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Characterization of the effects of phosphorylation by CK2 on the structure and binding properties of human HP1 beta.

MPS-Authors
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Munari,  F.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Gajda,  M. J.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

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Fischle,  W.
Research Group of Chromatin Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

Fulltext (public)

2019163.pdf
(Publisher version), 2MB

Supplementary Material (public)

2019163_Suppl.pdf
(Supplementary material), 971KB

Citation

Munari, F., Gajda, M. J., Hiragami-Hamada, K., Fischle, W., & Zweckstetter, M. (2014). Characterization of the effects of phosphorylation by CK2 on the structure and binding properties of human HP1 beta. FEBS Letters, 588(7), 1094-1099. doi:10.1016/j.febslet.2014.02.019.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0019-0540-A
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.