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Inseparable RNA binding and chromatin modification activities of a nucleosome-interacting surface in EZH2

ABSTRACT: Inseparable RNA binding and chromatin modification activities of a nucleosome-interacting surface in EZH2

PROVIDER: PRJNA820710 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR18503700_1.fastq.gz	Fastqsanger.gz
	SRR18503700_2.fastq.gz	Fastqsanger.gz
	SRR18503701_1.fastq.gz	Fastqsanger.gz
	SRR18503701_2.fastq.gz	Fastqsanger.gz
	SRR18503702_1.fastq.gz	Fastqsanger.gz

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Inseparable RNA binding and chromatin modification activities of a nucleosome-interacting surface in EZH2

Project description:Inseparable RNA binding and chromatin modification activities of a nucleosome-interacting surface in EZH2

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Inseparable RNA binding and chromatin modification activities of a nucleosome-interacting surface in EZH2 [ChIP-seq]

Project description:Inseparable RNA binding and chromatin modification activities of a nucleosome-interacting surface in EZH2 [ChIP-seq]

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Inseparable RNA binding and chromatin modification activities of a nucleosome-interacting surface in EZH2

Project description:Polycomb repressive complex 2 (PRC2) interacts with RNAs in cells, but there is no consensus on how RNA regulates its canonical functions, including chromatin modification and the maintenance of transcription programs in lineage-committed cells. We assayed two separation-of-function mutants of the catalytic subunit EZH2, defective in RNA binding but active in methyltransferase. We find that part of the RNA-binding surface of EZH2 is required for chromatin modification, yet this activity is independent of RNA. Mechanistically, the RNA-binding surface within EZH2 is required for chromatin modification in vitro and in cells, through interactions with nucleosomal DNA. Contrarily, an RNA-binding defective mutant exhibited normal chromatin modification activity in vitro and in lineage-committed cells, accompanied by normal gene repression activity. Collectively, we show that part of the RNA-binding surface of PRC2, rather than the RNA-binding activity per se, is required for the histone methylation of chromatin in vitro and in cells.

2023-12-11 | GSE199543 | GEO

Inseparable RNA binding and chromatin modification activities of a nucleosome-interacting surface in EZH2 [ChIP-seq]

2023-12-11 | GSE239445 | GEO

Inseparable RNA binding and chromatin modification activities of a nucleosome-interacting surface in EZH2

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

2023-12-11 | GSE239447 | GEO

iCLIP analysis of EZH2-interacting RNAs

Project description:RNAs directly interacting with EZH2 were isolated from human colorectal HCT116 cells using an in vivo crosslinking and immunoprecipitation strategy (iCLIP, König J et al, Nat Struct Mol Biol 2010) coupled to an ultrasequencing approach. RIP sequencing for 1 Human sample

2012-04-23 | E-GEOD-36070 | biostudies-arrayexpress

iCLIP analysis of EZH2-interacting RNAs

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RIP-seq of lncRNAs interacting with EZH2 in INA-6 multiple myeloma cells

Project description:To investigate lncRNAs interacting with the EZH2 enzyme, the catalytic subcomponent of the polycomb repressive complex 2. We performed nuclear extraction of the INA-6 MM cell line and proceeded do an immunoprecipitation against the EZH2 protein.

2023-09-30 | E-MTAB-13135 | biostudies-arrayexpress

Comprehensive nucleosome interactome screen establishes fundamental principles of nucleosome binding

Project description:Nuclear proteins bind chromatin to execute and regulate genome-templated processes. While structural and biochemical studies of individual nucleosome interactions have suggested that an acidic patch on the nucleosome disk surface may be a common site for recruitment to chromatin, the pervasiveness of acidic patch binding and whether other nucleosome surface binding hot-spots exist remains unclear. Here, we use nucleosome affinity proteomics with a library of nucleosomes that collectively disrupts all exposed histone surfaces to establish the universal principles of nucleosome binding. We find that the acidic patch and two adjacent surfaces are the primary hot-spots for nucleosome disk binding and are critical for the majority of nucleosome-protein interactions. In contrast, nearly half of the nucleosome disk surface participates only minimally in protein binding. In addition to establishing the fundamental principles of chromatin binding, our screen defines nucleosome surface requirements of nearly 300 nucleosome interacting proteins implicated in diverse nuclear processes including transcription, DNA damage repair, cell cycle regulation, and nuclear architecture. Building from our screen, we demonstrate that the Anaphase-Promoting Complex/Cyclosome directly binds the acidic patch and elucidate a redundant charge-based mechanism of acidic patch binding by nuclear pore protein ELYS. Overall, our interactome screen illuminates a highly competitive nucleosome binding hub for chromatin-targeted activities and curates a list of nucleosome interacting proteins that will enable mechanistic exploration of many unexpected chromatin-templated nuclear processes.

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Affinify Purification of EZH2 and phosphodeficient EZH2 identifies phosphorylation dependent interactions of EZH2

Project description:Overexpression of EZH2 in estrogen receptor negative (ER-) breast cancer promotes metastasis. EZH2 has been mainly studied as the catalytic component of the Polycomb Repressive Complex 2 (PRC2) that mediates gene repression by trimethylating histone H3 at lysine 27 (H3K27me3). However, how EZH2 drives metastasis despite the low H3K27me3 levels observed in ER- breast cancer is unknown. We have shown that in human invasive carcinomas and distant metastases, cytoplasmic EZH2 phosphorylated at T367 is significantly associated with ER- disease and low H3K27me3 levels. Here, we explore the interactome of EZH2 and of a phosphodeficient mutant EZH2_T367A. We identified novel interactors of EZH2, and identified interactions that are dependent on the phosphorylation and cellular localization of EZH2 that may play a role in EZH2 dependent metastatic progression.

2018-07-03 | PXD010073 | Pride

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