Acetylation of histones in isolated avian erythroid nuclei.
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. 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 cysteine. 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. 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. 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.
D000123:Acetyltransferases / Q000097:blood*; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002467:Cell Nucleus / Q000187:drug effects / Q000378:metabolism*; D002645:Chickens; D003513:Cycloheximide / Q000494:pharmacology; D004912:Erythrocytes / Q000378:metabolism*; D006657:Histones / Q000097:blood*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008345:Manganese / Q000494:pharmacology; D011188:Potassium / Q000494:pharmacology
D006657:Histones; D008345:Manganese; D003513:Cycloheximide; D000123:Acetyltransferases; D008274:Magnesium; D011188:Potassium; D002118:Calcium