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:

Nucleosome formation abolishes base-specific binding of histones

Abstract

CHROMATIN has a subunit structure1–5 and each subunit, for which the term nucleosome has been suggested5, has been proposed to consist of two of each of the four histones H2A, H2B, H3 and H4, and 200 base pairs of DNA (ref. 3). Do the histones responsible for generating the nucleosomes bind to specific sequences of the DNA? Heterologous reconstitution experiments showed that the four histones bound to DNA from bacteria or viruses gave rise to the same X-ray diffraction pattern6, the same size of nuclease-resistant DNA fragments7, and the same subunit structure, shown by electron microscopy5, as obtained for native chromatin. These findings suggest that the nucleosomes do not contain specific DNA sequences. This agrees with the apparently random distribution of nucleosomes along adenovirus DNA5. On the other hand, there is evidence that individual histones and polypeptides like polylysine or polyarginine bind preferentially to certain DNA sequences8–10.

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

Access options

Buy this article

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

Similar content being viewed by others

References

  1. Olins, A. L., and Olins, D. E., Science, 183, 330–332 (1974).

    Article  ADS  CAS  Google Scholar 

  2. Sahasrabuddhe, C. G., and Van Holde, K. E., J. biol. Chem., 249, 152–156 (1974).

    CAS  PubMed  Google Scholar 

  3. Kornberg, R. D., Science, 184, 868–871 (1974).

    Article  ADS  CAS  Google Scholar 

  4. Noll, M., Nature, 251, 249–251 (1974).

    Article  ADS  CAS  Google Scholar 

  5. Oudet, P., Gross-Bellard, M., and Chambon, P., Cell., 4, 281–300 (1975).

    Article  CAS  Google Scholar 

  6. Baldwin, J. P., Bradbury, E. M., Butler-Browne, G. S., and Stephens, R. M., FEBS Lett., 34, 133–136 (1973).

    Article  CAS  Google Scholar 

  7. Axel, R., Melchior, W., Jr, Sollner-Webb, B., and Felsenfeld, G., Proc. natn. Acad. Sci. U.S.A., 71, 4101–4105 (1974).

    Article  ADS  CAS  Google Scholar 

  8. Leng, M., and Felsenfeld, G., Proc. natn. Acad. Sci. U.S.A., 56, 1325–1332 (1966).

    Article  ADS  CAS  Google Scholar 

  9. Clark, R. J. and Felsenfeld, G., Nature new Biol., 240, 226–229 (1972).

    Article  CAS  Google Scholar 

  10. Hwan, J. C., Leffak, I. M., Li, H. J., Huang, P. C., and Mura, C., Biochemistry, 14, 1390–1396 (1975).

    Article  CAS  Google Scholar 

  11. Streeck, R. E., and Hobom, G., Eur. J. Biochem., 57, 595–606 (1975).

    Article  CAS  Google Scholar 

  12. Kornberg, R. D., and Thomas, J. O., Science, 184, 865–868 (1974).

    Article  ADS  CAS  Google Scholar 

  13. Van der Westhuyzen, D. R., and von Holt, C., FEBS Lett., 14, 333–337 (1971).

    Article  CAS  Google Scholar 

  14. Böhm, E. L., et al., FEBS Lett., 34, 217–221 (1973).

    Article  Google Scholar 

  15. Laemmli, U.K., Nature, 227, 680–685 (1970).

    Article  ADS  CAS  Google Scholar 

  16. Panyim, S., and Chalkley, R., Archs Biochem. Biophys., 130, 337–346 (1969).

    Article  CAS  Google Scholar 

  17. D'Anna, J. A., Jr, and Isenberg, I., Biochemistry, 13, 4992–4997 (1974).

    Article  CAS  Google Scholar 

  18. Johns, E. W. in Histories and Nucleohistones (edit. by Phililps, D. M. P.), 1–45 (Plenum, London and New York, 1971).

    Book  Google Scholar 

  19. Philippsen, P., Streeck, R. E., and Zachau, H. G., Eur. J. Biochem., 45, 479–488 (1974).

    Article  CAS  Google Scholar 

  20. Walz, A., and Pirotta, V., Nature, 254, 118–121 (1975).

    Article  ADS  CAS  Google Scholar 

  21. Richards, B. M., and Pardon, J. F., Expl Cell Res., 62, 184–196 (1970).

    Article  CAS  Google Scholar 

  22. Boseley, P. G., Bradbury, E. M., Butler-Browne, G. S., Carpenter, B. G., and Stephens, R. M., Eur. J. Biochem. (in the press).

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

STEINMETZ, M., STREECK, R. & ZACHAU, H. Nucleosome formation abolishes base-specific binding of histones. Nature 258, 447–450 (1975). https://doi.org/10.1038/258447a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/258447a0

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

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