Acetylation of histones in isolated avian erythroid nuclei

https://doi.org/10.1016/0005-2787(77)90350-1Get rights and content

Abstract

  • 1.

    1. Suspensions of avian erythroid nuclei, of high purity, were prepared. Acetylation of histones was observed when nuclei were incubated in the presence of [1-14C]acetyl CoA, but not in the presence of sodium [3H]acetate.

  • 2.

    2. The acetylation reaction was very heat labile and reproduced the in vivo reaction with high fidelity. The reaction was strongly inhibited by divalent cations and by cysteine.

  • 3.

    3. Studies, in which intact cells were pre-incubated with cycloheximide prior to the isolation of nuclei, suggested that histone acetylation in isolated erythroid nuclei was largely independent of histone synthesis.

  • 4.

    4. The pH profile suggested the presence of at least two histone acetyltransferases, with pH optima at 8.0 and 8.6. Acetylation of histone H4 appeared to be favoured at pH 8.0.

  • 5.

    5. Studies on histone acetylation in isolated nuclei should be very useful in correlating observations on histone acetylation in vivo, with experiments using purified histone acetyltransferases.

References (29)

  • H. Nohara et al.

    Biochim. Biophys. Acta

    (1968)
  • D. Gallwitz

    Biochem. Biophys. Res. Commun.

    (1970)
  • D. Gallwitz et al.

    Biochim. Biophys. Acta

    (1972)
  • I. Sures et al.

    FEBS Lett.

    (1975)
  • H.I. Sarkander et al.

    FEBS Lett.

    (1975)
  • N.P. Madsen

    Anal. Biochem.

    (1969)
  • S. Panyim et al.

    Arch. Biochem. Biophys.

    (1969)
  • B.S. McEwen et al.

    J. Biol. Chem.

    (1963)
  • W.K. Paik et al.

    Biochim. Biophys. Acta

    (1970)
  • J. Bonner et al.

    Life Sciences

    (1974)
  • E.M. Bradbury
  • V.G. Allfrey
  • L.S. Hnilica
  • G.H. Dixon et al.
  • Cited by (0)

    View full text