期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 282, 期 7, 页码 4408-4416出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M606773200
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资金
- Biotechnology and Biological Sciences Research Council [G20017] Funding Source: researchfish
- Medical Research Council [G0300332] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [G20017] Funding Source: Medline
- Medical Research Council [G0300332] Funding Source: Medline
- MRC [G0300332] Funding Source: UKRI
Histones are subject to a wide variety of post-translational modifications that play a central role in gene activation and silencing. We have used histone modification-specific antibodies to demonstrate that two histone modifications involved in gene activation, histone H3 acetylation and H3 lysine 4 methylation, are functionally linked. This interaction, in which the extent of histone H3 acetylation determines both the abundance and the degree of H3K4 methylation, plays a major role in the epigenetic response to histone deacetylase inhibitors. A combination of in vivo knockdown experiments and in vitro methyltransferase assays shows that the abundance of H3K4 methylation is regulated by the activities of two opposing enzyme activities, the methyltransferase MLL4, which is stimulated by acetylated substrates, and a novel and as yet unidentified H3K4me3 demethylase.
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