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

Ernesto Guccione, Christian Bassi, Fabio Casadio, Francesca Martinato, Matteo Cesaroni, Henning Schuchlautz, Bernhard Lüscher and Bruno Amati ()
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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

Nature, 2007, vol. 449, issue 7164, 933-937

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.

Date: 2007
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DOI: 10.1038/nature06166

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