Unknown

Dataset Information

0

Architecture of PRC2 Holo Complexes.

ABSTRACT: Polycomb repressive complex 2 (PRC2) is a chief epigenetic regulator. In a new article, Chen et al. describe the crystal structure of the heterotetrameric PRC2 holo complex, which provides important mechanistic insights into the organization of its subunits and the association of PRC2 with chromatin.

SUBMITTER: Vann KR 

PROVIDER: S-EPMC6014913 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Architecture of PRC2 Holo Complexes.

Vann Kendra R KR   Kutateladze Tatiana G TG  

Trends in biochemical sciences 20180503 7

Polycomb repressive complex 2 (PRC2) is a chief epigenetic regulator. In a new article, Chen et al. describe the crystal structure of the heterotetrameric PRC2 holo complex, which provides important mechanistic insights into the organization of its subunits and the association of PRC2 with chromatin. ...[more]

Similar Datasets

Unknown Cooperative DNA looping by PRC2 complexes.
| S-EPMC8216278 | biostudies-literature
Unknown Arabidopsis MSI1 connects LHP1 to PRC2 complexes.
| S-EPMC3715863 | biostudies-literature
Unknown Modeling holo-ACP:DH and holo-ACP:KR complexes of modular polyketide synthases: a docking and molecular dynamics study.
| S-EPMC3422181 | biostudies-literature
Unknown FIE, a nuclear PRC2 protein, forms cytoplasmic complexes in Arabidopsis thaliana.
| S-EPMC5100023 | biostudies-literature
Unknown Holo-Seq: single-cell sequencing of holo-transcriptome.
| S-EPMC6193298 | biostudies-literature
Unknown Chromatin regulated interchange between polycomb repressive complex 2 (PRC2)-Ezh2 and PRC2-Ezh1 complexes controls myogenin activation in skeletal muscle cells.
| S-EPMC3180244 | biostudies-literature
Unknown Molecular architecture of polycomb repressive complexes.
| S-EPMC5310723 | biostudies-literature
Unknown Three classes of response elements for human PRC2 and MLL1/2-Trithorax complexes.
| S-EPMC6158500 | biostudies-literature
Unknown Structures of Escherichia coli tryptophanase in holo and 'semi-holo' forms.
| S-EPMC4356303 | biostudies-literature
Unknown Characterization of the mycobacterial acyl-CoA carboxylase holo complexes reveals their functional expansion into amino acid catabolism.
| S-EPMC4347857 | biostudies-literature