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Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive

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Listed:
  • Ernesto Guccione

    (European Institute of Oncology (IEO), IFOM-IEO Campus)

  • Christian Bassi

    (European Institute of Oncology (IEO), IFOM-IEO Campus)

  • Fabio Casadio

    (European Institute of Oncology (IEO), IFOM-IEO Campus)

  • Francesca Martinato

    (European Institute of Oncology (IEO), IFOM-IEO Campus)

  • Matteo Cesaroni

    (European Institute of Oncology (IEO), IFOM-IEO Campus)

  • Henning Schuchlautz

    (Institute of Biochemistry, RWTH Aachen University Hospital)

  • Bernhard Lüscher

    (Institute of Biochemistry, RWTH Aachen University Hospital)

  • Bruno Amati

    (European Institute of Oncology (IEO), IFOM-IEO Campus)

Abstract

The arginine methyltransferase PRMT6 is shown to methylate histone H3 on Arg2 in mammalian cells, and this modification is mutually antagonistic with methylation of Lys4 on H3 by the methyl transferase complex MLL.

Suggested Citation

  • Ernesto Guccione & Christian Bassi & Fabio Casadio & Francesca Martinato & Matteo Cesaroni & Henning Schuchlautz & Bernhard Lüscher & Bruno Amati, 2007. "Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive," Nature, Nature, vol. 449(7164), pages 933-937, October.
    • Handle: RePEc:nat:nature:v:449:y:2007:i:7164:d:10.1038_nature06166
    DOI: 10.1038/nature06166
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    Cited by:

    1. Lihua Qiang & Yong Zhang & Zehui Lei & Zhe Lu & Shasha Tan & Pupu Ge & Qiyao Chai & Mengyuan Zhao & Xinwen Zhang & Bingxi Li & Yu Pang & Lingqiang Zhang & Cui Hua Liu & Jing Wang, 2023. "A mycobacterial effector promotes ferroptosis-dependent pathogenicity and dissemination," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    2. Ramachandran Prakasam & Angela Bonadiman & Roberta Andreotti & Emanuela Zuccaro & Davide Dalfovo & Caterina Marchioretti & Debasmita Tripathy & Gianluca Petris & Eric N. Anderson & Alice Migazzi & Lau, 2023. "LSD1/PRMT6-targeting gene therapy to attenuate androgen receptor toxic gain-of-function ameliorates spinobulbar muscular atrophy phenotypes in flies and mice," Nature Communications, Nature, vol. 14(1), pages 1-22, December.

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