Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Cryo-EM structures of PRC2 simultaneously engaged with two functionally distinct nucleosomes.
Journal, issue, pages	Nat Struct Mol Biol, Vol. 25, Issue 2, Page 154-162, Year 2018
Publish date	Jan 29, 2018
Authors	Simon Poepsel / Vignesh Kasinath / Eva Nogales /
PubMed Abstract	Epigenetic regulation is mediated by protein complexes that couple recognition of chromatin marks to activity or recruitment of chromatin-modifying enzymes. Polycomb repressive complex 2 (PRC2), a ...Epigenetic regulation is mediated by protein complexes that couple recognition of chromatin marks to activity or recruitment of chromatin-modifying enzymes. Polycomb repressive complex 2 (PRC2), a gene silencer that methylates lysine 27 of histone H3, is stimulated upon recognition of its own catalytic product and has been shown to be more active on dinucleosomes than H3 tails or single nucleosomes. These properties probably facilitate local H3K27me2/3 spreading, causing heterochromatin formation and gene repression. Here, cryo-EM reconstructions of human PRC2 bound to bifunctional dinucleosomes show how a single PRC2, via interactions with nucleosomal DNA, positions the H3 tails of the activating and substrate nucleosome to interact with the EED subunit and the SET domain of EZH2, respectively. We show how the geometry of the PRC2-DNA interactions allows PRC2 to accommodate varying lengths of the linker DNA between nucleosomes. Our structures illustrate how an epigenetic regulator engages with a complex chromatin substrate.
External links	Nat Struct Mol Biol / PubMed:29379173 / PubMed Central
Methods	EM (single particle)
Resolution	4.6 - 13.3 Å
Structure data	EMDB-7306: Structure of PRC2 bound to a H3K27me3/WT hetero-dinucleosome substrate with a 35 bp DNA linker Method: EM (single particle) / Resolution: 6.2 Å EMDB-7307: Structure of PRC2 bound to a H3K27me3/WT hetero-dinucleosome substrate with a 30 bp DNA linker Method: EM (single particle) / Resolution: 8.4 Å EMDB-7308: Structure of PRC2 bound to a H3K27me3/WT hetero-dinucleosome substrate with a 40 bp DNA linker Method: EM (single particle) / Resolution: 13.3 Å EMDB-7309: Structure of human PRC2 bound to a hetero-dinucleosome substrate with 35 bp linker DNA. 3D classification of signal subtracted particles lacking the unmodified substrate nucleosome. Example Class1. Method: EM (single particle) / Resolution: 7.4 Å EMDB-7310: Structure of human PRC2 bound to a hetero-dinucleosome substrate with 35 bp linker DNA. 3D classification of signal subtracted particles lacking the unmodified substrate nucleosome. Example Class3. Method: EM (single particle) / Resolution: 10.1 Å EMDB-7311: Structure of PRC2 bound to a H3K27me3/WT hetero-dinucleosome substrate with a 35 bp DNA linker. Masked refinement of PRC2-substrate nucleosome subcomplex. Method: EM (single particle) / Resolution: 4.9 Å EMDB-7312: Structure of human PRC2 bound to a hetero-dinucleosome substrate with 35 bp linker DNA. Refinement after signal subtraction of the modified nucleosome ton improve resolution of the substrate nucleosome - PRC2 interface. Method: EM (single particle) / Resolution: 7.7 Å EMDB-7313: Structure of human PRC2-AEBP2 Method: EM (single particle) / Resolution: 4.6 Å
Source	Homo sapiens (human)