Characterization of the effects of phosphorylation by CK2 on the structure and binding properties of human HP1β

Francesca Munari; Michal Jan Gajda; Kyoko Hiragami-Hamada; Wolfgang Fischle; Markus Zweckstetter

doi:10.1016/j.febslet.2014.02.019

Characterization of the effects of phosphorylation by CK2 on the structure and binding properties of human HP1β

Francesca Munari, Michal Jan Gajda, Kyoko Hiragami-Hamada, Wolfgang Fischle, Markus Zweckstetter^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

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.

Original language	English (US)
Pages (from-to)	1094-1099
Number of pages	6
Journal	FEBS Letters
Volume	588
Issue number	7
DOIs	https://doi.org/10.1016/j.febslet.2014.02.019
State	Published - Apr 2 2014
Externally published	Yes

Bibliographical note

Funding Information:
This work was supported by the Deutsche Forschungsgemeinschaft Collaborative Research Center 860 to M.Z. (project B2) and the Max Planck Society (W.F.). K.H.H. is supported by a Marie Curie Intra-European Fellowship for Career Development (IEF, FP7).

Keywords

Chromo domain
Chromoshadow
Heterochromatin Protein 1
NMR
Phosphorylation
Structure

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2014.02.019

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title = "Characterization of the effects of phosphorylation by CK2 on the structure and binding properties of human HP1β",

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 = "Chromo domain, Chromoshadow, Heterochromatin Protein 1, NMR, Phosphorylation, Structure",

author = "Francesca Munari and Gajda, {Michal Jan} and Kyoko Hiragami-Hamada and Wolfgang Fischle and Markus Zweckstetter",

note = "Funding Information: This work was supported by the Deutsche Forschungsgemeinschaft Collaborative Research Center 860 to M.Z. (project B2) and the Max Planck Society (W.F.). K.H.H. is supported by a Marie Curie Intra-European Fellowship for Career Development (IEF, FP7). ",

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AU - Munari, Francesca

AU - Gajda, Michal Jan

AU - Hiragami-Hamada, Kyoko

AU - Fischle, Wolfgang

AU - Zweckstetter, Markus

N1 - Funding Information: This work was supported by the Deutsche Forschungsgemeinschaft Collaborative Research Center 860 to M.Z. (project B2) and the Max Planck Society (W.F.). K.H.H. is supported by a Marie Curie Intra-European Fellowship for Career Development (IEF, FP7).

PY - 2014/4/2

Y1 - 2014/4/2

N2 - 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.

AB - 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.

KW - Chromo domain

KW - Chromoshadow

KW - Heterochromatin Protein 1

KW - NMR

KW - Phosphorylation

KW - Structure

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C2 - 24561199

AN - SCOPUS:84897076885

SN - 0014-5793

VL - 588

SP - 1094

EP - 1099

JO - FEBS Letters

JF - FEBS Letters

IS - 7

ER -

Characterization of the effects of phosphorylation by CK2 on the structure and binding properties of human HP1β

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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