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Cancer Associated Histone Mutations

ABSTRACT: Cancer Associated Histone Mutations

PROVIDER: PRJNA867413 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR20971556.fastq.gz	Fastqsanger.gz
	SRR20971557.fastq.gz	Fastqsanger.gz
	SRR20971558.fastq.gz	Fastqsanger.gz
	SRR20971559.fastq.gz	Fastqsanger.gz
	SRR20971560.fastq.gz	Fastqsanger.gz

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Cancer-associated Histone H3 N-terminal arginine mutations disrupt PRC2 activity and impair differentiation

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Cancer-associated Histone H3 N-terminal arginine mutations disrupt PRC2 activity and impair differentiation [CUT&RUN]

Project description:Dysregulated epigenetic states are a hallmark of cancer and often arise from genetic alterations in epigenetic regulators. This includes missense mutations in histones, which, together with associated DNA, form nucleosome core particles. However, the oncogenic mechanisms of most histone mutations are unknown. Here, we demonstrate that cancer-associated histone mutations at arginines in the histone H3 N-terminal tail disrupt repressive chromatin domains, alter gene regulation, and dysregulate differentiation. We find that histone H3R2C and R26C mutants reduce transcriptionally repressive H3K27me3. While H3K27me3 depletion in cells expressing these mutants was exclusively observed on the minor fraction of histone tails harboring the mutations, the same mutants recurrently disrupted broad H3K27me3 domains in the chromatin context, including near developmentally regulated promoters. H3K27me3 loss led to de-repression of differentiation pathways, with concordant effects between H3R2 and H3R26 mutants despite different proximity to the PRC2 substrate, H3K27. Functionally, H3R26C-expressing mesenchymal progenitor cells and murine embryonic stem cell-derived teratomas demonstrated impaired differentiation. Collectively, these data show that cancer-associated H3 N-terminal arginine mutations reduce PRC2 activity and disrupt chromatin-dependent developmental functions, a cancer-relevant phenotype.

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Cancer-associated Histone H3 N-terminal arginine mutations disrupt PRC2 activity and impair differentiation [scRNA-Seq]