Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Nature genetics - 1 Jun 2024

Gail Emma H, Healy Evan, Flanigan Sarena F, Jones Natasha, Ng Xiao Han, Uckelmann Michael, Levina Vitalina, Zhang Qi, Davidovich Chen

Abstract excerpt

Polycomb repressive complex 2 (PRC2) interacts with RNA in cells, but there is no consensus on how RNA regulates PRC2 canonical functions, including chromatin modification and the maintenance of transcription programs in lineage-committed cells. We assayed two separation-of-function mutants of the PRC2 catalytic subunit EZH2, defective in RNA binding but functional in methyltransferase activity. We find that part...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Chromatin
Share to Enhancer of Zeste Homolog 2 Protein

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Histones

Share to Methylation

Share to Nucleosomes

Share to Polycomb Repressive Complex 2

Share to Protein Binding

Source

Open in PubMed Open full text

Identifiers

PMID: 38744974
DOI: 10.1038/s41588-024-01740-8
PMCID: PMC11176075

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Inseparable RNA binding and chromatin modification activities of a nucleosome-interacting surface in EZH2.PMID 38744974Read ↗

Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms.Semantic proximity Read ↗

Structure of the catalytic domain of EZH2 reveals conformational plasticity in cofactor and substrate binding sites and explains oncogenic mutations.Semantic proximity Read ↗

Chromatin interaction analyses elucidate the roles of PRC2-bound silencers in mouse development.Semantic proximity Read ↗

EZH2-associated tumor malignancy: A prominent target for cancer treatment.Semantic proximity Read ↗

Jarid2 Methylation via the PRC2 Complex Regulates H3K27me3 Deposition during Cell Differentiation.Semantic proximity Read ↗

Structural context of disease-associated mutations and putative mechanism of autoinhibition revealed by X-ray crystallographic analysis of the EZH2-SET domain.Semantic proximity Read ↗

Targeting EZH2 in cancer.Semantic proximity Read ↗

Epigenetic regulation of signaling pathways in cancer: role of the histone methyltransferase EZH2.Semantic proximity Read ↗

Multifaceted role of the polycomb-group gene EZH2 in hematological malignancies.Semantic proximity Read ↗

Structural assembly of Polycomb group protein and Insight of EZH2 in cancer progression: A review.Semantic proximity Read ↗

SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex.Semantic proximity Read ↗

Convergent evolution between PALI1 and JARID2 for the allosteric activation of PRC2Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.