Nucleosomal structure as probed by H3 histone thiol reactivity - Conformation of H3 histone variants is differently affected by thiol group reagents

Nicoletta Ferrari, Ulrich Pfeffer, Giorgio Vidali

Research output: Contribution to journalArticlepeer-review

Abstract

Two H3 histone variants are found in equal amount in HeLa cells, and they have been characterized by two-dimensional gel electrophoresis followed by reaction with specific antibodies. These molecules are the only cysteine-containing histones, and they have been used as the target for thiol-specific reagents, in intact nuclei, isolated nucleosomes, histone complexes, and purified histones. Cysteine residues are available to N-ethylmaleimide only when histones are disassembled from the core particles. Upon reaction with these reagents, one of the H3 variants undergoes profound conformational changes, as revealed by an altered electrophoretic mobility.

Original languageEnglish
Pages (from-to)1-13
Number of pages13
JournalCell Biophysics
Volume10
Issue number1
DOIs
Publication statusPublished - Feb 1987

Keywords

  • H3 thiol reactivity
  • histone acetylation
  • Nucleosonal structure

ASJC Scopus subject areas

  • Cell Biology
  • Biophysics

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