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Low molecular weight nuclear RNA. The 3′-terminal sequence of the U2 RNA

Summary

The U2 RNA is one of the low molecular weight nuclear RNAs of Novikoff hepatoma ascites cells that is specifically localized in the extranucleolar portion of the nucleus. After the RNA was purified by polyacrylamide gel electrophoresis, it was subjected to various enzymatic digestion procedures for determination of its primary sequence of nucleotides. The U2 RNA contains 197 nucleotides. Its 5′ end, which is highly modified, contains N2, 2, 7-trimethyl guanylic acid and 11 pseudouridylic acid residues (Reddy et al, J. Biol. Chem. 247, 7245–7250, 1972) in addition to 10 2′-O-methyl ribose residues.

Its 3′-terminal portion (128 nucleotides) contains no methylated nucleotides and its sequence is:-A-U-A-C-G-U-C-C-U-C-U-A-U-C-C-G-A-G-G-A-C-A-A-U-A-ψ-U-A-ψ-U-A-A-A-U-G-G-A-U-U-U-U-U-G-G-A-A-C-U-A-G-G-A-G-U-U-G-G-A-A-U-A-G-G-A-G-C-U-U-G-C-U-C-C-G-U-C-C-A-C-C-U-C-A-C-G-C-A-U-C-G-A-C-C-U-G-G-U-A-U-U-G-C-G-C-A-G-U-A-C-C-C-U-C-A-G-G-A-A-C-G-G-U-G-C-A-C-C-AO H.

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References

  1. [1]

    H. Busch and K. Smetana, The Nucleolus, pp. 285–317, Academic Press, New York (1970).

  2. [2]

    H. Busch, T. S. Ro-Choi, A. W. Prestayko, H. Shibata, S. T. Crooke, S. M. El-Khatib, Y. C. Choi and C. M. Mauritzen, Persp. Biol. Med. 15, 117–139 (1971).

  3. [3]

    H. Busch, Y. C. Choi, I. Daskal, A. Inagaki, M. O. J. Olson, R. Reddy, T. S. Ro-Choi, H. Shibata and L. Yeoman, Acta Endocrinologica. Karolinska Symposium on Reproductive Endocrinology 5, 35–66 (1972).

  4. [4]

    T. S. Ro-Choi, Y. Moriyama, Y. C. Choi and H. Busch, J. Biol. Chem. 245, 1970–1977 (1970).

  5. [5]

    T. S. Ro-Choi, R. Reddy, D. Henning, T. Takano, C. W. Taylor and H. Busch, J. Biol. Chem. 247, 3205–3222 (1972).

  6. [6]

    J. L. Hodnett and H. Busch, J. Biol. Chem. 243, 6336–6344 (1968).

  7. [7]

    R. Weinberg and S. Penman, Biochim. Biophys. Acta 190, 10–29 (1969).

  8. [8]

    A. G. Saponara and M. D. Enger, Nature 223, 1365–1366 (1969).

  9. [9]

    R. Reddy, T. S. Ro-Choi, D. Henning, H. Shibata, Y. C. Choi and H. Busch, J. Biol. Chem. 247, 7245–7250 (1972).

  10. [10]

    F. Sanger and G. G. Brownlee, Methods Enzymol. (L. Grossman and K. Moldave, Eds.) Vol. XII, pp. 361–381, Academic Press, New York. (1967).

  11. [11]

    G. M. Tener, Methods Enzymol. (L. Grossman and K. Moldave, Eds.) Vol. XII, pp, 398–404, Academic Press, New York (1967).

  12. [12]

    C. M. Mauritzen, Y. C. Choi and H. Busch, in Methods in Cancer Research (H. Busch, Ed.), Vol. VI, pp. 253–282, Academic Press, New York (1970).

  13. [13]

    K. Higashi, H. R. Adams and H. Busch, Cancer Res. 26, 2196–2201 (1966).

  14. [14]

    T. Clausen, Anal. Biochem. 22, 70–73 (1968).

  15. [15]

    K. Randerath and E. Randerath, Proc Nucl. Acid Res. (Cantoni, G. L. and Davies, D. R., Eds.), Vol. 2, pp. 796–812, Harper & Row, New York (1971).

