期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 55, 期 8, 页码 2903-2906出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201510996
关键词
bivalent domains; chromatin; epigenetics; expressed protein ligation; PRC2
资金
- Sandoz Family Foundation
- NCCR Chemical Biology
- Swiss National Science Foundation [31003A_149789]
- EPFL
- Swiss National Science Foundation (SNF) [31003A_149789] Funding Source: Swiss National Science Foundation (SNF)
Nucleosomes carry extensive post-translational modifications (PTMs), which results in complex modification patterns that are involved in epigenetic signaling. Although two copies of each histone coexist in a nucleosome, they may not carry the same PTMs and are often differently modified ( asymmetric). In bivalent domains, a chromatin signature prevalent in embryonic stem cells (ESCs), namely H3 methylated at lysine4 (H3K4me3), coexists with H3K27me3 in asymmetric nucleosomes. We report a general, modular, and traceless method for producing asymmetrically modified nucleosomes. We further show that in bivalent nucleosomes, H3K4me3 inhibits the activity of the H3K27-specific lysine methyltransferase (KMT) polycomb repressive complex 2 (PRC2) solely on the same histone tail, whereas H3K27me3 stimulates PRC2 activity across tails, thereby partially overriding the H3K4me3-mediated repressive effect. To maintain bivalent domains in ESCs, PRC2 activity must thus be locally restricted or reversed.
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