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. 1987 May;7(5):1751–1758. doi: 10.1128/mcb.7.5.1751

Structure and expression of the chicken ferritin H-subunit gene.

P W Stevens, J B Dodgson, J D Engel
PMCID: PMC365276  PMID: 3600643

Abstract

Although the genomes of many species contain multiple copies of ferritin heavy (H)- and light (L)-chain sequences, the chicken genome contains only a single copy of the H-subunit gene. The primary transcription unit of this gene is 4.6 kilobase pairs and contains four exons which are posttranscriptionally spliced to generate a mature transcript of 869 nucleotides. Chicken and human ferritin H-subunit genomic loci are organized with similar exon-intron boundaries. They exhibit approximately 85% nucleotide identity in coding regions, which yield proteins 93% identical in amino acid sequence. We have identified a sequence of 22 highly conserved nucleotides in the 5' untranslated sequences of chicken, human, and tadpole ferritin H-subunit genes and propose that this conserved sequence may regulate iron-modulated translation of ferritin H-subunit mRNAs.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Akiyama Y., Kato S. Two cell lines from lymphomas of Marek's disease. Biken J. 1974 Sep;17(3):105–116. [PubMed] [Google Scholar]
  2. Arosio P., Adelman T. G., Drysdale J. W. On ferritin heterogeneity. Further evidence for heteropolymers. J Biol Chem. 1978 Jun 25;253(12):4451–4458. [PubMed] [Google Scholar]
  3. Aviv H., Leder P. Purification of biologically active globin messenger RNA by chromatography on oligothymidylic acid-cellulose. Proc Natl Acad Sci U S A. 1972 Jun;69(6):1408–1412. doi: 10.1073/pnas.69.6.1408. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Aziz N., Munro H. N. Both subunits of rat liver ferritin are regulated at a translational level by iron induction. Nucleic Acids Res. 1986 Jan 24;14(2):915–927. doi: 10.1093/nar/14.2.915. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Beug H., Palmieri S., Freudenstein C., Zentgraf H., Graf T. Hormone-dependent terminal differentiation in vitro of chicken erythroleukemia cells transformed by ts mutants of avian erythroblastosis virus. Cell. 1982 Apr;28(4):907–919. doi: 10.1016/0092-8674(82)90070-8. [DOI] [PubMed] [Google Scholar]
  6. Boyd D., Vecoli C., Belcher D. M., Jain S. K., Drysdale J. W. Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones. J Biol Chem. 1985 Sep 25;260(21):11755–11761. [PubMed] [Google Scholar]
  7. Breathnach R., Chambon P. Organization and expression of eucaryotic split genes coding for proteins. Annu Rev Biochem. 1981;50:349–383. doi: 10.1146/annurev.bi.50.070181.002025. [DOI] [PubMed] [Google Scholar]
  8. Brown A. J., Leibold E. A., Munro H. N. Isolation of cDNA clones for the light subunit of rat liver ferritin: evidence that the light subunit is encoded by a multigene family. Proc Natl Acad Sci U S A. 1983 Mar;80(5):1265–1269. doi: 10.1073/pnas.80.5.1265. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Brush D., Dodgson J. B., Choi O. R., Stevens P. W., Engel J. D. Replacement variant histone genes contain intervening sequences. Mol Cell Biol. 1985 Jun;5(6):1307–1317. doi: 10.1128/mcb.5.6.1307. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Choi O. R., Trainor C., Graf T., Beug H., Engel J. D. A single amino acid substitution in v-erbB confers a thermolabile phenotype to ts167 avian erythroblastosis virus-transformed erythroid cells. Mol Cell Biol. 1986 May;6(5):1751–1759. doi: 10.1128/mcb.6.5.1751. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Chou C. C., Gatti R. A., Fuller M. L., Concannon P., Wong A., Chada S., Davis R. C., Salser W. A. Structure and expression of ferritin genes in a human promyelocytic cell line that differentiates in vitro. Mol Cell Biol. 1986 Feb;6(2):566–573. doi: 10.1128/mcb.6.2.566. