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. 1983;2(5):775–779. doi: 10.1002/j.1460-2075.1983.tb01499.x

Isolation and sequence analysis of the human corticotropin-releasing factor precursor gene.

S Shibahara, Y Morimoto, Y Furutani, M Notake, H Takahashi, S Shimizu, S Horikawa, S Numa
PMCID: PMC555184  PMID: 6605851

Abstract

A human genomic DNA segment containing the gene for the corticotropin-releasing factor precursor has been isolated by screening a gene library with an ovine cDNA probe. The cloned DNA segment has been subjected to restriction endonuclease mapping and nucleotide sequence analysis. Comparison of the nucleotide sequence of the gene with that of the ovine cDNA indicates that an intron of 800 bp is inserted in the segment encoding the 5'-untranslated region of the mRNA. The segment corresponding to the protein-coding and the 3'-untranslated region of the mRNA is uninterrupted. The mRNA and amino acid sequences of the human corticotropin-releasing factor precursor have been deduced from the corresponding gene sequence. The deduced amino acid sequence of human corticotropin-releasing factor exhibits seven amino acid substitutions in comparison with the ovine counterpart.

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Selected References

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

  1. Amara S. G., David D. N., Rosenfeld M. G., Roos B. A., Evans R. M. Characterization of rat calcitonin mRNA. Proc Natl Acad Sci U S A. 1980 Aug;77(8):4444–4448. doi: 10.1073/pnas.77.8.4444. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Amara S. G., Jonas V., Rosenfeld M. G., Ong E. S., Evans R. M. Alternative RNA processing in calcitonin gene expression generates mRNAs encoding different polypeptide products. Nature. 1982 Jul 15;298(5871):240–244. doi: 10.1038/298240a0. [DOI] [PubMed] [Google Scholar]
  3. Benoist C., O'Hare K., Breathnach R., Chambon P. The ovalbumin gene-sequence of putative control regions. Nucleic Acids Res. 1980 Jan 11;8(1):127–142. doi: 10.1093/nar/8.1.127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Benton W. D., Davis R. W. Screening lambdagt recombinant clones by hybridization to single plaques in situ. Science. 1977 Apr 8;196(4286):180–182. doi: 10.1126/science.322279. [DOI] [PubMed] [Google Scholar]
  5. Blobel G., Dobberstein B. Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components. J Cell Biol. 1975 Dec;67(3):852–862. doi: 10.1083/jcb.67.3.852. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Bradbury A. F., Finnie M. D., Smyth D. G. Mechanism of C-terminal amide formation by pituitary enzymes. Nature. 1982 Aug 12;298(5875):686–688. doi: 10.1038/298686a0. [DOI] [PubMed] [Google Scholar]
  7. Breathnach R., Benoist C., O'Hare K., Gannon F., Chambon P. Ovalbumin gene: evidence for a leader sequence in mRNA and DNA sequences at the exon-intron boundaries. Proc Natl Acad Sci U S A. 1978 Oct;75(10):4853–4857. doi: 10.1073/pnas.75.10.4853. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. Chou P. Y., Fasman G. D. Empirical predictions of protein conformation. Annu Rev Biochem. 1978;47:251–276. doi: 10.1146/annurev.bi.47.070178.001343. [DOI] [PubMed] [Google Scholar]
  10. Crabtree G. R., Kant J. A. Organization of the rat gamma-fibrinogen gene: alternative mRNA splice patterns produce the gamma A and gamma B (gamma ') chains of fibrinogen. Cell. 1982 Nov;31(1):159–166. doi: 10.1016/0092-8674(82)90415-9. [DOI] [PubMed] [Google Scholar]
  11. DeNoto F. M., Moore D. D., Goodman H. M. Human growth hormone DNA sequence and mRNA structure: possible alternative splicing. Nucleic Acids Res. 1981 Aug 11;9(15):3719–3730. doi: 10.1093/nar/9.15.3719. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Early P., Rogers J., Davis M., Calame K., Bond M., Wall R., Hood L. Two mRNAs can be produced from a single immunoglobulin mu gene by alternative RNA processing pathways. Cell. 1980 Jun;20(2):313–319. doi: 10.1016/0092-8674(80)90617-0. [DOI] [PubMed] [Google Scholar]
