Large histone H3 lysine 9 dimethylated chromatin blocks distinguish differentiated from embryonic stem cells
نویسندگان
چکیده
منابع مشابه
Hypoxic stress induces dimethylated histone H3 lysine 9 through histone methyltransferase G9a in mammalian cells.
Dimethylated histone H3 lysine 9 (H3K9me2) is a critical epigenetic mark for gene repression and silencing and plays an essential role in embryogenesis and carcinogenesis. Here, we investigated the effects of hypoxic stress on H3K9me2 at both global and gene-specific level. We found that hypoxia increased global H3K9me2 in several mammalian cell lines. This hypoxia-induced H3K9me2 was temporall...
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In most eukaryotes, the histone methyltransferase SU(VAR)3-9 and its orthologues play amajor role in the function of centromeric heterochromatin. Although the methyltransferase domain isrequired for the formation of a fully functional centromere, mutations within other regions of the genesuch as the N-terminus also have a strong impact on its in vivo function. To analyze the contrib...
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Embryonic stem cell (ESC) chromatin is characterized by a unique set of histone modifications, including enrichment for H3 lysine 9 acetylation (H3K9ac). Recent studies suggest that histone deacetylase (HDAC) inhibitors promote pluripotency. Here, using H3K9ac ChIP followed by high throughput sequencing analyses and gene expression in E14 mouse ESCs before and after treatment with a low level o...
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متن کاملThe preRC protein ORCA organizes heterochromatin by assembling histone H3 lysine 9 methyltransferases on chromatin
Heterochromatic domains are enriched with repressive histone marks, including histone H3 lysine 9 methylation, written by lysine methyltransferases (KMTs). The pre-replication complex protein, origin recognition complex-associated (ORCA/LRWD1), preferentially localizes to heterochromatic regions in post-replicated cells. Its role in heterochromatin organization remained elusive. ORCA recognizes...
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ژورنال
عنوان ژورنال: Nature Genetics
سال: 2009
ISSN: 1061-4036,1546-1718
DOI: 10.1038/ng.297