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Homo sapiens

ABSTRACT: ChIP-seq of H3K27Ac in SKNO1 cells after knockdown of ASXL2

PROVIDER: PRJNA360173 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR5145757.fastq.gz	Fastqsanger.gz
	SRR5145758.fastq.gz	Fastqsanger.gz
	SRR5145759.fastq.gz	Fastqsanger.gz

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ChIP-seq of H3K27Ac in SKNO1 cells after knockdown of ASXL2

Project description:The goals of this study are to identify the changes of H3K27Ac in SKNO1 cells after knockdown of ASXL2

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Regulation of Histone Acetylation by SUMOylation Through TFAP2C Binding to the Chromatin and Recruitment of HDAC Complex

Project description:Enhancers are fundamental to gene regulation. Post-translational modifications by the small ubiquitin-like modifiers (SUMO) modify chromatin regulation enzymes, including histone acetylases and deacetylases. However, it remains unclear whether SUMOylation regulates enhancer marks, acetylation at the 27th lysine residue of the histone H3 protein (H3K27Ac). We hypothesize that SUMOylation regulates H3K27Ac. To test this hypothesis, we performed genome-wide ChIP-seq analyses. We discovered that knockdown (KD) of the SUMO activating enzyme catalytic subunit UBA2 reduced H3K27Ac at most enhancers. Bioinformatic analysis revealed that TFAP2C-binding sites are enriched in enhancers whose H3K27Ac was reduced by UBA2 KD. ChIP-seq analysis in combination with molecular biological methods showed that TFAP2C binding to enhancers increased upon UBA2 KD or inhibition of SUMOylation by a small molecule SUMOylation inhibitor. However, this is not due to the SUMOylation of TFAP2C itself. Proteomics analysis of TFAP2C interactome on the chromatin identified histone deacetylation (HDAC) machinery. TFAP2C KD reduced HDAC binding to chromatin and increased H3K27Ac marks at enhancer regions, suggesting that TFAP2C is involved in recruiting HDAC. Taken together, our findings provide important insights into regulation of enhancer marks by SUMOylation.

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