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 language | English (US) |
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Pages (from-to) | 1094-1099 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 588 |
Issue number | 7 |
DOIs | |
State | Published - Apr 2 2014 |
Externally published | Yes |
Keywords
- Chromo domain
- Chromoshadow
- Heterochromatin Protein 1
- NMR
- Phosphorylation
- Structure
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology