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Characterization of the effects of phosphorylation by CK2 on the structure and binding properties of human HP1β
Author(s) -
Munari Francesca,
Gajda Michal Jan,
Hiragami-Hamada Kyoko,
Fischle Wolfgang,
Zweckstetter Markus
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.02.019
Subject(s) - heterochromatin protein 1 , chromatin , heterochromatin , phosphorylation , microbiology and biotechnology , chemistry , casein kinase 2 , biophysics , biochemistry , protein kinase a , biology , dna , cyclin dependent kinase 2
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.