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Title 

Phosphorylation of serine-10 of histone H3 shields modified lysine-9 selectively during mitosis

Authors 

Young Sun JoungSun Hwa JoJung Sun ParkY KoYong-Kook Kang

Publisher 

Wiley-Blackwell

Issue Date 

2010

Citation 

Genes to Cells, vol. 15, no. 3, pp. 181-192

Abstract 

Post-translational modifications of histones play important roles in regulating chromatin dynamics and epigenetic inheritance during mitosis. The epigenetic significance and stability of histone H3-lysine 9 (H3K9) modifications have been well studied in interphase cells, whereas not as much in mitotic cells. Here, we inspected mitosis-coupled alterations in the global modifications of H3K9. Signals for H3K9 mono-, di-methylation and acetylation became invisible as cells entered mitosis in contrast to the pattern observed for H3-serine 10 phosphorylation (H3S10ph). Treatment with the aurora-B inhibitor ZM447439 or expression of the dominant negative mutant Aur-BK106R resulted in prometaphase chromosomes that lacked signals for H3S10ph but were positive for H3K9 modifications. Trimethylation was the sole K9 modification that remained consistently detectable throughout the cell cycle. This phenomenon was specific for H3K9-S10, as this pattern was not observed at H3K27-S28. Methylated H3K27 remained detectable throughout the cell cycle, despite phosphorylation of the adjacent H3S28. Contrastingly, our dot-blot experiment using synthetic peptides showed that phosphorylation of serine residue basically kept adjacent lysine from antibody access. Together, these results suggest that phosphorylation of serine residue occurs in a selective manner, being influenced by the types of modifications and the nature of neighboring lysine residues.

ISSN 

1356-9597

Link 

http://dx.doi.org/10.1111/j.1365-2443.2009.01375.x

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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