Nonenzymatic acetylation of histones with acetyl phosphate and acetyl adenylate.
Nonenzymatic acetylation of calf-thymus lysine- and arginine-rich histones was demonstrated to occur when these proteins were incubated with [14C]acetyl phosphate and [14C]acetyl adenylate. The levels of acetylation depend on both pH and on reagent concentration. When acetyl [33P]phosphate and acetyl [3H]adenylate were used as reagents, we found neither histone phosphorylation nor adenylylation. Most of the radioactivity of 14C-labeled acetylated histones was recovered as Ne-acetyllysine. Furthermore, only a small amount of O-bound radioactivity was released by the 14C-labeled acetylated arginine-rich histone during treatment with hydroxylamine. Experiments on the acetylation of histones, in the presence of increasing salt concentration, gave different results for the two acetylating agents.
D000085:Acetates; D000249:Adenosine Monophosphate / Q000031:analogs & derivatives*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001120:Arginine; D001665:Binding Sites; D001667:Binding, Competitive; D002250:Carbon Radioisotopes; D002417:Cattle; D006657:Histones; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008239:Lysine; D009943:Organophosphorus Compounds; D009994:Osmolar Concentration; D010761:Phosphorus Radioisotopes; D011189:Potassium Chloride; D011485:Protein Binding; D013950:Thymus Gland; D014316:Tritium
D000085:Acetates; D000596:Amino Acids; D002250:Carbon Radioisotopes; D006657:Histones; D009943:Organophosphorus Compounds; D010761:Phosphorus Radioisotopes; D014316:Tritium; D000249:Adenosine Monophosphate; D011189:Potassium Chloride; D001120:Arginine; D008239:Lysine