Arginine methylation at histone H3R2 controls deposition of H3K4 trimethylation

Antonis Kirmizis, Helena Santos-Rosa, Christopher J. Penkett, Michael A. Singer, Michiel Vermeulen, Matthias Mann, Jürg Bähler, Roland D. Green and Tony Kouzarides ()
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Antonis Kirmizis: Tennis Court Road, Cambridge CB2 1QN, UK
Helena Santos-Rosa: Tennis Court Road, Cambridge CB2 1QN, UK
Christopher J. Penkett: Wellcome Trust Sanger Institute, Hinxton, Cambridge CB10 1HH, UK
Michael A. Singer: NimbleGen Systems, Inc., 1 Science Court, Madison, Wisconsin 53711, USA
Michiel Vermeulen: Max Planck Institute for Biochemistry
Matthias Mann: Max Planck Institute for Biochemistry
Jürg Bähler: Wellcome Trust Sanger Institute, Hinxton, Cambridge CB10 1HH, UK
Roland D. Green: NimbleGen Systems, Inc., 1 Science Court, Madison, Wisconsin 53711, USA
Tony Kouzarides: Tennis Court Road, Cambridge CB2 1QN, UK

Nature, 2007, vol. 449, issue 7164, 928-932

Abstract: Methylation of histone H3 on residue Lys4 (H3K4) contributes to transcription activation. Now it is shown that in budding yeast, an adjacent modification, methylated Arg2, can inhibit H3K4 methylation by preventing the binding of a methyl transferase complex.

Date: 2007
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DOI: 10.1038/nature06160

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