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Methylation of H2AR29 is a novel repressive PRMT6 target

MPS-Authors
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Waldmann,  Tanja
Spemann Laboratory, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Izzo,  Annalisa
Spemann Laboratory, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Kamieniarz,  Kinga
Spemann Laboratory, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

Richter,  Florian
Max Planck Society;

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Vogler,  Christine
Spemann Laboratory, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Mittler,  Gerhard
Department of Cellular and Molecular Immunology, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Schneider,  Robert
Spemann Laboratory, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Citation

Waldmann, T., Izzo, A., Kamieniarz, K., Richter, F., Vogler, C., Sarg, B., et al. (2011). Methylation of H2AR29 is a novel repressive PRMT6 target. Epigenetics & Chromatin, 4, 1-10.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-8E33-4
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.