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Decoupling of H2Aub and H3K27me3 in early mammalian development

ABSTRACT: Decoupling of H2Aub and H3K27me3 in early mammalian development

PROVIDER: PRJNA715631 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR14004279_1.fastq.gz	Fastqsanger.gz
	SRR14004279_2.fastq.gz	Fastqsanger.gz
	SRR14004280_1.fastq.gz	Fastqsanger.gz
	SRR14004280_2.fastq.gz	Fastqsanger.gz
	SRR14004281_1.fastq.gz	Fastqsanger.gz

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Decoupling of H2Aub and H3K27me3 in early mammalian development

Project description:Polycomb group (PcG) proteins play critical roles during development. H2Aub and H3K27me3 are deposited by Polycomb-repressive Complex 1 and 2 (PRC1/2) respectively, and largely overlap in the genome due to mutual recruitment of the two complexes. However, whether PRC1/H2Aub and PRC2/H3K27me3 also function independently remains elusive. Here we uncovered a large-scale decoupling of H2Aub and H3K27me3 in preimplantation mouse embryos, at both canonical PcG targets and broad distal domains. H2Aub represses future bivalent genes without H3K27me3 but does not contribute to maintenance of H3K27me3-dependent non-canonical imprinting. Our study thus revealed their distinct and independent functions in early mammalian development.

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Project description:Trimethylation of histone H3 lysine 27 (H3K27me3) is important for gene silencing, (epi)genome organization and organismal development. In a prevalent model, the functional “readout” of H3K27me3 in mammalian cells is achieved through the H3K27me3-recognizing chromodomain harbored within the chromobox (CBX) component of canonical Polycomb repressive complex 1 (cPRC1), which induces chromatin compaction and gene repression. Here, we report that binding of H3K27me3 by a Bromo Adjacent Homology (BAH) domain harbored within BAH domain-containing protein 1 (BAHD1) is required for overall BAHD1 targeting to chromatin and for optimal repression of the H3K27me3-demarcated genes in mammalian cells. Disruption of direct interaction between BAHD1-BAH and H3K27me3 by point mutagenesis leads to chromatin remodeling, notably, increased histone acetylation, at its Polycomb gene targets. Mice carrying an H3K27me3-interaction-defective mutation of Bahd1BAH causes marked embryonic lethality, showing a requirement of this pathway for normal development. Altogether, this work demonstrates an H3K27me3-initiated signaling cascade that operates through a conserved BAH “reader” module within BAHD1 in mammals.

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