Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/34747
Title: The symmetric dimethylation of histone H3 arginine 2: A novel histone mark involved in Euchromatin maintenance
Authors: MIGLIORI VALENTINA
Keywords: histone, arginine methylation, epigenetics, chromatin, WDR5
Issue Date: 11-Apr-2012
Source: MIGLIORI VALENTINA (2012-04-11). The symmetric dimethylation of histone H3 arginine 2: A novel histone mark involved in Euchromatin maintenance. ScholarBank@NUS Repository.
Abstract: The Asymmetric dimethylation of histone H3 Arginine 2 acts as a repressive mark that antagonizes trimethylation of H3 lysine 4. In this study, I report that H3R2 is also symmetrically dimethylated (H3R2me2s) by PRMT5 and PRMT7 and present in euchromatic regions. Profiling of H3-tail interactors by SILAC-Mass Spectrometry revealed that H3R2me2s excludes binding of RBBP7, a central component of co-repressor complexes Sin3a, NURD and PRC2. Conversely H3R2me2s enhances binding of WDR5, a common component of the MLL/Set1a/b, the NLS1 and the ATAC co-activator complexes. The interaction with WDR5 distinguishes H3R2me2s from H3R2me2a, which impedes its recruitment to chromatin. The crystallographic structure of WDR5 and the H3R2me2s peptide in a stable complex elucidates the molecular determinants of this high affinity interaction (collaboration with Marina Mapelli IFOM IEO Milan). My findings provide insight of H3R2me2s as a novel mark that keeps genes poised in euchromatin for transcriptional activation upon cell cycle withdrawal and differentiation.
URI: http://scholarbank.nus.edu.sg/handle/10635/34747
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