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De novo methylation of histone H3K23 by the methyltransferases EHMT1/GLP and EHMT2/G9a.
Vinson, David A; Stephens, Kimberly E; O'Meally, Robert N; Bhat, Shri; Dancy, Blair C R; Cole, Robert N; Yegnasubramanian, Srinivasan; Taverna, Sean D.
Affiliation
  • Vinson DA; Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
  • Stephens KE; Center for Epigenetics, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
  • O'Meally RN; Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
  • Bhat S; Center for Epigenetics, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
  • Dancy BCR; Department of Pediatrics, Division of Infectious Diseases, University of Arkansas for Medical Sciences, Arkansas Children's Research Institute, Little Rock, AR, 72202, USA.
  • Cole RN; Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
  • Yegnasubramanian S; Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
  • Taverna SD; Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
Epigenetics Chromatin ; 15(1): 36, 2022 11 21.
Article in En | MEDLINE | ID: mdl-36411491
ABSTRACT
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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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Histones / Histone-Lysine N-Methyltransferase Limits: Animals Language: En Journal: Epigenetics Chromatin Year: 2022 Document type: Article Affiliation country: United States
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Histones / Histone-Lysine N-Methyltransferase Limits: Animals Language: En Journal: Epigenetics Chromatin Year: 2022 Document type: Article Affiliation country: United States