 12: 3651–3657
Yu Y, Radisky E, Leibold EA (1992) The iron-responsive element binding protein: purification, cloning and regulation in rat liver. J Biol Chem 267: 19005–19010
Zhang W, Wagner BJ, Ehrenman K, Schaeifer AW, DeMaria CT, Crater D, DeHaven K, Long L, Brewer G (1993) Purification, characterization, and cDNA cloning of an AU-rich element RNA-binding protein, AUF1. Mol Cell Biol 13: 7652–7665
Zheng L, Kennedy MC, Blondin GA, Beinert H, Zalkin H (1992) Binding of cytosolic aconitase to the iron responsive element of porcine mitochondrial aconitase mRNA. Arch Biochem Biophys 299: 356–360
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Henderson, B.R., Kühn, L.C. (1997). Interaction Between Iron-Regulatory Proteins and Their RNA Target Sequences, Iron-Responsive Elements. In: Jeanteur, P. (eds) Cytoplasmic fate of messenger RNA. Progress in Molecular and Subcellular Biology, vol 18. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-60471-3_6
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