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Distribution of H3K27me3, H3K27ac, and H3K4me1 in E(z) temperature sensitive cells

ABSTRACT: PcG protein complex PRC2 is a methyltransferase specific for histone H3 lysine27, and H3K27me3 is essential for stable transcription silencing. Here we have determined genomic distributions of H3K27me3, H3K27ac, and H3K4me1 in cultured Drosophila E(z) temperature sensitive cells at 25°C and 31°C where E(z) is largely inactivated by hybridization of ChIP products with tiling microarrays.

ORGANISM(S): Drosophila melanogaster

PROVIDER: GSE61262 | GEO | 2015/05/14

SECONDARY ACCESSION(S): PRJNA260619

REPOSITORIES: GEO

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Distribution of H3K27me3, H3K27ac, and H3K4me1 in E(z) temperature sensitive cells

Project description:PcG protein complex PRC2 is a methyltransferase specific for histone H3 lysine27, and H3K27me3 is essential for stable transcription silencing. Here we have determined genomic distributions of H3K27me3, H3K27ac, and H3K4me1 in cultured Drosophila E(z) temperature sensitive cells at 25°C and 31°C where E(z) is largely inactivated by hybridization of ChIP products with tiling microarrays. Genomic distributions of H3K27me3, H3K27ac, and H3K4me1 in cultured Drosophila E(z) temperature sensitive cells (EZ2-2) at 25°C and 31°C where E(z) is largely inactivated by hybridization of ChIP products with tiling microarrays

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Project description:PcG protein complex PRC2 is a methyltransferase specific for histone H3 lysine27, and H3K27me3 is essential for stable transcription silencing. Less well known but quantitatively much more important is the genome-wide role of PRC2 that dimethylates ~70% of total H3K27. Here we show that H3K27me2 occurs in inverse proportion to transcriptional activity in genes and intergenic regions and its loss results in global transcriptional derepression proportionally greatest in previously silent or weakly transcribed regions. H3K27me2 levels are controlled by opposing roaming activities of PRC2 and the H3K27 demethylase dUTX. Unexpectedly, we find an equally pervasive distribution of histone H2A ubiquitylated at lysine 118 (H2AK118ub), attributed to the RING1 subunit of PRC1-type complexes. Examination of global changes in five epigenetic marks when E(z) is inactivated in E(z) temperature-sensitive cells at 25°C and 31°C. Genome-wide binding of Polycomb was also examined to classify canonical PcG target regions.

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Project description:Polycomb group (PcG) proteins maintain the silenced state of key developmental genes in animals, but how these proteins are recruited to specific regions of the genome is still poorly understood. In Drosophila, PcG proteins are recruited to Polycomb response elements (PREs) that include combinations of sites for sequence specific DNA binding “PcG recruiters,” including Pho, Cg, and Spps. To understand their roles in PcG recruitment, we compared Pho-, Cg-, and Spps-binding sites against H3K27me3 and key PcG proteins by ChIP-seq in wild-type and mutant third instar larvae. H3K27me3 in canonical Polycomb domains is decreased after the reduction of any recruiter. Reduction of Spps and Pho, but not Cg, causes the redistribution of H3K27me3 to heterochromatin. Regions with dramatically depleted H3K27me3 after Spps knockout are usually accompanied by decreased Pho binding, suggesting their cooperative binding. PcG recruiters, the PRC2 component E(z), and the PRC1 components Psc and Ph cobind thousands of active genes outside of H3K27me3 domains. This study demonstrates the importance of distinct PcG recruiters for the establishment of unique Polycomb domains. Different PcG recruiters can act both cooperatively and independently at specific PcG target genes, highlighting the complexity and diversity of PcG recruitment mechanisms.

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