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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-0540-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-2764-7
Genre: Journal Article

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 Creators:
Munari, F.1, Author              
Gajda, M. J.1, Author              
Hiragami-Hamada, K., Author
Fischle, W.2, Author              
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              
2Research Group of Chromatin Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578604              

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Free keywords: 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.

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Language(s): eng - English
 Dates: 2014-02-202014-04-02
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.febslet.2014.02.019
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Title: FEBS Letters
Source Genre: Journal
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Pages: - Volume / Issue: 588 (7) Sequence Number: - Start / End Page: 1094 - 1099 Identifier: -