  16. [16]

    G. R. Wyatt, Biochem. J. 48, 584–590 (1951).

  17. [17]

    H. Singh and B. G. Lane, Can. J. Biochem. 240, 1742–1748 (1964).

  18. [18]

    N. W. Y. Ho and P. T. Gilham, Biochem. 6, 3632–3639 (1967).

  19. [19]

    B. G. Barrell, Proc. Nucl. Acid Res. (G. L. Cantoni and D. R. Davies, Eds.), Vol. 2, pp. 751–779, Harper & Row, New York (1971).

  20. [20]

    J. C. Lee, N. W. Y. Ho and P. T. Gilham, Biochim. Biophys. Acta 95, 503–504 (1965).

  21. [21]

    G. G. Brownlee, F. Sanger and B. G. Barrell, J. Mol. Biol. 34, 379–412 (1968).

  22. [22]

    B. G. Forget and S. M. Weissman, Science 158, 1695–1699 (1968).

  23. [23]

    B. Dubuy and S. M. Weissman, J. Biol. Chem. 246, 747–761 (1971).

  24. [24]

    G. G. Brownlee, Nature New Biology 229, 147–149 (1971).

  25. [25]

    S. Altman and J. D. Smith, Nature New Biology 233, 35–39 (1971).

  26. [26]

    K. Ohe and S. M. Weissman, J. Biol. Chem. 246, 6991–7009 (1971).

  27. [27]

    R. DeWachter, A. VandenBerghe, J. Merregaert, R. Contreras and W. Fiers, Proc. Nat. Acad. Sci. USA 68, 585–589 (1971).

  28. [28]

    W. Min-Jou, G. Haegeman, M. Ysebaert and W. Fiers, Nature New Biology 236, 82–85 (1972).

  29. [29]

    P. Fellner, C. Ehresmann and J. P. Ebel, Nature New Biology 239, 1–5 (1972).

  30. [30]

    S. Seeber, Y. C. Choi and H. Busch, J. Biol. Chem. 246, 2633–2644. (1971)

  31. [31]

    S. Seeber and H. Busch, J. Biol. Chem. 246, 7144–7150 (1971).

  32. [32]

    A. Inagaki and H. Busch, J. Biol. Chem. 247, 3327–3335 (1972).

  33. [33]

    R. N. Nazar and H. Busch, Biochim. Biophys. Acta. 299, 428–443, 1973.

  34. [34]

    R. Kanamaru, Y. C. Choi and H. Busch, Physcol-Chem. Phys. 4, 103–124 (1972).

  35. [35]

    Y. Moriyama, J. L. Hodnett, A. W. Prestayko and H. Busch, J. Mol. Biol. 39, 335–349 (1969).

  36. [36]

    A. W. Prestayko and H. Busch, Biochim. Biophys. Acta 169, 338–349 (1968).

  37. [37]

    H. W. U. Heyden and H. G. Zachau, Biochim. Biophys. Acta 232, 641–660 (1971).

  38. [38]

    M. Artman and J. S. Roth, J. Mol. Biol. 60, 291–301 (1971).

  39. [39]

    M. D. Enger and R. A. Walters, Biochem. 9, 3551–3562 (1970).

  40. [40]

    A. Rein, Biochim. Biophys. Acta 169, 338–349 (1971).

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Additional information

These studies were supported by the Public Health Service Cancer Center Grant CA-10893.

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Shibata, H., Reddy, R., Henning, D. et al. Low molecular weight nuclear RNA. The 3′-terminal sequence of the U2 RNA. Mol Cell Biochem 4, 3–19 (1974). https://doi.org/10.1007/BF01731099

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Keywords

  • Nucleotide
  • Polyacrylamide
  • Primary Sequence
  • Enzymatic Digestion
  • Ribose