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Costanzo F., Colombo M., Staempfli S., Santoro C., Marone M., Frank R., Delius H., Cortese R. Structure of gene and pseudogenes of human apoferritin H. Nucleic Acids Res. 1986 Jan 24;14(2):721–736. doi: 10.1093/nar/14.2.721. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Costanzo F., Santoro C., Colantuoni V., Bensi G., Raugei G., Romano V., Cortese R. Cloning and sequencing of a full length cDNA coding for a human apoferritin H chain: evidence for a multigene family. EMBO J. 1984 Jan;3(1):23–27. doi: 10.1002/j.1460-2075.1984.tb01756.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Didsbury J. R., Theil E. C., Kaufman R. E., Dickey L. F. 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. 1986 Jan 15;261(2):949–955. [PubMed] [Google Scholar]
  15. Dodgson J. B., Strommer J., Engel J. D. Isolation of the chicken beta-globin gene and a linked embryonic beta-like globin gene from a chicken DNA recombinant library. Cell. 1979 Aug;17(4):879–887. doi: 10.1016/0092-8674(79)90328-3. [DOI] [PubMed] [Google Scholar]
  16. Dolan M., Dodgson J. B., Engel J. D. Analysis of the adult chicken beta-globin gene. Nucleotide sequence of the locus, microheterogeneity at the 5'-end of beta-globin mRNA, and aberrant nuclear RNA species. J Biol Chem. 1983 Mar 25;258(6):3983–3990. [PubMed] [Google Scholar]
  17. Dörner M. H., Salfeld J., Will H., Leibold E. A., Vass J. K., Munro H. N. Structure of human ferritin light subunit messenger RNA: comparison with heavy subunit message and functional implications. Proc Natl Acad Sci U S A. 1985 May;82(10):3139–3143. doi: 10.1073/pnas.82.10.3139. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Engel J. D., Dodgson J. B. Analysis of the adult and embryonic chicken globin genes in chromosomal DNA. J Biol Chem. 1978 Nov 25;253(22):8239–8246. [PubMed] [Google Scholar]
  19. Fyrberg E. A., Kindle K. L., Davidson N., Kindle K. L. The actin genes of Drosophila: a dispersed multigene family. Cell. 1980 Feb;19(2):365–378. doi: 10.1016/0092-8674(80)90511-5. [DOI] [PubMed] [Google Scholar]
  20. Goldberg D. A. Isolation and partial characterization of the Drosophila alcohol dehydrogenase gene. Proc Natl Acad Sci U S A. 1980 Oct;77(10):5794–5798. doi: 10.1073/pnas.77.10.5794. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Hentze M. W., Keim S., Papadopoulos P., O'Brien S., Modi W., Drysdale J., Leonard W. J., Harford J. B., Klausner R. D. Cloning, characterization, expression, and chromosomal localization of a human ferritin heavy-chain gene. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7226–7230. doi: 10.1073/pnas.83.19.7226. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Jain S. K., Barrett K. J., Boyd D., Favreau M. F., Crampton J., Drysdale J. W. Ferritin H and L chains are derived from different multigene families. J Biol Chem. 1985 Sep 25;260(21):11762–11768. [PubMed] [Google Scholar]
  23. Lehrach H., Diamond D., Wozney J. M., Boedtker H. RNA molecular weight determinations by gel electrophoresis under denaturing conditions, a critical reexamination. Biochemistry. 1977 Oct 18;16(21):4743–4751. doi: 10.1021/bi00640a033. [DOI] [PubMed] [Google Scholar]
  24. Leibold E. A., Aziz N., Brown A. J., Munro H. N. Conservation in rat liver of light and heavy subunit sequences of mammalian ferritin. Presence of unique octopeptide in the light subunit. J Biol Chem. 1984 Apr 10;259(7):4327–4334. [PubMed] [Google Scholar]
  25. Maxam A. M., Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 1980;65(1):499–560. doi: 10.1016/s0076-6879(80)65059-9. [DOI] [PubMed] [Google Scholar]
