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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1985 Jan;82(2):617–621. doi: 10.1073/pnas.82.2.617

Complete coding sequence of rat tyrosine hydroxylase mRNA.

B Grima, A Lamouroux, F Blanot, N F Biguet, J Mallet
PMCID: PMC397092  PMID: 2857492

Abstract

Several clones specific for tyrosine hydroxylase [tyrosine 3-monooxygenase, L-tyrosine, tetrahydropteridine:oxygen oxidoreductase (3-hydroxylating), EC 1.14.16.2] have been identified from a rat PC12 library by using the previously characterized clone pTH-1. The most complete of these, pTH-51, is 1758 base pairs long and covers most of the length of the mRNA, including the entire coding and 3' untranslated region. The polypeptide has an estimated molecular weight of 55,903 and some of its characteristic features are discussed.

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Selected References

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

  1. Andrews D. W., Langan T. A., Weiner N. Evidence for the involvement of a cyclic AMP-independent protein kinase in the activation of soluble tyrosine hydroxylase from rat striatum. Proc Natl Acad Sci U S A. 1983 Apr;80(8):2097–2101. doi: 10.1073/pnas.80.8.2097. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Blobel G., Dobberstein B. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J Cell Biol. 1975 Dec;67(3):835–851. doi: 10.1083/jcb.67.3.835. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Casadaban M. J., Cohen S. N. Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J Mol Biol. 1980 Apr;138(2):179–207. doi: 10.1016/0022-2836(80)90283-1. [DOI] [PubMed] [Google Scholar]
  4. Chou P. Y., Fasman G. D. Prediction of protein conformation. Biochemistry. 1974 Jan 15;13(2):222–245. doi: 10.1021/bi00699a002. [DOI] [PubMed] [Google Scholar]
  5. El Mestikawy S., Glowinski J., Hamon M. Tyrosine hydroxylase activation in depolarized dopaminergic terminals--involvement of Ca2+-dependent phosphorylation. Nature. 1983 Apr 28;302(5911):830–832. doi: 10.1038/302830a0. [DOI] [PubMed] [Google Scholar]
  6. Grosveld F. G., Dahl H. H., de Boer E., Flavell R. A. Isolation of beta-globin-related genes from a human cosmid library. Gene. 1981 Apr;13(3):227–237. doi: 10.1016/0378-1119(81)90028-7. [DOI] [PubMed] [Google Scholar]
  7. Hanahan D. Studies on transformation of Escherichia coli with plasmids. J Mol Biol. 1983 Jun 5;166(4):557–580. doi: 10.1016/s0022-2836(83)80284-8. [DOI] [PubMed] [Google Scholar]
  8. Haycock J. W., Bennett W. F., George R. J., Waymire J. C. Multiple site phosphorylation of tyrosine hydroxylase. Differential regulation in situ by a 8-bromo-cAMP and acetylcholine. J Biol Chem. 1982 Nov 25;257(22):13699–13703. [PubMed] [Google Scholar]
  9. Haycock J. W., Meligeni J. A., Bennett W. F., Waymire J. C. Phosphorylation and activation of tyrosine hydroxylase mediate the acetylcholine-induced increase in catecholamine biosynthesis in adrenal chromaffin cells. J Biol Chem. 1982 Nov 10;257(21):12641–12648. [PubMed] [Google Scholar]
  10. Heindell H. C., Liu A., Paddock G. V., Studnicka G. M., Salser W. A. The primary sequence of rabbit alpha-globin mRNA. Cell. 1978 Sep;15(1):43–54. doi: 10.1016/0092-8674(78)90081-8. [DOI] [PubMed] [Google Scholar]
