Abstract
Based on studies of histone acetylation in vivo inPhysarum polycephalum, we present the following hypotheses: (1) Transcription-specific histone acetylation on histones H3 and H4 is a localized process at the nuclear matrix; (2) Histone acetylation in the S phase, which is specific for newly synthesized histones, occurs in an intranuclear nonlocalized process.
These hypotheses can explain: (1) the histone specificity of histone acetylation that is dependent on the functional state of the chromatin; (2) the apparent absence of turnover of histone acetylation in the bulk of the chromatin despite a definite low level of steady-state acetylation of all four core histones in bulk chromatin; (3) the pattern of butyrate-induced hyperacetylation observed for active and inactive chromatin.
Similar content being viewed by others
References
Waterborg, J. H., and Matthews, H. R. (1983),Biochemistry 22, 1489–1496.
Waterborg, J. H., and Matthews, H. R. (1984) Submitted.
Mende, L. M., Waterborg, J. H., Mueller, R. D., and Matthews, H. R. (1983),Biochemistry 22, 38–51.
Muldoon, J. J., Evans, T. E., Nygaard, O. D., and Evans, H. H. (1971),Biochim. Biophys. Acta 247, 310–321.
Evans, T. E., and Evans, H. H. (1980),J. Bacteriol. 143, 897–905.
Rao, B., and Gontcharoff, M. (1969),Exp. Cell Res. 56, 269–274.
Mohberg, J., Dworzak, E., and Sachsenmaier, W. (1980),Exptl. Cell Res. 126, 351–357.
Fouquet, H., Boehm, R., Wick, R., Sauer, H. W., and Scheller, K. (1975)Archiv. Biochem. Biophys. 168, 273–280.
Bonner, W. M., West, M. H. P., and Stedman, H. D. (1980),Eur. J. Biochem. 109, 17–23.
Johnson, E. M., Matthews, H. R., Littau, V. C., Lothstein, L., Bradbury, E. M., and Allfrey, V. G. (1978),Arch. Biochem. Biophys. 191, 537–550.
Waterborg, J. H., Fried, S. R., and Matthews, H. R. (1983),Eur. J. Biochem. 136, 245–252.
Waterborg, J. H., and Matthews, H. R. (1983),FEBS Lett. 162, 416–419.
Matthews, H. R., and Waterborg, J. H. (1983) inThe Enzymology of Post-Translational Modification of Proteins (Freedman, R., and Hawkins, H. C., eds.), Academic Press, London, in press, pp.
Chahal, S. S., Matthews, H. R., and Bradbury, E. M. (1980),Nature 287, 76–79.
Prior, C. P., Cantor, C. R., Johnson, E. M., Littau, V. C., and Allfrey, V. G. (1983),Cell,34 1033–1042.
Pierron, G., Sauer, H. W., Toublan, B., and Jalouzot, R. (1982),Eur. J. Cell Biol. 29, 104–113.
Thoma, F., Koller, T., and Klug, A. (1979),J. Cell. Biol. 83, 403–426.
Azorin, F., Perez-Grau, L., and Subirana, J. A. (1982),Chromosoma 85, 251–260.
Cavazza, B., Trefiletti, V., Pioli, F., Ricci, E., and Patrone, E. (1983),J. Cell Sci. 62, 81–102.
Weishood, S. (1982),Nature 297, 289–295.
Allan, J., Harborne, N., Rau, D. C., and Gould, H. (1982),J. Cell Biol. 92, 285–297.
Cary, P. D., Moss, T., and Bradbury, E. M. (1978),Eur. J. Biochem. 89, 475–482.
Rill, R. L., and Osterhof, D. K. (1982),J. Biol. Chem. 257, 14,875–14,880.
Brandt, W. F., Boehm, L., and Von Holt, C. (1975),FEBS Lett. 51, 88–93.
Boehm, L., Crane-Robinson, C., and Sautiere, P. (1980),Eur. J. Biochem. 106, 525–530.
Boehm, L., Briand, G., Sautiere, P., and Crane-Robinson, C. (1981),Eur. J. Biochem. 119, 67–74.
Boehm, L., Briand, G., Sautiere, P., and Crane-Robinson, C. (1982),Eur. J. Biochem. 123, 299–303.
Grigoryev, S. A., and Krashenninnikov, I. A. (1982),Eur. J. Biochem. 129, 119–125.
Mathis, D., Oudet, P., and Chambon, P. (1980),Progr. Nucl. Acid Res. Mol. Biol. 24, 1–55.
Sures, I., and Gallwitz, D. (1980),Biochem. 19, 943–951.
Dod, B., Kervabon, A., and Parello, J. (1982),Eur. J. Biochem. 121, 401–405.
