Histone hyperacetylation: its effects on nucleosome conformation and stability

Biochemistry. 1986 Mar 25;25(6):1421-8. doi: 10.1021/bi00354a035.


We have prepared nucleosome particles from HeLa cells that have been subjected to butyrate treatment. Fractions containing different levels of acetylation have been obtained within the range 7-17 acetyl groups per nucleosome. We have put special emphasis in the characterization of the particles with the highest level of histone acetylation. At low to physiological ionic strengths, these nucleosomes exhibit only small differences in hydrodynamic behavior and circular dichroism from control particles with minimal acetylation. There are, however, significant differences in thermal denaturation and nuclease sensitivity. In terms of stability toward high salt, the hyperacetylated and control particles behave identically. A model that reconciles these results is proposed. The major conclusion from our results, however, is that, at physiological ionic strength and in the absence of factors other than acetylation, the highly hyperacetylated nucleosomes remain essentially folded.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetylation
  • Cell Fractionation / methods
  • Cell Nucleus / ultrastructure
  • Chromatin / ultrastructure
  • Circular Dichroism
  • DNA, Neoplasm / isolation & purification
  • Electrophoresis, Polyacrylamide Gel
  • HeLa Cells / analysis
  • Histones / isolation & purification*
  • Humans
  • Molecular Weight
  • Nucleic Acid Denaturation
  • Nucleosomes / ultrastructure*
  • Osmolar Concentration
  • Protein Conformation
  • Protein Denaturation
  • Protein Processing, Post-Translational
  • Sodium Chloride


  • Chromatin
  • DNA, Neoplasm
  • Histones
  • Nucleosomes
  • Sodium Chloride