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MPP8 mediates the interactions between DNA methyltransferase Dnmt3a and H3K9 methyltransferase GLP/G9a

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  • Yanqi Chang

    (Emory University School of Medicine)

  • Lidong Sun

    (H. Lee Moffitt Cancer Center and Research Institute)

  • Kenji Kokura

    (H. Lee Moffitt Cancer Center and Research Institute)

  • John R. Horton

    (Emory University School of Medicine)

  • Mikiko Fukuda

    (Experimental Research Center for Infectious Diseases, Institute for Virus Research, Kyoto University, 53 Shogoin, Kawara-cho, Sakyo-ku)

  • Alexsandra Espejo

    (M.D. Anderson Cancer Center, University of Texas, 1808 Park Road 1C, Smithville, Texas 78957, USA.)

  • Victoria Izumi

    (H. Lee Moffitt Cancer Center and Research Institute)

  • John M. Koomen

    (H. Lee Moffitt Cancer Center and Research Institute)

  • Mark T. Bedford

    (M.D. Anderson Cancer Center, University of Texas, 1808 Park Road 1C, Smithville, Texas 78957, USA.)

  • Xing Zhang

    (Emory University School of Medicine)

  • Yoichi Shinkai

    (Experimental Research Center for Infectious Diseases, Institute for Virus Research, Kyoto University, 53 Shogoin, Kawara-cho, Sakyo-ku)

  • Jia Fang

    (H. Lee Moffitt Cancer Center and Research Institute)

  • Xiaodong Cheng

    (Emory University School of Medicine)

Abstract

DNA CpG methylation and histone H3 lysine 9 (H3K9) methylation are two major repressive epigenetic modifications, and these methylations are positively correlated with one another in chromatin. Here we show that G9a or G9a-like protein (GLP) dimethylate the amino-terminal lysine 44 (K44) of mouse Dnmt3a (equivalent to K47 of human DNMT3A) in vitro and in cells overexpressing G9a or GLP. The chromodomain of MPP8 recognizes the dimethylated Dnmt3aK44me2. MPP8 also interacts with self-methylated GLP in a methylation-dependent manner. The MPP8 chromodomain forms a dimer in solution and in crystals, suggesting that a dimeric MPP8 molecule could bridge the methylated Dnmt3a and GLP, resulting in a silencing complex of Dnmt3a–MPP8–GLP/G9a on chromatin templates. Together, these findings provide a molecular explanation, at least in part, for the co-occurrence of DNA methylation and H3K9 methylation in chromatin.

Suggested Citation

  • Yanqi Chang & Lidong Sun & Kenji Kokura & John R. Horton & Mikiko Fukuda & Alexsandra Espejo & Victoria Izumi & John M. Koomen & Mark T. Bedford & Xing Zhang & Yoichi Shinkai & Jia Fang & Xiaodong Che, 2011. "MPP8 mediates the interactions between DNA methyltransferase Dnmt3a and H3K9 methyltransferase GLP/G9a," Nature Communications, Nature, vol. 2(1), pages 1-10, September.
    • Handle: RePEc:nat:natcom:v:2:y:2011:i:1:d:10.1038_ncomms1549
    DOI: 10.1038/ncomms1549
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    Cited by:

    1. Kosuke Yamaguchi & Xiaoying Chen & Brianna Rodgers & Fumihito Miura & Pavel Bashtrykov & Frédéric Bonhomme & Catalina Salinas-Luypaert & Deis Haxholli & Nicole Gutekunst & Bihter Özdemir Aygenli & Lau, 2024. "Non-canonical functions of UHRF1 maintain DNA methylation homeostasis in cancer cells," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    2. A. Emilia Arguello & Ang Li & Xuemeng Sun & Tanner W. Eggert & Elisabeth Mairhofer & Ralph E. Kleiner, 2022. "Reactivity-dependent profiling of RNA 5-methylcytidine dioxygenases," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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