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TitleStructures of monomeric and dimeric PRC2:EZH1 reveal flexible modules involved in chromatin compaction.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 714, Year 2021
Publish dateJan 29, 2021
AuthorsDaniel Grau / Yixiao Zhang / Chul-Hwan Lee / Marco Valencia-Sánchez / Jenny Zhang / Miao Wang / Marlene Holder / Vladimir Svetlov / Dongyan Tan / Evgeny Nudler / Danny Reinberg / Thomas Walz / Karim-Jean Armache /
PubMed AbstractPolycomb repressive complex 2 (PRC2) is a histone methyltransferase critical for maintaining gene silencing during eukaryotic development. In mammals, PRC2 activity is regulated in part by the ...Polycomb repressive complex 2 (PRC2) is a histone methyltransferase critical for maintaining gene silencing during eukaryotic development. In mammals, PRC2 activity is regulated in part by the selective incorporation of one of two paralogs of the catalytic subunit, EZH1 or EZH2. Each of these enzymes has specialized biological functions that may be partially explained by differences in the multivalent interactions they mediate with chromatin. Here, we present two cryo-EM structures of PRC2:EZH1, one as a monomer and a second one as a dimer bound to a nucleosome. When bound to nucleosome substrate, the PRC2:EZH1 dimer undergoes a dramatic conformational change. We demonstrate that mutation of a divergent EZH1/2 loop abrogates the nucleosome-binding and methyltransferase activities of PRC2:EZH1. Finally, we show that PRC2:EZH1 dimers are more effective than monomers at promoting chromatin compaction, and the divergent EZH1/2 loop is essential for this function, thereby tying together the methyltransferase, nucleosome-binding, and chromatin-compaction activities of PRC2:EZH1. We speculate that the conformational flexibility and the ability to dimerize enable PRC2 to act on the varied chromatin substrates it encounters in the cell.
External linksNat Commun / PubMed:33514705 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 4.8 Å
Structure data

23021

7kso

EMDB-23021, PDB-7kso:
Cryo-EM structure of PRC2:EZH1-AEBP2-JARID2
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-23022:
Cryo-EM map of PRC2:EZH1-AEBP2
Method: EM (single particle) / Resolution: 4.1 Å

23024

7ksr

EMDB-23024, PDB-7ksr:
PRC2:EZH1_A from a dimeric PRC2 bound to a nucleosome
Method: EM (single particle) / Resolution: 4.1 Å

23025

7ktp

EMDB-23025, PDB-7ktp:
PRC2:EZH1_B from a dimeric PRC2 bound to a nucleosome
Method: EM (single particle) / Resolution: 4.8 Å

23026

7ktq

EMDB-23026, PDB-7ktq:
Nucleosome from a dimeric PRC2 bound to a nucleosome
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-23103:
PRC2:EZH1 dimer bound to a nucleosome (composite map)
Method: EM (single particle) / Resolution: 4.8 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
  • xenopus laevis (African clawed frog)
KeywordsGENE REGULATION/Transferase / Chromatin / methyltransferase / nucleosome-modifying complex / GENE REGULATION / GENE REGULATION-Transferase complex / GENE REGULATION/DNA / GENE REGULATION-DNA complex

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