Abstract
Polycomb repressive complexes 1 and 2 (PRC1 and 2) play a critical role in the epigenetic regulation of transcription during cellular differentiation, stem cell pluripotency and neoplastic progression. Here we show that the polycomb group protein EED, a core component of PRC2, physically interacts with and functions as part of PRC1. Components of PRC1 and PRC2 compete for EED binding. EED functions to recruit PRC1 to H3K27me3 loci and enhances PRC1-mediated H2A ubiquitin E3 ligase activity. Taken together, we suggest an integral role for EED as an epigenetic exchange factor coordinating the activities of PRC1 and 2.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Animals
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Antibodies / pharmacology
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Cell Line, Tumor
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Enhancer of Zeste Homolog 2 Protein
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Gene Knockdown Techniques
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Genetic Loci
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Histone Methyltransferases
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Histone-Lysine N-Methyltransferase / metabolism
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Histones / metabolism
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Humans
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Male
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Mice, SCID
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Models, Biological
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Polycomb Repressive Complex 1 / metabolism
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Polycomb Repressive Complex 2 / metabolism*
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Polycomb-Group Proteins / metabolism*
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Protein Binding / drug effects
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Ubiquitin-Protein Ligases / metabolism
Substances
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Antibodies
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EED protein, human
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Eed protein, mouse
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Histones
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Polycomb-Group Proteins
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Histone Methyltransferases
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EZH2 protein, human
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Enhancer of Zeste Homolog 2 Protein
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Histone-Lysine N-Methyltransferase
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Polycomb Repressive Complex 2
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Polycomb Repressive Complex 1
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RNF2 protein, human
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Ubiquitin-Protein Ligases