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DREAM represses distinct targets by cooperating with different THAP domain proteins

ABSTRACT: DREAM represses distinct targets by cooperating with different THAP domain proteins

PROVIDER: PRJNA648943 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR12331800.fastq.gz	Fastqsanger.gz
	SRR12331801.fastq.gz	Fastqsanger.gz
	SRR12331802.fastq.gz	Fastqsanger.gz
	SRR12331803.fastq.gz	Fastqsanger.gz
	SRR12331804.fastq.gz	Fastqsanger.gz

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DREAM represses distinct targets by cooperating with different THAP domain proteins [RNA-seq]

Project description:The DREAM (DP, Retinoblastoma [Rb]-like, E2F, and MuvB) complex controls cellular quiescence by repressing cell cycle and other genes, but its mechanism of action is unclear. Here we demonstrate that two C. elegans THAP domain proteins, LIN-15B and LIN-36, co-localize with DREAM and function by different mechanisms for repression of distinct sets of targets. LIN-36 represses classical cell cycle targets by promoting DREAM binding and gene body enrichment of H2A.Z. Furthermore, the function of DREAM subunit EFL-1/E2F is specific for LIN-36 targets. In contrast, LIN-15B represses a subset of germline targets by facilitating H3K9me2 promoter marking. In humans, THAP proteins have been implicated in cell cycle regulation by poorly understood mechanisms. We propose that THAP domain proteins are key mediators of Rb/DREAM function, facilitating repression of distinct sets of targets.

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DREAM represses distinct targets by cooperating with different THAP domain proteins [CHIP-seq]

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DREAM represses distinct targets by cooperating with different THAP domain proteins [CHIP-seq]

Project description:DREAM represses distinct targets by cooperating with different THAP domain proteins [CHIP-seq]

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DREAM represses distinct targets by cooperating with different THAP domain proteins [RNA-seq]

Project description:DREAM represses distinct targets by cooperating with different THAP domain proteins [RNA-seq]

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DREAM represses distinct targets by cooperating with different THAP domain proteins

Project description:Summary The DREAM (dimerization partner [DP], retinoblastoma [Rb]-like, E2F, and MuvB) complex controls cellular quiescence by repressing cell-cycle and other genes, but its mechanism of action is unclear. Here, we demonstrate that two C. elegans THAP domain proteins, LIN-15B and LIN-36, co-localize with DREAM and function by different mechanisms for repression of distinct sets of targets. LIN-36 represses classical cell-cycle targets by promoting DREAM binding and gene body enrichment of H2A.Z, and we find that DREAM subunit EFL-1/E2F is specific for LIN-36 targets. In contrast, LIN-15B represses germline-specific targets in the soma by facilitating H3K9me2 promoter marking. We further find that LIN-36 and LIN-15B differently regulate DREAM binding. In humans, THAP proteins have been implicated in cell-cycle regulation by poorly understood mechanisms. We propose that THAP domain proteins are key mediators of Rb/DREAM function. Graphical abstract Highlights • THAP domain proteins LIN-36 and LIN-15B cooperate with the Rb-DREAM complex• LIN-36 and LIN-15B repress distinct sets of DREAM targets via different mechanisms• With LIN-36, DREAM represses cell-cycle genes through gene body enrichment of H2A.Z• With LIN-15B, DREAM represses germline genes through H3K9me2 promoter marking Gal et al. show that two THAP domain proteins are key mediators of retinoblastoma-DREAM function in C. elegans, repressing distinct targets by different mechanisms. With LIN-36, DREAM represses cell-cycle genes through gene body enrichment of H2A.Z; with LIN-15B, DREAM represses germline-specific genes in the soma through H3K9me2 promoter marking.

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DREAM represses distinct targets by cooperating with different THAP domain proteins

Project description:This SuperSeries is composed of the SubSeries listed below.

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The DREAM complex antagonizes WDR5a and represses the productive elongation of transcription in Arabidopsis [RNA-seq]

Project description:The master transcriptional repressor DREAM (dimerization partner, RB-like, E2F and multi-vulval class B) complex regulates cell cycle in eukaryotes, but much remains unknown about how it transmits repressive signals on chromatin to the primary transcriptional machinery (e.g., Pol II). Through a genetic screen, we identified BTE1 (barrier of transcription elongation 1), a key component in the plant DREAM complex. The subsequent characterization demonstrated that the DREAM complex represses Pol II elongation. The core DREAM subunits E2F transcription factors recruit BTE1 to accumulate at the promoter-proximal regions of target genes. DREAM target genes exhibit characteristic enrichment of H2A.Z and H3K4me2 modification on chromatin. The DREAM complex BTE1 subunit interacts with WDR5a, repressing WDR5a chromatin binding and the productive elongation of transcription on BTE1-targeted genomic loci. Thus, we demonstrate a major role of DREAM complex in the control of transition from transcription initiation to productive elongation around TSSs on the open chromatin via inhibiting WDR5a function.

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The DREAM complex antagonizes WDR5a and represses the productive elongation of transcription in Arabidopsis [ChIP-seq]

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The DREAM complex antagonizes WDR5a and represses the productive elongation of transcription in Arabidopsis [GRO-seq]

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Chromatin-seq and RNA-seq of dREAM subunit deficient Drosophila S2R+ cells

Project description:dREAM is a multi-functional complex which activates and represses genes involved in the G2/M transition and is involved in maintaining chromatin boundaries through interactions with CTCF and BEAF-32, however the mechanisms by which it carries out gene and chromatin regulation is yet to be uncovered. Applying a novel Mnase-seq technique, RNAi and RNA-seq we report links between transcriptional changes in S2R+ cells deficient for dREAM subunits and changes in chromatin structure. The most distinct chromatin phenotype of these cells are at CTCF binding sites, several of which are located between divergent gene pairs which show impaired regulation in cells deficient for a dREAM component.

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