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Characterization of the effects of phosphorylation by CK2 on the structure and binding properties of human HP1β |
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| Authors: | Francesca Munari Michal Jan Gajda Kyoko Hiragami-Hamada Wolfgang Fischle Markus Zweckstetter |
| Institution: | 1. Department for NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany;2. German Center for Neurodegenerative Diseases (DZNE), Göttingen, Germany;3. Laboratory of Chromatin Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany;4. Center for Nanoscale Microscopy and Molecular Physiology of the Brain (CNMPB), University Medical Center, Göttingen, Germany |
| 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. |
| Keywords: | CK2 casein kinase 2 CD chromo domain CSD chromoshadow domain HP1 heterochromatin protein 1 MS mass spectrometry NMR nuclear magnetic resonance SAXS small angle X-ray scattering |
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