title: Methylation of H2AR29 is a novel repressive PRMT6 target.
abstract: BACKGROUND
  Covalent histone modifications are central to all DNA-dependent processes. Modifications of histones H3 and H4 are becoming well characterised, but knowledge of how H2A modifications regulate chromatin dynamics and gene expression is still very limited.
  
  
  RESULTS
  To understand the function of H2A modifications, we performed a systematic analysis of the histone H2A methylation status. We identified and functionally characterised two new methylation sites in H2A: R11 (H2AR11) and R29 (H2AR29). Using an unbiased biochemical approach in combination with candidate assays we showed that protein arginine methyltransferase (PRMT) 1 and PRMT6 are unique in their ability to catalyse these modifications. Importantly we found that H2AR29me2 is specifically enriched at genes repressed by PRMT6, implicating H2AR29me2 in transcriptional repression.
  
  
  CONCLUSIONS
  Our data establishes R11 and R29 as new arginine methylation sites in H2A. We identified the specific modifying enzymes involved, and uncovered a novel functional role of H2AR29me2 in gene silencing in vivo. Thus this work reveals novel insights into the function of H2A methylation and in the mechanisms of PRMT6-mediated transcriptional repression.
authors.affiliation: MPI for Immunobiology and Epigenetics, Stübeweg 51, 79108 Freiburg, Germany.|University of Konstanz, Doerenkamp-Zbinden chair, Universitätsstr. 10, 78457 Konstanz, Germany.
authors.forename: Tanja
authors.initials: T
authors.lastname: Waldmann
authors.affiliation: MPI for Immunobiology and Epigenetics, Stübeweg 51, 79108 Freiburg, Germany.
authors.forename: Annalisa
authors.initials: A
authors.lastname: Izzo
authors.affiliation: MPI for Immunobiology and Epigenetics, Stübeweg 51, 79108 Freiburg, Germany.
authors.forename: Kinga
authors.initials: K
authors.lastname: Kamieniarz
authors.affiliation: MPI for Immunobiology and Epigenetics, Stübeweg 51, 79108 Freiburg, Germany.
authors.forename: Florian
authors.initials: F
authors.lastname: Richter
authors.affiliation: MPI for Immunobiology and Epigenetics, Stübeweg 51, 79108 Freiburg, Germany.
authors.forename: Christine
authors.initials: C
authors.lastname: Vogler
authors.affiliation: Innsbruck Medical University, Division of Clinical Biochemistry, Biocenter, Fritz-Pregl-Str. 3, 6020 Innsbruck, Austria.
authors.forename: Bettina
authors.initials: B
authors.lastname: Sarg
authors.affiliation: Innsbruck Medical University, Division of Clinical Biochemistry, Biocenter, Fritz-Pregl-Str. 3, 6020 Innsbruck, Austria.
authors.forename: Herbert
authors.initials: H
authors.lastname: Lindner
authors.affiliation: Princeton University, Department of Molecular Biology, 415 Shultz Laboratory, Princeton, NJ 08540, USA.
authors.forename: Nicolas L
authors.initials: NL
authors.lastname: Young
authors.affiliation: MPI for Immunobiology and Epigenetics, Stübeweg 51, 79108 Freiburg, Germany.
authors.forename: Gerhard
authors.initials: G
authors.lastname: Mittler
authors.affiliation: Princeton University, Department of Molecular Biology, 415 Shultz Laboratory, Princeton, NJ 08540, USA.
authors.forename: Benjamin A
authors.initials: BA
authors.lastname: Garcia
authors.affiliation: MPI for Immunobiology and Epigenetics, Stübeweg 51, 79108 Freiburg, Germany.
authors.forename: Robert
authors.initials: R
authors.lastname: Schneider