2013
DOI: 10.1016/j.jmb.2012.10.018
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Hinge and Chromoshadow of HP1α Participate in Recognition of K9 Methylated Histone H3 in Nucleosomes

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Cited by 47 publications
(83 citation statements)
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“…Previous studies have shown that both human HP1α and the S. pombe HP1 protein, Swi6, display a lower specificity for the H3K9me3 mark in mononucleosomes than in H3-tail peptides, and that this specificity increases when assayed using nucleosome arrays (27,30). To further characterize the role of HP1α's N-terminal phosphorylation in its nucleosome binding, we examined HP1α's binding to a 12-mer nucleosome array with or without the H3Kc9me3 mark.…”
Section: Resultsmentioning
confidence: 99%
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“…Previous studies have shown that both human HP1α and the S. pombe HP1 protein, Swi6, display a lower specificity for the H3K9me3 mark in mononucleosomes than in H3-tail peptides, and that this specificity increases when assayed using nucleosome arrays (27,30). To further characterize the role of HP1α's N-terminal phosphorylation in its nucleosome binding, we examined HP1α's binding to a 12-mer nucleosome array with or without the H3Kc9me3 mark.…”
Section: Resultsmentioning
confidence: 99%
“…Previous studies have indicated that two stretches of basic residues in the hinge region are critical for HP1's ability to bind DNA (30,32). However, the N-terminal and hinge regions are physically separated by the CD, and the functional interactions between these regions have yet to be defined.…”
Section: Resultsmentioning
confidence: 99%
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