Abstract
Histone H4 is a highly conserved structural component of the nucleosome subunit of chromatin. The activation of chromatin is accompanied by changes in structure which may be caused by histone modification or by interactions of specific non-histone proteins, or both. Histone H4 can be modified by acetylation and this modification has been correlated with chromosome assembly1 and with transcription2. We have now tested these correlations by studying H4 acetate content as a function of the cell cycle using the naturally synchronous cell cycle in Physarum polycephalum. The results show two clear correlations: (1) tetra-acetylated H4 correlates with transcription; (2) highly acetylated H4 (2 to 4 acetates per molecule) is inversely correlated with HI phosphorylation and initiation of chromosome condensation in prophase. The results are consistent with turnover of di-acetylated H4 during chromosome assembly in S phase.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Dixon, G. H. et al. Ciba Fdn Symp. 28, 229–258 (1975).
Allfrey, V. G. in Chromatin and Chromosome Structure (eds Li, H. J. & Eckhardt, R. A.) 167–191 (Academic, New York, 1977).
Mohberg, J. & Rusch, H. P. Archs Biochem. Biophys. 134, 577–585 (1969).
Corbett, S., Miller, S., Robinson, V. J., Matthews, H. R. & Bradbury, E. M. Trans. biochem. Soc. 5, 943–946 (1977).
Bradbury, E. M., Inglis, R. J., Matthews, H. R. & Sarner, N. Eur. J. Biochem. 33, 131–139 (1973).
Riggs, M. G., Whittaker, R. G., Neumann, J. R. & Ingram, V. M. Nature 268, 463–464 (1977).
Ruiz-Carrillo, A., Waugh, L. J. & Allfrey, V. G. Science 190, 117–128 (1975).
Panyim, S. & Chalkley, R. Biochemistry 8, 3972–3977 (1969).
Jackson, V., Shires, A., Tanphaichitr & Chalkley, R. J. molec. Biol. 104, 471–483 (1976).
Braun, R., Mittermayer, C. & Rusch, H. P. Biochim. biophys. Acta 114, 527–535 (1966).
Mittermayer, C., Braun, R. & Rusch, H. P. Biochim. biophys. Acta 91, 387–398 (1964).
Grant, W. D. Eur. J. Biochem. 29, 94–98 (1972).
Davies, K. E. & Walker, I. O. J. Cell Sci. 26, 267–279 (1977).
Sauer, H. W. in Cell Cycle Regulation (eds Jeter, J. R. et al.) 149–156 (Academic, New York, 1978).
Matthews, H. R. in The Cell Cycle (ed. Johns, P.) (Cambridge University Press, in the press).
Molgaard, H. V., Matthews, H. R. & Bradbury, E. M. Eur. J. Biochem. 68, 541–549 (1976).
Vogt, V. & Braun, R. J. molec. Biochem. 106, 567–587 (1976).
D'Anna, J. A., Tobey, R. A., Barham, S. S. & Gurley, L. R. Biochem. biophys. Res. Commun. 77, 187–194 (1977).
Lake, R. S. & Salzmann, N. P. Biochemistry 11, 4817–4822 (1972).
Gurley, L. R., D'Anna, J. A., Barham, S. S., Deaven, L. L. & Tobey, R. A. Eur. J. Biochem. 84, 1–16 (1978).
Matthews, H. R. in Protein Phosphorylation in Regulation (ed. Cohen, P.) (North-Holland, Amsterdam, 1978).
Cary, P. D., Moss, T. & Bradbury, E. M. Eur. J. Biochem. 89, 475–482 (1978).
Whitlock, J. & Simpson, R. T. J. biol. Chem. 252, 6516–6520 (1977).
Vidali, G., Boffa, L. C., Bradbury, E. M. & Allfrey, V. G. Proc. natn. Acad. Sci. U.S.A. 75, 2239–2243 (1978).
Mathis, D. J., Oudet, P., Wasylyk, B. & Chambon, P. Nucleic Acids Res. 5, 3523–3547 (1978).
Finch, J. T. & Klug, A. Proc. natn. Acad. Sci. U.S.A. 73, 1897–1901 (1976).
Carpenter, B. G., Baldwin, J. P., Bradbury, E. M. & Ibel, K. Nucleic Acids Res. 3, 1739–1746 (1976).
Suau, P., Bradbury, E. M. & Baldwin, J. P. Eur. J. Biochem. 97, 593–602 (1979).
Johnson, E. M., Allfrey, V. G., Bradbury, E. M. & Matthews, H. R. Proc. natn. Acad. Sci. U.S.A. 75, 1116–1120 (1978).
Adolph, K. W., Cheng, S. M. & Laemmli, U. K. Cell 12, 805–816 (1977).
Goodwin, G. H. & Johns, E. W. Eur. J. Biochem. 40, 215–220 (1973).
Levy-W., B., Wong, N. C. W. & Dixon, G. H. Proc. natn. Acad. Sci. U. S. A. 74, 2810–2814 (1977).
Vidali, G., Boffa, L. & Allfrey, V. G. Cell 12, 408–415 (1977).
Weisbrod, S. & Weintraub, H. Proc. natn. Acad. Sci. U.S.A. 76, 635–650 (1979).
Laemmli, U. K. Nature 227, 680–682 (1970).
Borun, T. W., Ajiro, K., Zweidler, A., Dolby, T. W. & Stephens, R. E. J. biol. Chem. 252, 173–180 (1977).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Chahal, S., Matthews, H. & Bradbury, E. Acetylation of histone H4 and its role in chromatin structure and function. Nature 287, 76–79 (1980). https://doi.org/10.1038/287076a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/287076a0
This article is cited by
-
Chemical “Diversity” of Chromatin Through Histone Variants and Histone Modifications
Current Molecular Biology Reports (2015)
-
Transcription of mononucleosomal particles acetylated in the presence of n-butyrate
Molecular Biology Reports (1993)
-
Treatment with sodium butyrate inhibits the complete condensation of interphase chromatin
Chromosoma (1988)
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.