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Histone H1 is located in the interior of the chromatin 30-nm filament

Abstract

THE linker histone H1 binds to the nucleosome and is essential for the organization of nucleosomes into the 30-nm filament of chromatin1. It has been implicated in the repression of transcription2–5, and phosphorylation of H1 may be involved in cell-cycle-dependent chromatin condensation and decondensation6. A long-standing issue concerns the location of H1 in the chromatin filament7. The original solenoidal model8 proposes that H1 is inside the 30-nm filament, but other models, also helical, suggest a variable9 or more accessible10 location for H1. Investigations to determine the location of the linker histone based on its access-ibility to antibodies11–15 or immobilized proteases16 under various ionic conditions have yielded conflicting results. Here we use neutron scattering in a direct structural determination to show that H1 is located in the interior of the filament.

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References

  1. Thoma, F., Koller, T. & Klug, A. J. Cell Biol. 83, 403–427 (1979).

    Article  CAS  Google Scholar 

  2. Schlissel, M. S. & Brown, D. D. Cell 37, 903–913 (1984).

    Article  CAS  Google Scholar 

  3. Wolffe, A. P. & Brown, D. D. Science 241, 1626–1632 (1988).

    Article  ADS  CAS  Google Scholar 

  4. Kamakaka, R. T. & Thomas, J. O. EMBO J. 9, 3997–4006 (1990).

    Article  CAS  Google Scholar 

  5. Croston, G. E., Kerrigan, L. A., Lira, L. M., Marshak, D. R. & Kadonaga, J. T. Science 251, 643–649 (1991).

    Article  ADS  CAS  Google Scholar 

  6. Roth, S. Y. & Allis, C. D. Trends biochem. Sci. 17, 93–98 (1992).

    Article  CAS  Google Scholar 

  7. Felsenfeld, G. & McGhee, J. D. Cell 44, 375–377 (1986).

    Article  CAS  Google Scholar 

  8. Finch, J. T. & Klug, A. Proc. natn. Acad. Sci. U.S.A. 73, 1897–1901 (1976).

    Article  ADS  CAS  Google Scholar 

  9. McGhee, J. D., Nickol, J. D., Felsenfeld, G. & Rau, D. C. Cell 33, 831–841 (1983).

    Article  CAS  Google Scholar 

  10. Woodcock, C. L. F., Frado, L.-L & Rattner, J. B. J. Cell Biol. 99, 42–52 (1984).

    Article  CAS  Google Scholar 

  11. Dimitrov, S. I., Russanova, V. R. & Pashev, I. G. EMBOJ. 6, 2387–2392 (1987).

    Article  CAS  Google Scholar 

  12. Russanova, V. R., Dimitrov, S. I., Makarov, V. L. & Pashev, I. G. Eur. J. Biochem. 167, 321–326 (1987).

    Article  CAS  Google Scholar 

  13. Cattini, P. A. & Allan, J. J. Histochem. Cytochem. 36, 425–432 (1988).

    Article  CAS  Google Scholar 

  14. Thibodeau, A. & Ruiz-Carrillo, A. J. biol. Chem. 263, 16236–16241 (1988).

    CAS  PubMed  Google Scholar 

  15. Banchev, T. B., Srebeva, L. N. & Zlatanova, J. S. Molec. cell. Biochem. 95, 167–175 (1990).

    Article  CAS  Google Scholar 

  16. Leuba, S. H., Zlatanova, J. & van Holde, K. J. molec. Biol. 229, 917–929 (1993).

    Article  CAS  Google Scholar 

  17. Suau, P., Bradbury, E. M. & Baldwin, J. P. Eur. J. Biochem. 97, 593–602 (1979).

    Article  CAS  Google Scholar 

  18. Gerchman, S. E. & Ramakrishnan, V. Proc. natn. Acad. Sci. U.S.A. 84, 7802–7806 (1987).

    Article  ADS  CAS  Google Scholar 

  19. Serdyuk, I. N. Brookhaven Symp. Biol. 27, IV:49–60 (1975).

    Google Scholar 

  20. Lasters, I. et al. Eur. J. Biochem. 151, 283–289 (1985).

    Article  CAS  Google Scholar 

  21. Graziano, V., Gerchman, S. E. & Ramakrishnan, V. J. molec. Biol. 203, 997–1007 (1988).

    Article  CAS  Google Scholar 

  22. Hayes, J. J. & Wolffe, A. P. Proc. natn. Acad. Sci. U.S.A. 90, 6415–6419 (1993).

    Article  ADS  CAS  Google Scholar 

  23. Caron, F. & Thomas, J. O. J. molec. Biol. 146, 513–537 (1981).

    Article  CAS  Google Scholar 

  24. Thomas, J. O. & Rees, C. Eur. J. Biochem. 134, 109–115 (1983).

    Article  CAS  Google Scholar 

  25. Graziano, V. & Ramakrishnan, V. J. molec. Biol. 214, 897–910 (1990).

    Article  CAS  Google Scholar 

  26. Studier, F. W., Rosenberg, A. H., Dunn, J. J. & Dubendorff, J. W. Meth. Enzym. 185, 61–89 (1990).

    Google Scholar 

  27. Shannon, M. F. & Wells, J. R. E. J. biol. Chem. 262, 9664–9668 (1987).

    CAS  PubMed  Google Scholar 

  28. Porod, G. in Small Angle X-ray Scattering (eds Glatter, O. & Kratky, O.) 17–33 (Academic, London, 1982).

    Google Scholar 

  29. Ibel, K. & Stuhrmann, H. J. molec. Biol. 93, 255–265 (1975).

    Article  CAS  Google Scholar 

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Graziano, V., Gerchman, S., Schneider, D. et al. Histone H1 is located in the interior of the chromatin 30-nm filament. Nature 368, 351–354 (1994). https://doi.org/10.1038/368351a0

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