PuSH - Publication Server of Helmholtz Zentrum München

Waldmann, T.* ; Izzo, A.* ; Kamieniarz, K.* ; Richter, F.M.* ; Vogler, C.* ; Sarg, B.* ; Lindner, H.* ; Young, N.L.* ; Mittler, G.* ; Garcia, B.A.* ; Schneider, R.*

Methylation of H2AR29 is a novel repressive PRMT6 target.

Epigenetics Chromatin 4:11 (2011)
DOI Order publishers version
Open Access Gold as soon as Publ. Version/Full Text is submitted to ZB.
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.
Altmetric
Additional Metrics?
Edit extra informations Login
Publication type Article: Journal article
Document type Scientific Article
e-ISSN 1756-8935
Quellenangaben Volume: 4, Issue: , Pages: , Article Number: 11 Supplement: ,
Publisher BioMed Central
Publishing Place London
Reviewing status Peer reviewed