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Recognition of ubiquitinated histone H2A constitutes a treatment target for RSF1-driven ovarian cancer

ABSTRACT: Recognition of ubiquitinated histone H2A constitutes a treatment target for RSF1-driven ovarian cancer

PROVIDER: PRJNA1182350 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR31232100_1.fastq.gz	Fastqsanger.gz
	SRR31232100_2.fastq.gz	Fastqsanger.gz
	SRR31232101_1.fastq.gz	Fastqsanger.gz
	SRR31232101_2.fastq.gz	Fastqsanger.gz
	SRR31232102_1.fastq.gz	Fastqsanger.gz

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Similar Datasets

Recognition of ubiquitinated histone H2A constitutes a treatment target for RSF1-driven ovarian cancer

Project description:RNA-seq results revealed that overexpression of RSF1, but not RSF1ΔUAB, induced a gene expression program enriched for cancer stem cell markers. Conversely, overexpression of a UAB domain decoy peptide reduced cell proliferation and blocked the cancer stem cell gene expression programs in OVCAR3 cells. Together, these studies reveal the critical role of recognizing H2Aub in RSF1-driven ovarian cancer and demonstrate that the interaction between RSF1 and H2Aub constitutes a druggable target for treating ovarian cancers with high levels of RSF1.

2025-03-01 | GSE281128 | GEO

Ubiquitinated histone H2A mapping in Drosophila ML-DmBG3 cells

Project description:Monoubiquitinated histone H2A produced by the Sce/Ring subunit of the Polycomb Repressive Complex 1 (PRC1) was mapped genome-wide in Drosophila ML-DmBG3 cells using chromatin immunoprecipitation followed by hybridization to Affymetrix tiling arrays. ML-DmBG3 chromatin immunoprecipitated with anti-histone H2AK119ub antibody and matching input chromatin were amplified, labeled and hybridized to Affymetrix tiling arrays to determine the locations of ubiquitinated H2A genome-wide.

2013-08-09 | E-GEOD-49634 | biostudies-arrayexpress

Ubiquitinated histone H2A mapping in Drosophila ML-DmBG3 cells

2013-08-09 | GSE49634 | GEO

TRIM37 is a novel H2A ubiquitin ligase and a Breast Cancer Oncogene

Project description:The TRIM37 gene is mutatedin Mulbery nanism, a rare autosomal recessive disorder, and is in the 17q23 chromosomal region that is amplified in up to ~40% of breast cancers. Trim37 contains a RING finger domain, a hallmark of E3 ubiquitin ligases, but the protein substrate(s) of Trim37 is unknown. Mono-ubiquitination of histone H2A is a chromatin modification associated with transcriptional repression and here we report that Trim37 is an H2A ubiquitin ligase. Genome-wide Chip-CHIP experiments indicate that in human breast cancer cells containing amplified 17q23, Trim37 is bound to the promoters of many tumor suppressor genes. RNA interference (RNAi)-mediated knockdown of Trim37 results in loss of ubiquitinated H2A, dissociation of PRC1 and PRC2, and transcriptional reactivation of silenced genes. Knockdown of Trim37 in human breast cancer cells containing amplified 17q23 substantially decreases tumor growth in mouse xenografts. Collectively, our results reveal Trim37 as a new H2A ubiquitin ligase that is overexpressed in a subset of breast cancers and redirects PRC2 to silence tumor suppressors and other genes resulting in oncogenesis. Identification of TRIM37 Binding targets in MCF7 cells from the two replicate experiments

2014-10-06 | E-GEOD-48196 | biostudies-arrayexpress

Recognition of inherently unstable H2A-nucleosome by Swc2 is a major determinant for unidirectional H2A.Z exchange

