Truncated HP1 lacking a functional chromodomain induces heterochromatinization upon in vivo targeting

Maartje C. Brink, Yme Van Der Velden, Wim De Leeuw, Julio Mateos-Langerak, Andrew S. Belmont, Roel Van Driel, Pernette J. Verschure

Research output: Contribution to journalArticlepeer-review


Packaging of the eukaryotic genome into higher order chromatin structures is tightly related to gene expression. Pericentromeric heterochromatin is typified by accumulations of heterochromatin protein 1 (HP1), methylation of histone H3 at lysine 9 (MeH3K9) and global histone deacetylation. HP1 interacts with chromatin by binding to MeH3K9 through the chromodomain (CD). HP1 dimerizes with itself and binds a variety of proteins through its chromoshadow domain. We have analyzed at the single cell level whether HP1 lacking its functional CD is able to induce heterochromatinization in vivo. We used a lac-operator array-based system in mammalian cells to target EGFP-lac repressor tagged truncated HP1α and HP1β to a lac operator containing gene-amplified chromosome region in living cells. After targeting truncated HP1α or HP1β we observe enhanced tri-MeH3K9 and recruitment of endogenous HP1α and HP1β to the chromosome region. We show that CD-less HP1α can induce chromatin condensation, whereas the effect of truncated HP1β is less pronounced. Our results demonstrate that after lac repressor-mediated targeting, HP1α and HP1β without a functional CD are able to induce heterochromatinization.

Original languageEnglish (US)
Pages (from-to)53-61
Number of pages9
JournalHistochemistry and Cell Biology
Issue number1-2
StatePublished - Jan 2006


  • Epigenetics
  • Gene expression
  • Heterochromatin protein 1
  • Histone methylation
  • Large-scale chromatin structure

ASJC Scopus subject areas

  • Histology
  • Molecular Biology
  • Medical Laboratory Technology
  • Cell Biology


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