Characterization of the effects of phosphorylation by CK2 on the structure and binding properties of human HP1β

Francesca Munari, Michal Jan Gajda, Kyoko Hiragami-Hamada, Wolfgang Fischle, Markus Zweckstetter*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Proteins of the Heterochromatin Protein 1 (HP1) family are regulators of chromatin structure and genome function in eukaryotes. Post-translational modifications expand the repertoire of the chemical diversity of HP1 proteins and regulate their activity. Here, we investigated the effect of phosphorylation by Casein kinase 2 (CK2) on the structure, dynamics and binding activity of human HP1β. We show that Ser89 in the hinge region is the most effective substrate, followed by Ser175 at the C-terminal tail. Phosphorylation at these sites results in localized conformational changes in HP1β that do not compromise the ability of the protein to bind chromatin.

Original languageEnglish (US)
Pages (from-to)1094-1099
Number of pages6
JournalFEBS Letters
Volume588
Issue number7
DOIs
StatePublished - Apr 2 2014

Keywords

  • Chromo domain
  • Chromoshadow
  • Heterochromatin Protein 1
  • NMR
  • Phosphorylation
  • Structure

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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