Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Letter
  • Published:

Comparison of α-tropomyosin sequences from smooth and striated muscle

Nature volume 315, pages 67–70 (1985)Cite this article

Abstract

Tropomyosins are a closely related family of proteins with a dimeric α-coiled-coil structure1. Skeletal isoforms are composed of two types of subunits, α and β2–4 which, in turn, are assorted into two main molecular species αα and αβ5–7. Both isoforms are present in different molar ratios in individual skeletal muscle types8,9. In small mammals, however, onlyα-chain is expressed in cardiac muscle8. Tropomyosin, in association with the troponin complex (troponin-I, -T and -C) plays a central role in the Ca2+dependent regulation of vertebrate striated muscle contraction10–12. On the other hand, despite structural similarities with the striated isoforms, the function of this protein in smooth muscle and non-muscle cells remains unknown, because in these cells contraction is thought to be regulated by myosin-linked processes independently of tropomyosin13–15. Here we report the nucleotide sequences of cloned complementary DNAs for rat striated and smooth muscle α-tropomyosin. Comparison of the derived amino-acid sequences reveals the existence of tissue-specific peptides that delimit the putative troponin-I and troponin-T binding domains of tropomyosin. S1-nuclease mapping studies reveal the existence of three distinct α-tropomyosin messenger RNA isoforms each encoding a different protein; these isoforms are tissue-specific, developmentally regulated and most probably encoded by the same gene.

This is a preview of subscription content, access via your institution

Access options

Buy this article

  • Purchase on Springer Link
  • Instant access to full article PDF
Buy now

Prices may be subject to local taxes which are calculated during checkout

Similar content being viewed by others

References

  1. Smillie, L. B. Trends biochem. Sci. 4, 151–154 (1979).

    Article  CAS  Google Scholar 

  2. Sodek, J., Hodges, R. S. & Smillie, L. B. J. biol. Chem. 253, 1129–1136 (1978).

    CAS  PubMed  Google Scholar 

  3. Stone, D. & Smillie, L. B. J. biol. Chem. 253, 1137–1148 (1978).

    CAS  PubMed  Google Scholar 

  4. Mak, A. S., Lewis, W. G. & Smillie, L. B. FEBS Lett. 105, 232–234 (1979).

    Article  CAS  Google Scholar 

  5. Eisenberg, E. & Kielley, W. W. J. biol. Chem. 249, 4742–4748 (1974).

    CAS  PubMed  Google Scholar 

  6. Yamaguchi, M., Greaser, M. & Cassens, R. G. J. ultrastruct. Res. 48, 33–48 (1974).

    Article  CAS  Google Scholar 

  7. Lehrer, S. S. Proc. natn. Acad. Sci. U.S.A. 72, 3377–3381 (1975).

    Article  ADS  CAS  Google Scholar 

  8. Cummins, P. & Perry, S. V. Biochem. J. 133, 765–777 (1973).

    Article  CAS  Google Scholar 

  9. Cummins, P. & Perry, S. V. Biochem. J. 43–49 (1974).

  10. Perry, S. V. Biochem. Soc. Trans. 7, 593 (1979).

    Article  CAS  Google Scholar 

  11. Taylor, E. W. CRC Crit. Rev. Biochem. 6, 103–164 (1979).

    Article  Google Scholar 

  12. Adelstein, R. S. & Eisenberg, E. A. Rev. Biochem. 49, 921–956 (1980).

    Article  CAS  Google Scholar 

  13. Gorecka, A., Aksoy, M. O. & Hartshorne, D. J. Biochem. biophys. Res. Commun. 71, 325–331 (1976).

    Article  CAS  Google Scholar 

  14. Sobieszek, A. & Small, J. V. J. molec. Biol. 101, 75–92 (1976).

    Article  Google Scholar 

  15. Chacko, S., Conti, M. A. & Adelstein, R. S. Proc. natn. Acad. Sci. U.S.A. 74, 129–133 (1977).

    Article  ADS  CAS  Google Scholar 

  16. Nadal-Ginard, B. Cell 15, 855–864 (1978).

    Article  CAS  Google Scholar 

  17. Elzinga, M. & Trus, B. in Methods in Peptide and Protein Sequence Analysis (ed. Birr, C.) 213–224 (Elsevier, Amsterdam, 1980).