  11. Hoeldtke R., Kaufman S. Bovine adrenal tyrosine hydroxylase: purification and properties. J Biol Chem. 1977 May 25;252(10):3160–3169. [PubMed] [Google Scholar]
  12. Joh T. H., Baetge E. E., Ross M. E., Reis D. J. Evidence for the existence of homologous gene coding regions for the catecholamine biosynthetic enzymes. Cold Spring Harb Symp Quant Biol. 1983;48(Pt 1):327–335. doi: 10.1101/sqb.1983.048.01.036. [DOI] [PubMed] [Google Scholar]
  13. Joh T. H., Park D. H., Reis D. J. Direct phosphorylation of brain tyrosine hydroxylase by cyclic AMP-dependent protein kinase: mechanism of enzyme activation. Proc Natl Acad Sci U S A. 1978 Oct;75(10):4744–4748. doi: 10.1073/pnas.75.10.4744. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kozak M. Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs. Nucleic Acids Res. 1984 Jan 25;12(2):857–872. doi: 10.1093/nar/12.2.857. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kozak M. Point mutations close to the AUG initiator codon affect the efficiency of translation of rat preproinsulin in vivo. Nature. 1984 Mar 15;308(5956):241–246. doi: 10.1038/308241a0. [DOI] [PubMed] [Google Scholar]
  16. Krebs E. G., Beavo J. A. Phosphorylation-dephosphorylation of enzymes. Annu Rev Biochem. 1979;48:923–959. doi: 10.1146/annurev.bi.48.070179.004423. [DOI] [PubMed] [Google Scholar]
  17. Lamouroux A., Faucon Biguet N., Samolyk D., Privat A., Salomon J. C., Pujol J. F., Mallet J. Identification of cDNA clones coding for rat tyrosine hydroxylase antigen. Proc Natl Acad Sci U S A. 1982 Jun;79(12):3881–3885. doi: 10.1073/pnas.79.12.3881. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Le Douarin N. M. The ontogeny of the neural crest in avian embryo chimaeras. Nature. 1980 Aug 14;286(5774):663–669. doi: 10.1038/286663a0. [DOI] [PubMed] [Google Scholar]
  19. Lloyd T. The effects of phosphatidylinositol on tyrosine hydroxylase. Stimulation and inactivation. J Biol Chem. 1979 Aug 10;254(15):7247–7254. [PubMed] [Google Scholar]
  20. Lomedico P. T., Saunders G. F. Preparation of pancreatic mRNA: cell-free translation of an insulin-immunoreactive polypeptide. Nucleic Acids Res. 1976 Feb;3(2):381–391. doi: 10.1093/nar/3.2.381. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Mallet J., Faucon Biguet N., Buda M., Lamouroux A., Samolyk D. Detection and regulation of the tyrosine hydroxylase mRNA levels in rat adrenal medulla and brain tissues. Cold Spring Harb Symp Quant Biol. 1983;48(Pt 1):305–308. doi: 10.1101/sqb.1983.048.01.033. [DOI] [PubMed] [Google Scholar]
  22. Markey K. A., Kondo H., Shenkman L., Goldstein M. Purification and characterization of tyrosine hydroxylase from a clonal pheochromocytoma cell line. Mol Pharmacol. 1980 Jan;17(1):79–85. [PubMed] [Google Scholar]
  23. Messing J., Crea R., Seeburg P. H. A system for shotgun DNA sequencing. Nucleic Acids Res. 1981 Jan 24;9(2):309–321. doi: 10.1093/nar/9.2.309. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Miyata T., Yasunaga T., Nishida T. Nucleotide sequence divergence and functional constraint in mRNA evolution. Proc Natl Acad Sci U S A. 1980 Dec;77(12):7328–7332. doi: 10.1073/pnas.77.12.7328. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Nishioka Y., Leder P. The complete sequence of a chromosomal mouse alpha--globin gene reveals elements conserved throughout vertebrate evolution. Cell. 1979 Nov;18(3):875–882. doi: 10.1016/0092-8674(79)90139-9. [DOI] [PubMed] [Google Scholar]
