De novo methylation of histone H3K23 by the methyltransferases EHMT1/GLP and EHMT2/G9a

被引:0
作者
David A. Vinson
Kimberly E. Stephens
Robert N. O’Meally
Shri Bhat
Blair C. R. Dancy
Robert N. Cole
Srinivasan Yegnasubramanian
Sean D. Taverna
机构
[1] Johns Hopkins University School of Medicine,Department of Pharmacology and Molecular Sciences
[2] Johns Hopkins University School of Medicine,Center for Epigenetics
[3] University of Arkansas for Medical Sciences,Department of Pediatrics, Division of Infectious Diseases
[4] Arkansas Children’s Research Institute,Department of Biological Chemistry
[5] Johns Hopkins University School of Medicine,undefined
[6] Sidney Kimmel Comprehensive Cancer Center,undefined
[7] Johns Hopkins University School of Medicine,undefined
[8] Walter Reed Army Institute of Research,undefined
来源
Epigenetics & Chromatin | / 15卷
关键词
Histone; H3K23 methylation; H3K18 methylation; G9a; EHMT2; GLP; EHMT1; Epigenetics;
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摘要
Epigenetic modifications to histone proteins serve an important role in regulating permissive and repressive chromatin states, but despite the identification of many histone PTMs and their perceived role, the epigenetic writers responsible for generating these chromatin signatures are not fully characterized. Here, we report that the canonical histone H3K9 methyltransferases EHMT1/GLP and EHMT2/G9a are capable of catalyzing methylation of histone H3 lysine 23 (H3K23). Our data show that while both enzymes can mono- and di-methylate H3K23, only EHMT1/GLP can tri-methylate H3K23. We also show that pharmacologic inhibition or genetic ablation of EHMT1/GLP and/or EHMT2/G9a leads to decreased H3K23 methylation in mammalian cells. Taken together, this work identifies H3K23 as a new direct methylation target of EHMT1/GLP and EHMT2/G9a, and highlights the differential activity of these enzymes on H3K23 as a substrate.
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