Project description:The site-specific chromatin incorporation of eukaryotic histone variant H2A.Z is driven by the multi-component chromatin remodeling complex SWR1/SRCAP/ p400. The budding yeast SWR1 complex replaces the H2A-H2B dimer in the canonical nucleosome with the H2A.Z-H2B dimer, but the mechanism governing the directionality of H2A-to-H2A.Z exchange remains elusive. Here, we use single-molecule force spectroscopy to dissect the disassembly/ reassembly of H2A-nucleosome and H2A.Z-nucleosome. We find that the N-terminal 1-135 residues of yeast SWR1-complex-protein-2 (previously termed Swc2-Z) facilitate the disassembly of nucleosomes containing H2A but not H2A.Z. The Swc2-mediated nucleosome disassembly/reassembly requires the inherently unstable H2A-nucleosome, whose instability is conferred by three H2A α2-helix residues Gly47, Pro49 and Ile63 as they selectively weaken the structural rigidity of H2A-H2B dimer. It also requires Swc2-ZN (residues 1-37) that directly anchors to H2A-nucleosome and functions in the SWR1-catalyzed H2A.Z replacement in vitro and yeast H2A.Z deposition in vivo. Our findings providecrucial insights into how SWR1 complex discriminates between the H2A-nucleosome and H2A.Z-nucleosome, establishing a simple paradigm for the governace of unidirectional H2A.Z exchange.

2021-04-12 | GSE171844 | GEO

A Cryptic Basic Groove formed by Ubiquitin and Histone H3 Mediates the Selective Recognition of H2AK119Ub Nucleosomes by Synovial Sarcoma X Breakpoint 1 Protein

Project description:The cancer-specific fusion oncoprotein SS18-SSX1 disturbs chromatin accessibility by hijacking the chromatin-remodeling BAF complex from the promoters or enhancers to the H2AK119Ub-marked polycomb-repressed chromatin regions. Relocation of the BAF complex was achieved through selective recognition of the H2AK119Ub nucleosomes by the synovial sarcoma X breakpoint 1 protein SSX1, which neither has a ubiquitin (Ub)-binding domain nor binds to free Ub. To elucidate the mechanism by which SSX1 selectively recognizes H2AK119Ub nucleosomes, here we report the cryo-EM structure of SSX1 bound to H2AK119Ub nucleosomes at a resolution of 3.1 Å. The structure reveals that the SSX1 N-terminal basic region (residues W164, R167, L168, R169) is anchored to the H2A/H2B acidic patch, while the aromatic amino acid (residue Y177) in the middle of SSX1 interacts with the hydrophobic pocket formed by the H2A α2 and α3 helixes. Ub recognition by SSX1 is unique and depends on a cryptic basic groove formed by H3 (residues R49, R52, K56) and the Ub motif (residues R42, R72, R74) on the H2AK119 site. Our results describe a novel mode of site-specific ubiquitinated nucleosome recognition that underlies the specific hijacking of the BAF complex to polycomb regions by SS18-SSX1 in synovial sarcoma.

2023-09-04 | GSE236811 | GEO

TRIM37 is a novel H2A ubiquitin ligase and a Breast Cancer Oncogene

2014-10-06 | GSE48196 | GEO

Recognition of inherently unstable H2A-nucleosome by Swc2 is a major determinant for unidirectional H2A.Z exchange

Project description:Recognition of inherently unstable H2A-nucleosome by Swc2 is a major determinant for unidirectional H2A.Z exchange

| PRJNA721183 | ENA

ChlP-seq of MYC in HTA10-Myc/h2a and h2a

Project description:ChlP-seq of MYC in HTA10-Myc/h2a and h2a

2025-04-11 | GSE283930 | GEO

H2A ubiquitination is essential for Polycomb Repressive Complex 1-mediated gene regulation in Marchantia polymorpha

Project description:Polycomb repressive complex 1 (PRC1) and PRC2 are chromatin regulators maintaining transcriptional repression by depositing H2A mono-ubiquitination (H2Aub) or H3 lysine 27 tri-methylation (H3K27me3), respectively. While PRC1 is known to be required for transcriptional repression, the contribution of H2Aub in the Polycomb repressive system remains unclear in plants. Here, we directly test the requirement of H2Aub for gene repression in Marchantia polymorpha by generating point mutants in H2A that fail to be ubiquitinated by PRC1. These mutants show reduced H3K27me3 levels on the same target sites as mutants in PRC1 subunits MpBMI1 and the homolog MpBMI1L, revealing that PRC1-catalyzed H2Aub is essential for Polycomb system function. Furthermore, we demonstrate that H2Aub contributes to the PRC1-mediated silencing of genes and transposable elements. Together, our data provide evidence that H2Aub plays indispensable roles in the PRC1-initiated repressive system in Marchantia.

2021-08-13 | GSE164394 | GEO

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