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  N-terminal phosphorylation of HP1α increases its nucleosome-binding specificity.

Nishibuchi, G., Machida, S., Osakabe, A., Murakoshi, H., Hiragami-Hamada, K., Nakagawa, R., et al. (2014). N-terminal phosphorylation of HP1α increases its nucleosome-binding specificity. Nucleic Acids Research, 42(20), 12498-12511. doi:10.1093/nar/gku995.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0025-024D-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CC4B-F
Genre: Journal Article

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Nishibuchi, G., Author
Machida, S., Author
Osakabe, A., Author
Murakoshi, H., Author
Hiragami-Hamada, K.1, Author              
Nakagawa, R., Author
Fischle, W.1, Author              
Nishimura, Y., Author
Kurumizaka, H., Author
Tagami, H., Author
Nakayama, J., Author
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1Research Group of Chromatin Biochemistry, MPI for Biophysical Chemistry, Max Planck Society, ou_578604              

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 Abstract: Heterochromatin protein 1 (HP1) is an evolutionarily conserved chromosomal protein that binds to lysine 9-methylated histone H3 (H3K9me), a hallmark of heterochromatin. Although HP1 phosphorylation has been described in several organisms, the biological implications of this modification remain largely elusive. Here we show that HP1's phosphorylation has a critical effect on its nucleosome binding properties. By in vitro phosphorylation assays and conventional chromatography, we demonstrated that casein kinase II (CK2) is the kinase primarily responsible for phosphorylating the N-terminus of human HP1α. Pull-down assays using in vitro-reconstituted nucleosomes showed that unmodified HP1α bound H3K9-methylated and H3K9-unmethylated nucleosomes with comparable affinity, whereas CK2-phosphorylated HP1α showed a high specificity for H3K9me3-modified nucleosomes. Electrophoretic mobility shift assays showed that CK2-mediated phosphorylation diminished HP1α's intrinsic DNA binding, which contributed to its H3K9me-independent nucleosome binding. CK2-mediated phosphorylation had a similar effect on the nucleosome-binding specificity of fly HP1a and S. pombe Swi6. These results suggested that HP1 phosphorylation has an evolutionarily conserved role in HP1's recognition of H3K9me-marked nucleosomes.

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Language(s): eng - English
 Dates: 2014-10-202014-11-10
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1093/nar/gku995
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Title: Nucleic Acids Research
Source Genre: Journal
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Pages: - Volume / Issue: 42 (20) Sequence Number: - Start / End Page: 12498 - 12511 Identifier: -