Journal
SCIENCE
Volume 359, Issue 6378, Pages 940-944Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aar5700
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Funding
- Eli Lilly through the Lilly Research Award Program
- Helen Hay Whitney Foundation
- Alexander von Humboldt Foundation (Germany)
- European Molecular Biology Organization
- European Union [HEALTH-F4-2008-201648]
- European Research Council (ERC) [233226, 670821]
- Innovative Medicines Initiative Joint Undertaking (ULTRA-DD) [115766]
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Transcriptionally repressive histone H3 lysine 27 methylation by Polycomb repressive complex 2 (PRC2) is essential for cellular differentiation and development. Here we report cryo-electron microscopy structures of human PRC2 in a basal state and two distinct active states while in complex with its cofactors JARID2 and AEBP2. Both cofactors mimic the binding of histone H3 tails. JARID2, methylated by PRC2, mimics a methylated H3 tail to stimulate PRC2 activity, whereas AEBP2 interacts with the RBAP48 subunit, mimicking an unmodified H3 tail. SUZ12 interacts with all other subunits within the assembly and thus contributes to the stability of the complex. Our analysis defines the complete architecture of a functionally relevant PRC2 and provides a structural framework to understand its regulation by cofactors, histone tails, and RNA.
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