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Chromatin spreading in 3D through Insulator looping regulates genes through to H3K27me3 micro-domains

ABSTRACT: Chromatin spreading in 3D through Insulator looping regulates genes through to H3K27me3 micro-domains

PROVIDER: PRJNA534289 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR8946071.fastq.gz	Fastqsanger.gz
	SRR8946072.fastq.gz	Fastqsanger.gz
	SRR8946073.fastq.gz	Fastqsanger.gz
	SRR8946074.fastq.gz	Fastqsanger.gz
	SRR8946075.fastq.gz	Fastqsanger.gz

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Chromatin spreading in 3D through Insulator looping regulates genes through to H3K27me3 micro-domains

Project description:We used the technology of ChIP-sequencing to analyze changes in H3K27me3 levels in Drosophila Schneider S2 depleted of endogenous Beaf32 and expressing insulator mutants ('mut-Beaf32' or 'muBeaf') as compared to control cells expressing wild-type Beaf32 (Control; 'CTL')

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Insulator-based loops mediate the spreading of H3K27me3 over distant micro-domains repressing euchromatin genes.

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NURF301 contributes to gypsy chromatin insulator-mediated nuclear organization

Project description:Chromatin insulators are DNA-protein complexes that can prevent the spread of repressive chromatin and block communication between enhancers and promoters to regulate gene expression. In Drosophila, the gypsy chromatin insulator complex consists of three core proteins: CP190, Su(Hw), and Mod(mdg4)67.2. These factors concentrate at nuclear foci termed insulator bodies, and their normal localization is correlated with proper insulator function. Here, we identified NURF301/E(bx), a nucleosome remodeling factor, as a novel regulator of gypsy insulator body localization through a high-throughput RNAi imaging screen. NURF301 promotes gypsy-dependent insulator barrier activity and physically interacts with gypsy insulator proteins. Using ChIP-seq, we found that NURF301 co-localizes with insulator proteins genome-wide, and NURF301 promotes chromatin association of Su(Hw) and CP190 at gypsy insulator binding sites. These effects correlate with NURF301-dependent nucleosome repositioning. At the same time, CP190 and Su(Hw) are also required for recruitment of NURF301 to chromatin. Finally, Oligopaint FISH combined with immunofluorescence revealed that NURF301 promotes 3D contact between insulator bodies and gypsy binding site DNA, and NURF301 is required for proper nuclear positioning of gypsy binding sites. Our data provide new insights into how a nucleosome remodeling factor and insulator proteins cooperatively contribute to nuclear organization.

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Genome-wide binding of two new insulator-like proteins Pita and ZIPIC

Project description:Insulators are multiprotein–DNA complexes that regulate nuclear architecture. The Drosophila CP190 protein is a common cofactor of two main insulator complexes formed by the DNA-binding proteins Su(Hw) and dCTCF. Here, we have identified two new DNA-binding proteins, Pita and ZIPIC, that interact with CP190. In vitro, CP190 interacts with Pita through the BTB domain and with ZIPIC through the centrosomal targeting domain. The artificial binding sites for Pita or ZIPIC partially block enhancers and protect gene expression from PRE-mediated silencing in transgenic lines. Pita binds adjacent to dCTCF in the well-studied Mcp insulator and is required for its activity, which indicates that two insulator proteins can cooperate in organizing a functional insulator. Pita and ZIPIC preferentially bind to the promoter regions and extensively colocalize with dCTCF and BEAF. These results suggest that insulator proteins can fulfill multiple functions in chromosome architecture and gene expression.

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Nucleation and spreading rejuvenate polycomb domains every cell cycle

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