Divergent Residues Within Histone H3 Dictate a Unique Chromatin Structure in Saccharomyces cerevisiae

Genetics. 2016 Jan;202(1):341-9. doi: 10.1534/genetics.115.180810. Epub 2015 Nov 3.


Histones are among the most conserved proteins known, but organismal differences do exist. In this study, we examined the contribution that divergent amino acids within histone H3 make to cell growth and chromatin structure in Saccharomyces cerevisiae. We show that, while amino acids that define histone H3.3 are dispensable for yeast growth, substitution of residues within the histone H3 α3 helix with human counterparts results in a severe growth defect. Mutations within this domain also result in altered nucleosome positioning, both in vivo and in vitro, which is accompanied by increased preference for nucleosome-favoring sequences. These results suggest that divergent amino acids within the histone H3 α3 helix play organismal roles in defining chromatin structure.

Keywords: H3; S. cerevisiae; histone; nucleosome positioning.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Chromatin / chemistry*
  • Histones / chemistry*
  • Humans
  • Molecular Sequence Data
  • Nucleosomes
  • Recombinant Proteins
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / growth & development
  • Saccharomyces cerevisiae / ultrastructure*


  • Chromatin
  • Histones
  • Nucleosomes
  • Recombinant Proteins