Estepa, I., and Pestana, A. (1983),Eur. J. Biochem. 132, 249–254.
Wiktorowicz, J. E., and Bonner, J. (1982),J. Biol. Chem. 257, 12,893–12,900.
Boehm, J., Schlaeger, E.-J., and Knippers, R. (1980),Eur. J. Biochem. 112, 353–362.
Garcea, R. L., and Alberts, B. M. (1980),J. Biol. Chem. 255, 11,454–11,463.
Fukushima, M., Ota, K., Fujimoto, D., and Horiuchi, K. (1980),Biochem. Biophys. Res. Commun. 92, 1409–1414.
Waterborg, J. H., and Matthews, H. R. (1982),Anal. Biochem. 122, 313–318.
Waterborg, J. H., and Matthews, H. R. (1982),Exptl. Cell Res. 138, 462–466.
Kikuchi, H., and Fujimoto, D. (1973),FEBS Lett. 29, 280–282.
Hay, C. W., and Candido, E. P. M. (1983),J. Biol. Chem. 258, 3726–3734.
Dÿkwel, P. A., Mullenders, L. H. F., and Wanka, F. (1979),Nucleic Acids Res. 6, 219–230.
Pardoll, D. M., Vogelstein, B., and Coffey, D. S. (1980),Cell 19, 527–536.
McCready, S. J., Godwin, J., Mason, D. W., Brazell, I. A., and Cook, P. R. (1980),J. Cell Sci. 46, 365–386.
Berezney, R., and Buchholtz, L. A. (1981),Exptl. Cell Res. 132, 1–13.
Smith, H. C., and Berezney, R. (1983),Biochemistry 22, 3042–3046.
Pardoll, D. M., and Vogelstein, B. (1980),Exptl. Cell Res. 128, 466–470.
Clawson, G. A., and Smuckler A. E. (1980),Biochem. Biophys. Res. Commun. 96, 812–816.
Maundrell, K., Maxwell, E. S., Puvion, E., and Scherrer, K. (1981),Exptl. Cell Res. 136, 435–445.
Ben-Ze'ev, A., Abulafia, R., and Aloni, Y. (1982),EMBO J. 1, 1225–1231.
Robinson, S. I., Small, D., Idzerda, R., McKnight, G. S., and Vogelstein, B. (1983),Nucleic Acids Res. 11, 5113–5130.
Reeves, R., and Candido, E. P. M. (1980),Nucleic Acids Res. 8, 1947–1963.
Reeves, R., and Chang, D. (1983),J. Biol. Chem. 258, 679–687.
Wiegand, R. C., and Brutlag, D. L. (1981),J. Biol. Chem. 256, 4578–4583.
Horiuchi, K., and Fujimoto, D. (1972),J. Biochem. Tokyo 72, 433–438.
Ruiz-Carillo, A., Wangh, L. J., and Allfrey, V. G. (1975),Science 190, 117–128.
Woodland, H. R. (1979),Dev. Biol. 68, 360–370.
Moyne, G., Katinka, M., Saragosti, S., Chestier, A., and Yaniv, M. (1981),Progr. Nucl. Acid. Res. Mol. Biol. 26, 151–167.
Seale, R. L. (1981),Biochem. 20, 6432–6437.
Annunziato, A. T., and Seale, R. L. (1982),J. Cell Biol. 95, 73a.
Jackson, V., Shires, A., Chalkley, R., and Granner, D. K. (1975),J. Biol. Chem. 250, 4856–4863.
Jackson, V., Shires, A., Tanphaichitr, N., and Chalkley, R. (1976),J. Mol. Biol. 104, 471–483.
Cousens, L. S., Gallwitz, D., and Alberts, B. M. (1979),J. Biol. Chem. 254, 1716–1723.
Nelson, D., Covault, J., and Chalkley, R. (1980),Nucleic Acids Res. 8, 1745–1763.
Covault, J., and Chalkley, R. (1980),J. Biol. Chem. 255, 9110–9116.
Cousens, L. S., and Alberts, B. M. (1982),J. Biol. Chem. 257, 3945–3949.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Waterborg, J.H., Matthews, H.R. Intranuclear localization of histone acetylation inPhysarum polycephalum and the structure of functionally active chromatin. Cell Biophysics 5, 265–279 (1983). https://doi.org/10.1007/BF02788625
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF02788625
Index Entries
- Intranuclear localization, of histone acetylation
- localization
- intranuclear, of histone acetylation
- histone acetylation, intranuclear localization of
- acetylation, intranuclear localization of histone
- Physarum polycephalum, histone acetylation and chromatin structure in
- chromatin structure, inPhysarum polycephalum