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Nucleic Acids Res. 2018 Jan 9;46(1):189-202. doi: 10.1093/nar/gkx1010.

Regulation of transcriptional silencing and chromodomain protein localization at centromeric heterochromatin by histone H3 tyrosine 41 phosphorylation in fission yeast.

Author information

1
Department of Biochemistry, National University of Singapore, Yong Loo Lin School of Medicine, Singapore.
2
Department of Biological Sciences, National University of Singapore.
3
Cancer Science Institute, National University of Singapore, Yong Loo Lin School of Medicine, Singapore.
4
National University Health System (NUHS), Singapore.

Abstract

Heterochromatin silencing is critical for genomic integrity and cell survival. It is orchestrated by chromodomain (CD)-containing proteins that bind to methylated histone H3 lysine 9 (H3K9me), a hallmark of heterochromatin. Here, we show that phosphorylation of tyrosine 41 (H3Y41p)-a novel histone H3 modification-participates in the regulation of heterochromatin in fission yeast. We show that a loss-of-function mutant of H3Y41 can suppress heterochromatin de-silencing in the centromere and subtelomere repeat regions, suggesting a de-silencing role for H3Y41p on heterochromatin. Furthermore, we show both in vitro and in vivo that H3Y41p differentially regulates two CD-containing proteins without the change in the level of H3K9 methylation: it promotes the binding of Chp1 to histone H3 and the exclusion of Swi6. H3Y41p is preferentially enriched on centromeric heterochromatin during M- to early S phase, which coincides with the localization switch of Swi6/Chp1. The loss-of-function H3Y41 mutant could suppress the hypersensitivity of the RNAi mutants towards hydroxyurea (HU), which arrests replication in S phase. Overall, we describe H3Y41p as a novel histone modification that differentially regulates heterochromatin silencing in fission yeast via the binding of CD-containing proteins.

PMID:
29136238
PMCID:
PMC5758876
DOI:
10.1093/nar/gkx1010
[Indexed for MEDLINE]
Free PMC Article

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