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The cDNA for the β-subunit of human chorionic gonadotropin suggests evolution of a gene by readthrough into the 3′-untranslated region

Nature volume 286, pages 684687 (14 August 1980) | Download Citation

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Abstract

A 579-base pair approximately full-length cDNA which codes for the 145-amino acid long β-subunit of human chorionic gonadotropin (HCG) has been cloned in the plasmid vector pBR322 and its complete nucleotide sequence determined. A hydrophobic presequence of 20 amino acids can be identified from the nucleotide sequence. The amino acid sequence of the β-subunit is known to be related to those of the β-subunits of the other glycoprotein hormones LH, FSH and TSH, but the β-subunit of HCG is unique in that it contains a C-terminal extension of about 30 amino acids which has no homologous counterpart in the other three hormones. Analysis of the βHCG cDNA nucleotide sequence suggests that this extension may have arisen by the loss of the termination codon of an ancestral β-like gene so that most of what was previously the 3′-untranslated region now codes for protein. The β-subunit of HCG terminates with the codon UAA located 16 bases before the poly (A) in the sequence AAUAAA. This sequence is believed to be a recognition signal involved in either polyadenylation or processing and therefore has a dual role in this gene, serving both a coding and a regulatory function.

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References

  1. 1.

    , , & in Peptide Hormones (ed. Parsons, J. A.) 299–315 (University Park Press, Baltimore, 1976).

  2. 2.

    Fedn Proc. 36, 2119–2127 (1977).

  3. 3.

    , , & in Detection and Prevention of Cancer Part 2, Vol. 1 (ed. Nieburgs, H. E.) 937–963 (Dekker, New York, 1978).

  4. 4.

    , , & Proc. natn. Acad. Sci. U.S.A. 76, 6622–6626 (1979).

  5. 5.

    & Biochem. biophys. Res. Commun. 40, 422–427 (1970).

  6. 6.

    , & J. biol. Chem. 248, 6796–6809 (1973).

  7. 7.

    , & J. biol. Chem. 250, 5247–5258 (1975).

  8. 8.

    , & Biochem. biophys. Res. Commun. 48, 530–537 (1972).

  9. 9.

    , , , & Biochem. J. 126, 441–442 (1971).

  10. 10.

    & J. clin. Endocr. Metab. 39, 169–202 (1974).

  11. 11.

    & J. biol. Chem. 250, 6735–6746 (1975).

  12. 12.

    & J. biol. Chem. 252, 5393–5397 (1977).

  13. 13.

    & J. biol. Chem. 252, 5386–5392 (1977).

  14. 14.

    & J. biol. Chem. 251, 993–1005 (1976).

  15. 15.

    & Biochem. biophys. Res. Commun. 54, 426–431 (1973).

  16. 16.

    & J. clin. Endocr. Metab. 39, 203–205 (1974).

  17. 17.

    & Nature 281, 351–356 (1979).

  18. 18.

    & Nature 263, 211–214 (1976).

  19. 19.

    , & Biochem. biophys. Res. Commun. 72, 381–390 (1976).

  20. 20.

    et al. J. biol. Chem. 253, 7109–7114 (1978).

  21. 21.

    , & J. biol. Chem. 251, 2945–2951 (1976).

  22. 22.

    , Biochem. biophys. Res. Commun. 77, 426–433 (1977).

  23. 23.

    , , & Clin. Endocr. 1, 315–316, (1973).

  24. 24.

    , & (in preparation).

  25. 25.

    , , , & Nucleic Acids Res. 5, 1153–1163 (1978).

  26. 26.

    J. molec. Biol. (in the press).

  27. 27.

    & Proc. natn. Acad. Sci. U.S.A. 74, 560–564 (1977).

  28. 28.

    & Nucleic Acids Res. 5, 4537–4545 (1978).

  29. 29.

    et al. Proc. natn. Acad. Sci. U.S.A. 75, 2616–2620 (1978).

  30. 30.

    , , , & Biochem. biophys. Res. Commun. 85, 1247–1253 (1978).

  31. 31.

    Cell 15, 1109–1123 (1978).

  32. 32.

    et al. J. biol. Chem. 253, 3643–3647 (1978).

  33. 33.

    & Nucleic Acids Res. 5, 2359–2371 (1978).

  34. 34.

    et al. Proc. natn. Acad. Sci. U.S.A. 76, 4981–4985 (1979).

  35. 35.

    et al. Nature 282, 525–527 (1979).

  36. 36.

    , , , & Nature 270, 494–499 (1977).

  37. 37.

    , , & Science 205, 602–607 (1979).

  38. 38.

    , , & J. biol. Chem. 252, 5040–5053 (1977).

  39. 39.

    & Cell 9, 733–746 (1976).

  40. 40.

    , , , & Proc. natn. Acad. Sci. U.S.A. 74, 5145–5149 (1977).

  41. 41.

    , , , & Nucleic Acids Res. 8, r49–r62 (1980).

  42. 42.

    , & in Hormonal Proteins and Peptides Vol. 1 (ed. Li, C. H.) (Academic, New York, 1973).

  43. 43.

    Haemoglobins in Genetics and Evolution (Columbia University Press, New York, 1963).

  44. 44.

    , , , & Eur. J. Biochem. 72, 453–463 (1977).

  45. 45.

    , , & Eur. J. Biochem. 87, 551–561 (1978).

  46. 46.

    et al. Nature 276, 298–301 (1978).

  47. 47.

    , & Nature 234, 337–340 (1971).

  48. 48.

    , & J. Bact. 114, 577–591 (1973).

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Affiliations

  1. Howard Hughes Medical Institute Laboratory, Department of Biochemistry and Biophysics, University of California, San Francisco, California 94143

    • John C. Fiddes
    •  & Howard M. Goodman

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https://doi.org/10.1038/286684a0

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