  26. Melton D. A., Krieg P. A., Rebagliati M. R., Maniatis T., Zinn K., Green M. R. Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter. Nucleic Acids Res. 1984 Sep 25;12(18):7035–7056. doi: 10.1093/nar/12.18.7035. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Messing J., Vieira J. A new pair of M13 vectors for selecting either DNA strand of double-digest restriction fragments. Gene. 1982 Oct;19(3):269–276. doi: 10.1016/0378-1119(82)90016-6. [DOI] [PubMed] [Google Scholar]
  28. Munro H. N., Linder M. C. Ferritin: structure, biosynthesis, and role in iron metabolism. Physiol Rev. 1978 Apr;58(2):317–396. doi: 10.1152/physrev.1978.58.2.317. [DOI] [PubMed] [Google Scholar]
  29. Otsuka S., Listowsky I., Niitsu Y., Urushizaki I. Assembly of intra- and interspecies hybrid apoferritins. J Biol Chem. 1980 Jul 10;255(13):6234–6237. [PubMed] [Google Scholar]
  30. Palmieri S., Beug H., Graf T. Isolation and characterization of four new temperature-sensitive mutants of avian erythroblastosis virus (AEV). Virology. 1982 Dec;123(2):296–311. doi: 10.1016/0042-6822(82)90263-x. [DOI] [PubMed] [Google Scholar]
  31. Samarut J., Gazzolo L. Target cells infected by avian erythroblastosis virus differentiate and become transformed. Cell. 1982 Apr;28(4):921–929. doi: 10.1016/0092-8674(82)90071-x. [DOI] [PubMed] [Google Scholar]
  32. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Sargent T. D., Dawid I. B. Differential gene expression in the gastrula of Xenopus laevis. Science. 1983 Oct 14;222(4620):135–139. doi: 10.1126/science.6688681. [DOI] [PubMed] [Google Scholar]
  34. Shinjyo S. [Isolation and properties of ferritin from chicken (Gallus domesticus, broiler) spleen]. Seikagaku. 1973 Jun;45(6):289–295. [PubMed] [Google Scholar]
  35. Shull G. E., Theil E. C. Translational control of ferritin synthesis by iron in embryonic reticulocytes of the bullfrog. J Biol Chem. 1982 Dec 10;257(23):14187–14191. [PubMed] [Google Scholar]
  36. Smith D. R., Calvo J. M. Nucleotide sequence of the E coli gene coding for dihydrofolate reductase. Nucleic Acids Res. 1980 May 24;8(10):2255–2274. doi: 10.1093/nar/8.10.2255. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Theil E. C. Ferritin: structure, function, and regulation. Adv Inorg Biochem. 1983;5:1–38. [PubMed] [Google Scholar]
  38. Theil E. C., Tosky G. M. Red cell ferritin and iron storage during chick embryonic development. Dev Biol. 1979 Apr;69(2):666–672. doi: 10.1016/0012-1606(79)90320-8. [DOI] [PubMed] [Google Scholar]
  39. Weaver R. F., Weissmann C. Mapping of RNA by a modification of the Berk-Sharp procedure: the 5' termini of 15 S beta-globin mRNA precursor and mature 10 s beta-globin mRNA have identical map coordinates. Nucleic Acids Res. 1979 Nov 10;7(5):1175–1193. doi: 10.1093/nar/7.5.1175. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Wilbur W. J., Lipman D. J. Rapid similarity searches of nucleic acid and protein data banks. Proc Natl Acad Sci U S A. 1983 Feb;80(3):726–730. doi: 10.1073/pnas.80.3.726. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Yamamoto M., Yew N. S., Federspiel M., Dodgson J. B., Hayashi N., Engel J. D. Isolation of recombinant cDNAs encoding chicken erythroid delta-aminolevulinate synthase. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3702–3706. doi: 10.1073/pnas.82.11.3702. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Zinn K., DiMaio D., Maniatis T. Identification of two distinct regulatory regions adjacent to the human beta-interferon gene. Cell. 1983 Oct;34(3):865–879. doi: 10.1016/0092-8674(83)90544-5. [DOI] [PubMed] [Google Scholar]
  43. Zähringer J., Baliga B. S., Munro H. N. Novel mechanism for translational control in regulation of ferritin synthesis by iron. Proc Natl Acad Sci U S A. 1976 Mar;73(3):857–861. doi: 10.1073/pnas.73.3.857. [DOI] [PMC free article] [PubMed] [Google Scholar]

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