  13. Fink G. Has corticotropin-releasing factor finally been found? Nature. 1981 Dec 10;294(5841):511–512. doi: 10.1038/294511a0. [DOI] [PubMed] [Google Scholar]
  14. Frischauf A. M., Garoff H., Lehrach H. A subcloning strategy for DNA sequence analysis. Nucleic Acids Res. 1980 Dec 11;8(23):5541–5549. doi: 10.1093/nar/8.23.5541. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Furutani Y., Morimoto Y., Shibahara S., Noda M., Takahashi H., Hirose T., Asai M., Inayama S., Hayashida H., Miyata T. Cloning and sequence analysis of cDNA for ovine corticotropin-releasing factor precursor. Nature. 1983 Feb 10;301(5900):537–540. doi: 10.1038/301537a0. [DOI] [PubMed] [Google Scholar]
  16. GUILLEMIN R., ROSENBERG B. Humoral hypothalamic control of anterior pituitary: a study with combined tissue cultures. Endocrinology. 1955 Nov;57(5):599–607. doi: 10.1210/endo-57-5-599. [DOI] [PubMed] [Google Scholar]
  17. Ichikawa T., McMaster D., Lederis K., Kobayashi H. Isolation and amino acid sequence of urotensin I, a vasoactive and ACTH-releasing neuropeptide, from the carp (Cyprinus carpio) urophysis. Peptides. 1982 Sep-Oct;3(5):859–867. doi: 10.1016/0196-9781(82)90028-6. [DOI] [PubMed] [Google Scholar]
  18. Land H., Schütz G., Schmale H., Richter D. Nucleotide sequence of cloned cDNA encoding bovine arginine vasopressin-neurophysin II precursor. Nature. 1982 Jan 28;295(5847):299–303. doi: 10.1038/295299a0. [DOI] [PubMed] [Google Scholar]
  19. Lawn R. M., Fritsch E. F., Parker R. C., Blake G., Maniatis T. The isolation and characterization of linked delta- and beta-globin genes from a cloned library of human DNA. Cell. 1978 Dec;15(4):1157–1174. doi: 10.1016/0092-8674(78)90043-0. [DOI] [PubMed] [Google Scholar]
  20. Lederis K., Letter A., McMaster D., Moore G., Schlesinger D. Complete amino acid sequence of urotensin I, a hypotensive and corticotropin-releasing neuropeptide from Catostomus. Science. 1982 Oct 8;218(4568):162–165. doi: 10.1126/science.6981844. [DOI] [PubMed] [Google Scholar]
  21. Lederis K., Vale W., Rivier J., MacCannell K. L., McMaster D., Kobayashi Y., Suess U., Lawrence J. Urotensin I - a novel CRF-like peptide in Catostomus commersoni urophysis. Proc West Pharmacol Soc. 1982;25:223–227. [PubMed] [Google Scholar]
  22. 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]
  23. Montecucchi P. C., Gozzini L. Secondary structure prediction of sauvagine, a novel biologically active polypeptide from a frog. Int J Pept Protein Res. 1982 Aug;20(2):139–143. doi: 10.1111/j.1399-3011.1982.tb02666.x. [DOI] [PubMed] [Google Scholar]
  24. Mount S. M. A catalogue of splice junction sequences. Nucleic Acids Res. 1982 Jan 22;10(2):459–472. doi: 10.1093/nar/10.2.459. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Nakanishi S., Inoue A., Kita T., Nakamura M., Chang A. C., Cohen S. N., Numa S. Nucleotide sequence of cloned cDNA for bovine corticotropin-beta-lipotropin precursor. Nature. 1979 Mar 29;278(5703):423–427. doi: 10.1038/278423a0. [DOI] [PubMed] [Google Scholar]
  26. Noda M., Teranishi Y., Takahashi H., Toyosato M., Notake M., Nakanishi S., Numa S. Isolation and structural organization of the human preproenkephalin gene. Nature. 1982 Jun 3;297(5865):431–434. doi: 10.1038/297431a0. [DOI] [PubMed] [Google Scholar]
  27. Okayama H., Berg P. High-efficiency cloning of full-length cDNA. Mol Cell Biol. 1982 Feb;2(2):161–170. doi: 10.1128/mcb.2.2.161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Philippsen P., Kramer R. A., Davis R. W. Cloning of the yeast ribosomal DNA repeat unit in SstI and HindIII lambda vectors using genetic and physical size selections. J Mol Biol. 1978 Aug 15;123(3):371–386. doi: 10.1016/0022-2836(78)90085-2. [DOI] [PubMed] [Google Scholar]
