Nonenzymatic acetylation of histones with acetyl phosphate and acetyl adenylate

Biochemistry. 1975 Jun 17;14(12):2681-5. doi: 10.1021/bi00683a018.

Abstract

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.

MeSH terms

  • Acetates
  • Adenosine Monophosphate / analogs & derivatives*
  • Amino Acids / analysis
  • Animals
  • Arginine
  • Binding Sites
  • Binding, Competitive
  • Carbon Radioisotopes
  • Cattle
  • Histones*
  • Hydrogen-Ion Concentration
  • Kinetics
  • Lysine
  • Organophosphorus Compounds*
  • Osmolar Concentration
  • Phosphorus Radioisotopes
  • Potassium Chloride
  • Protein Binding
  • Thymus Gland
  • Tritium

Substances

  • Acetates
  • Amino Acids
  • Carbon Radioisotopes
  • Histones
  • Organophosphorus Compounds
  • Phosphorus Radioisotopes
  • Tritium
  • Adenosine Monophosphate
  • Potassium Chloride
  • Arginine
  • Lysine