  26. Otten U., Thoenen H. Effect of glucocorticoids on nerve growth factor-mediated enzyme induction in organ cultures of rat sympathetic ganglia: enchanced response and reduced time requirement to initiate enzyme induction. J Neurochem. 1977 Jul;29(1):69–75. doi: 10.1111/j.1471-4159.1977.tb03925.x. [DOI] [PubMed] [Google Scholar]
  27. Reis D. J., Joh T. H., Ross R. A. Effects of reserpine on activities and amounts of tyrosine hydroxylase and dopamine-beta-hydroxylase in catecholamine neuronal systems in rat brain. J Pharmacol Exp Ther. 1975 Jun;193(3):775–784. [PubMed] [Google Scholar]
  28. Rigby P. W., Dieckmann M., Rhodes C., Berg P. Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase I. J Mol Biol. 1977 Jun 15;113(1):237–251. doi: 10.1016/0022-2836(77)90052-3. [DOI] [PubMed] [Google Scholar]
  29. 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]
  30. Shenolikar S., Cohen P. The substrate specificity of cyclic AMP-dependent protein kinase: amino acid sequences at the phosphorylation sites of herring protamine (clupeine). FEBS Lett. 1978 Feb 1;86(1):92–98. doi: 10.1016/0014-5793(78)80106-9. [DOI] [PubMed] [Google Scholar]
  31. Thayer R. E. An improved method for detecting foreign DNA in plasmids of Escherichia coli. Anal Biochem. 1979 Sep 15;98(1):60–63. doi: 10.1016/0003-2697(79)90705-x. [DOI] [PubMed] [Google Scholar]
  32. Thoenen H., Mueller R. A., Axelrod J. Trans-synaptic induction of adrenal tyrosine hydroxylase. J Pharmacol Exp Ther. 1969 Oct;169(2):249–254. [PubMed] [Google Scholar]
  33. Thoenen H. Trans-synaptic enzyme induction. Life Sci. 1974 Jan 16;14(2):223–235. doi: 10.1016/0024-3205(74)90052-6. [DOI] [PubMed] [Google Scholar]
  34. Treiman M., Weber W., Gratzl M. 3',5'-cyclic adenosine monophosphate- and Ca2+-calmodulin-dependent endogenous protein phosphorylation activity in membranes of the bovine chromaffin secretory vesicles: identification of two phosphorylated components as tyrosine hydroxylase and protein kinase regulatory subunit type II. J Neurochem. 1983 Mar;40(3):661–669. doi: 10.1111/j.1471-4159.1983.tb08031.x. [DOI] [PubMed] [Google Scholar]
  35. Vigny A., Henry J. P. Bovine adrenal tyrosine hydroxylase: comparative study of native and proteolyzed enzyme, and their interaction with anions. J Neurochem. 1981 Feb;36(2):483–489. doi: 10.1111/j.1471-4159.1981.tb01618.x. [DOI] [PubMed] [Google Scholar]
  36. Vigny A., Henry J. P. Mechanism of tyrosine hydroxylase activation by phosphorylation. Biochem Biophys Res Commun. 1982 May 14;106(1):1–7. doi: 10.1016/0006-291x(82)92049-6. [DOI] [PubMed] [Google Scholar]
  37. Zigmond R. E., Chalazonitis A. Long-term effects of preganglionic nerve stimulation on tyrosine hydroxylase activity in the rat superior cervical ganglion. Brain Res. 1979 Mar 23;164:137–152. doi: 10.1016/0006-8993(79)90011-8. [DOI] [PubMed] [Google Scholar]
  38. Zigmond R. E., Mackay A. V., Iversen L. L. Minimum duration of trans-synaptic stimulation required for the induction of tyrosine hydroxylase by reserpine in the rat superior cervical ganglion. J Neurochem. 1974 Aug;23(2):355–358. doi: 10.1111/j.1471-4159.1974.tb04365.x. [DOI] [PubMed] [Google Scholar]

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