    Google Scholar 

  18. Stone, D., Sodek, J., Johnson, P. & Smillie, L. B. Proc. IX FEBS Meet. 31, 125–136 (1975).

    Google Scholar 

  19. Lehrer, S. S., Betteridge, D. R., Graceffa, P., Wong, S. & Seidel, J. C. Biochemistry 23, 1591–1595 (1984).

    Article  CAS  Google Scholar 

  20. Pearlstone, J. & Smillie, L. B. J. biol. Chem. 258, 2534–2542 (1983).

    CAS  PubMed  Google Scholar 

  21. Nonomura, Y., Drabikowski, W. & Ebashi, S. J. Biochem., Tokyo 64, 419–422 (1968).

    Article  CAS  Google Scholar 

  22. Cohen, C., Caspar, D. L. D., Parry, D. A. D. & Lucas, R. M. Cold Spring Harb. Symp. quant. Biol. 36, 205–215 (1971).

    Article  CAS  Google Scholar 

  23. Margossian, S. S. & Cohen, C. J. molec. Biol. 81, 409–413 (1973).

    Article  CAS  Google Scholar 

  24. Ohtsuki, I. J. Biochem., Tokyo 75, 753–765 (1974).

    Article  CAS  Google Scholar 

  25. Stewart, M. & McLachlan, A. D. J. molec. Biol. 103, 251–260 (1976).

    Article  CAS  Google Scholar 

  26. Morris, E. P. & Lehrer, S. S. Biophys. J. 33, 239a (1981).

  27. Chong, P. C. S. & Hodges, R. S. J. biol. Chem. 257, 9152–9160 (1982).

    CAS  PubMed  Google Scholar 

  28. Pato, M. D., Mak, A. S. & Smillie, L. B. J. biol. Chem. 256, 602–607 (1981).

    CAS  PubMed  Google Scholar 

  29. Mak, A. S. & Smillie, L. B. J. molec. Biol. 149, 541–550 (1981).

    Article  CAS  Google Scholar 

  30. Yamaguchi, M., Ver, A., Carlos, A. & Seidel, J. C. Biochemistry 23, 774–779 (1984).

    Article  CAS  Google Scholar 

  31. Mahdavi, V., Periasamy, M. & Nadal-Ginard, B. Nature 297, 659–665 (1982).

    Article  ADS  CAS  Google Scholar 

  32. Nguyen, H. T., Wydro, R. M., Gubits, R. M. & Nadal-Ginard, B. Proc. natn. Acad. Sci. U.S.A. 79, 5230–5234 (1982).

    Article  ADS  CAS  Google Scholar 

  33. Wydro, R. M., Nguyen, H. T., Gubits, R. M. & Nadal-Ginard, B. J. biol. Chem. 258, 670–678 (1983).

    CAS  PubMed  Google Scholar 

  34. Lowey, S. & Risby, D. Nature 234, 81–85 (1971).

    Article  ADS  CAS  Google Scholar 

  35. Gauthier, G. F., Lowey, S. & Hobbs, A. W. Nature 274, 24–29 (1978).

    Article  ADS  Google Scholar 

  36. Nudel, U. et al. Proc. natn. Acad. Sci. U.S.A. 79, 2763–2767 (1982).

    Article  ADS  CAS  Google Scholar 

  37. Dhoot, G. K. & Perry, S. V. Nature 278, 714–718 (1979).

    Article  ADS  CAS  Google Scholar 

  38. Toyota, N. & Shimada, Y. J. Cell Biol. 91, 497–504 (1981).

    Article  CAS  Google Scholar 

  39. Toyota, N. & Shimada, Y. Cell 33, 297–304 (1983).

    Article  CAS  Google Scholar 

  40. Chakraborty, P. R., Ruiz-Opazo, N., Shouval, D. & Shafritz, D. A. Nature 286, 531–533 (1980).

    Article  ADS  CAS  Google Scholar 

  41. Wood, K. O. & Lee, J. C. Nucleic Acids Res. 3, 1961–1971 (1976).

    Article  CAS  Google Scholar 

  42. Zain, S., Sambrook, J., Roberts, R. J., Keller, W., Fried, M. & Dunn, A. R. Cell 16, 851–861 (1979).

    Article  CAS  Google Scholar 

  43. Soeiro, R., Birnboim, H. C. & Darnell, J. E. J. molec. Biol. 19, 362–372 (1966).

    Article  CAS  Google Scholar 

  44. Garfinkel, L. I., Periasamy, M. & Nadal-Ginard, B. J. biol. Chem. 257, 11078–11086 (1982).

    CAS  PubMed  Google Scholar 

  45. Sanger, F., Nichlen, S. & Coulson, A. R. Proc. natn. Acad. Sci. U.S.A. 74, 5463–5467 (1977).

    Article  ADS  CAS  Google Scholar 

  46. Mahadavi, V., Chambers, A. P. & Nadal-Ginard, B. Proc. natn. Acad. Sci. U.S.A. 81, 2626–2630 (1984).

    Article  ADS  Google Scholar 

  47. Casey, J. & Davidson, N. Nucleic Acids Res. 4, 1539 (1977).

    Article  CAS  Google Scholar 

  48. Berk, A. J. & Sharp, P. A. Cell 12, 721 (1977).

    Article  CAS  Google Scholar 

Download references

Author information

Author notes

  1. Judah Weinberger

    Present address: Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, 02115, USA

Authors and Affiliations

  1. Laboratory of Molecular and Cellular Cardiology, Department of Cardiology, Children's Hospital and Department of Pediatrics, Harvard Medical School, 300 Longwood Avenue, Boston, Massachusetts, 02115, USA

    Nelson Ruiz-Opazo, Judah Weinberger & Bernardo Nadal-Ginard

Authors
  1. Nelson Ruiz-Opazo
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Judah Weinberger
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Bernardo Nadal-Ginard
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Ruiz-Opazo, N., Weinberger, J. & Nadal-Ginard, B. Comparison of α-tropomyosin sequences from smooth and striated muscle. Nature 315, 67–70 (1985). https://doi.org/10.1038/315067a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/315067a0

This article is cited by

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.

Search

Advanced search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing