Modulation of the nucleosome structure by histone acetylation

Eur J Biochem. 1980 Sep;110(1):143-52. doi: 10.1111/j.1432-1033.1980.tb04849.x.

Abstract

A rapid procedure for the isolation of core particles from Chinese hamster ovary cells is described which permits measurements, usually at the day of their preparation. Particles of 145 +/- 5 base pairs, derived from interphase cells, will be compared with the analogue specimens from butyrate-treated cells, metaphase cells and a standard preparation from chicken erythrocytes. Butyrate cause an increase in the acetylation of histones H3 and H4, which induces alterations of the interhistone and histone-DNA interactions. Changes in the interhistone contacts, correlated to an extension of alpha-helical segments, lead to an altered accessibility of the H3 cysteine side-chains and to a different histone displacement by protamines. On the other hand, histone-DNA contacts are loosened in parts and this is particularly evident from the changes in the premelting region of a thermal-denaturation profile.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Animals
  • Butyrates
  • Cell Cycle
  • Chickens
  • Cricetinae
  • Cricetulus
  • Erythrocytes
  • Female
  • Histones*
  • Hot Temperature
  • Macromolecular Substances
  • Molecular Conformation
  • Nucleosomes* / drug effects
  • Ovary / cytology
  • Protamines / pharmacology

Substances

  • Butyrates
  • Histones
  • Macromolecular Substances
  • Nucleosomes
  • Protamines