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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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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.

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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.

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