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

FEBS Lett. 2014 Apr 2;588(7):1094-9. doi: 10.1016/j.febslet.2014.02.019. Epub 2014 Feb 20.

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.

Keywords: Chromo domain; Chromoshadow; Heterochromatin Protein 1; NMR; Phosphorylation; Structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Casein Kinase II / chemistry*
  • Chromobox Protein Homolog 5
  • Chromosomal Proteins, Non-Histone / chemistry*
  • Chromosomal Proteins, Non-Histone / metabolism
  • Consensus Sequence
  • Heterochromatin / metabolism
  • Humans
  • Kinetics
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Phosphorylation
  • Protein Binding
  • Protein Processing, Post-Translational*

Substances

  • CBX1 protein, human
  • Chromosomal Proteins, Non-Histone
  • Heterochromatin
  • Chromobox Protein Homolog 5
  • Casein Kinase II