Histones H3/H4 form a tight complex with the inner nuclear membrane protein LBR and heterochromatin protein 1

EMBO Rep. 2001 Oct;2(10):920-5. doi: 10.1093/embo-reports/kve199. Epub 2001 Sep 24.


We have recently shown that heterochromatin protein 1 (HP1) interacts with the nuclear envelope in an acetylation-dependent manner. Using purified components and in vitro assays, we now demonstrate that HP1 forms a quaternary complex with the inner nuclear membrane protein LBR and a sub-set of core histones. This complex involves histone H3/H4 oligomers, which mediate binding of LBR to HP1 and cross-link these two proteins that do not interact directly with each other. Consistent with previous observations, HP1 and LBR binding to core histones is strongly inhibited when H3/H4 are modified by recombinant CREB-binding protein, revealing a new mechanism for anchoring domains of under-acetylated chromatin to the inner nuclear membrane.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Animals
  • Binding Sites
  • Blotting, Western
  • Cell Nucleus / metabolism
  • Dose-Response Relationship, Drug
  • Electrophoresis, Polyacrylamide Gel
  • Fishes
  • Glutathione Transferase / metabolism
  • Heterochromatin / metabolism
  • Histones / metabolism*
  • Intracellular Membranes / metabolism
  • Mice
  • Models, Biological
  • Plasmids / metabolism
  • Precipitin Tests
  • Protein Binding
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / metabolism
  • Recombinant Proteins / metabolism
  • Turkeys


  • Heterochromatin
  • Histones
  • Recombinant Fusion Proteins
  • Recombinant Proteins
  • Glutathione Transferase