  29. Polsky F., Edgell M. H., Seidman J. G., Leder P. High capacity gel preparative electrophoresis for purification of fragments of genomic DNA. Anal Biochem. 1978 Jul 1;87(2):397–410. doi: 10.1016/0003-2697(78)90689-9. [DOI] [PubMed] [Google Scholar]
  30. Proudfoot N. J., Brownlee G. G. 3' non-coding region sequences in eukaryotic messenger RNA. Nature. 1976 Sep 16;263(5574):211–214. doi: 10.1038/263211a0. [DOI] [PubMed] [Google Scholar]
  31. SAFFRAN M., SCHALLY A. V. The release of corticotrophin by anterior pituitary tissue in vitro. Can J Biochem Physiol. 1955 May;33(3):408–415. [PubMed] [Google Scholar]
  32. Seidah N. G., Rochemont J., Hamelin J., Benjannet S., Chrétien M. The missing fragment of the pro-sequence of human pro-opiomelanocortin: sequence and evidence for C-terminal amidation. Biochem Biophys Res Commun. 1981 Sep 30;102(2):710–716. doi: 10.1016/s0006-291x(81)80190-8. [DOI] [PubMed] [Google Scholar]
  33. Shibasaki T., Ling N., Guillemin R. A radioimmunoassay for gamma 1-melanotropin and evidence that the smallest pituitary gamma-melanotropin is amidated at the COOH-terminus. Biochem Biophys Res Commun. 1980 Oct 16;96(3):1393–1399. doi: 10.1016/0006-291x(80)90105-9. [DOI] [PubMed] [Google Scholar]
  34. Smith G. E., Summers M. D. The bidirectional transfer of DNA and RNA to nitrocellulose or diazobenzyloxymethyl-paper. Anal Biochem. 1980 Nov 15;109(1):123–129. doi: 10.1016/0003-2697(80)90019-6. [DOI] [PubMed] [Google Scholar]
  35. Southern E. M. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol. 1975 Nov 5;98(3):503–517. doi: 10.1016/s0022-2836(75)80083-0. [DOI] [PubMed] [Google Scholar]
  36. Spiess J., Rivier J., Rivier C., Vale W. Primary structure of corticotropin-releasing factor from ovine hypothalamus. Proc Natl Acad Sci U S A. 1981 Oct;78(10):6517–6521. doi: 10.1073/pnas.78.10.6517. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Steiner D. F., Quinn P. S., Chan S. J., Marsh J., Tager H. S. Processing mechanisms in the biosynthesis of proteins. Ann N Y Acad Sci. 1980;343:1–16. doi: 10.1111/j.1749-6632.1980.tb47238.x. [DOI] [PubMed] [Google Scholar]
  38. Suchanek G., Kreil G. Translation of melittin messenger RNA in vitro yields a product terminating with glutaminylglycine rather than with glutaminamide. Proc Natl Acad Sci U S A. 1977 Mar;74(3):975–978. doi: 10.1073/pnas.74.3.975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Sutcliffe J. G. Complete nucleotide sequence of the Escherichia coli plasmid pBR322. Cold Spring Harb Symp Quant Biol. 1979;43(Pt 1):77–90. doi: 10.1101/sqb.1979.043.01.013. [DOI] [PubMed] [Google Scholar]
  40. Vale W., Spiess J., Rivier C., Rivier J. Characterization of a 41-residue ovine hypothalamic peptide that stimulates secretion of corticotropin and beta-endorphin. Science. 1981 Sep 18;213(4514):1394–1397. doi: 10.1126/science.6267699. [DOI] [PubMed] [Google Scholar]
  41. Weinstock R., Sweet R., Weiss M., Cedar H., Axel R. Intragenic DNA spacers interrupt the ovalbumin gene. Proc Natl Acad Sci U S A. 1978 Mar;75(3):1299–1303. doi: 10.1073/pnas.75.3.1299. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Woo S. L., Dugaiczyk A., Tsai M. J., Lai E. C., Catterall J. F., O'Malley B. W. The ovalbumin gene: cloning of the natural gene. Proc Natl Acad Sci U S A. 1978 Aug;75(8):3688–3692. doi: 10.1073/pnas.75.8.3688. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Yasuda N., Greer M. A., Aizawa T. Corticotropin-releasing factor. Endocr Rev. 1982 Spring;3(2):123–140. doi: 10.1210/edrv-3-2-123. [DOI] [PubMed] [Google Scholar]
  44. Yoo O. J., Powell C. T., Agarwal K. L. Molecular cloning and nucleotide sequence of full-length of cDNA coding for porcine gastrin. Proc Natl Acad Sci U S A. 1982 Feb;79(4):1049–1053. doi: 10.1073/pnas.79.4.1049. [DOI] [PMC free article] [PubMed] [Google Scholar]

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