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Heterochromatin Protein 1; Chromo domain; Chromoshadow; NMR; Structure; Phosphorylation
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 HP1 beta. 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 HP1 beta that do not compromise the ability of the protein to bind chromatin. (C) 2014 Federation of European Biochemical Societies.
