کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2047597 | 1074005 | 2014 | 6 صفحه PDF | دانلود رایگان |
• HP1β contains two primary sites for CK2 with distinct phosphorylation kinetics.
• Localized conformational and dynamic changes occur at the sites of phosphorylation.
• HP1β phosphorylated at S89 and S175 retains its ability to bind chromatin.
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.
Journal: FEBS Letters - Volume 588, Issue 7, 2 April 2014, Pages 1094–1099