The Polycomb repression complex 2 (PRC2) plays an essential role in vertebrate development and is responsible for the di- and trimethylation of lysine 27 of Histone H3 (H3K27me2/3). The H3K27me3 modification is associated with chromatin compaction and is involved in the transcriptional gene repression. Several genes encoding PRC2 components are mutated in multiple types of cancers, highlighting the importance of this complex for proper gene regulation and cellular differentiation. Initial structural studies by electron microscopy and X-ray crystallography have shed light on the architecture of the entire human PRC2-AEBP2 complex and the atomic details of some of its core components. A recent high-resolution structure of an active fungal PRC2 subcomplex has provided important mechanistic and functional insights into PRC2 activity and regulation. In this chapter, we present these findings and review, from a structural perspective, the current understanding of PRC2 methyltransferase activity and regulation.
CITATION STYLE
Huang, C. S., Nogales, E., & Ciferri, C. (2017). Molecular Architecture of the Polycomb Repressive Complex 2. In Polycomb Group Proteins (pp. 165–189). Elsevier Inc. https://doi.org/10.1016/B978-0-12-809737-3.00008-8
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