Methylarginine, specifically asymmetric dimethylarginine (ADMA) and symmetric dimethylarginine (SDMA), are epigenetic modifications that play roles in chromatin regulation and gene expression. These methylarginine marks are predominantly found on arginine residues within histone proteins and are recognized by specialized chromatin binding proteins. Histones, the proteins which package DNA into nucleosomes, can be modified by methylation on arginine residues. This modification is catalysed by a family of enzymes termed protein arginine methyltransferases (PRMTs). PRMTs can add mono- and dimethylarginine marks on histones, leading to the creation of asymmetric dimethylarginine (ADMA) and symmetric dimethylarginine (SDMA) residues. PRMT5 is a well-known PRMT enzyme responsible for catalysing the symmetric dimethylation of arginine residues on histones. The SDMA mark is recognized by various chromatin binding proteins, including SMN (Survival of Motor Neuron) complex, WDR77, and MEP50, which play essential roles in RNA splicing regulation and processing, highlighting a connection between methylarginine marks and RNA metabolism. Coactivator-associated arginine methyltransferase 1 (CARM1), also known as PRMT4, catalyses the asymmetric dimethylation of arginine residues on histones. CARM1-mediated ADMA marks can be recognized by chromatin binding proteins such as p300 and CBP, which possess specialized domains called bromodomains. The interaction between these proteins and ADMA marks are important for transcriptional activation and gene regulation. CARM1 is known to be involved as a coactivator for nuclear hormone receptors such as estrogen receptor alpha (ERα). CARM1 is involved in epigenetic regulation by methylating histone proteins and non-histone proteins. It specifically methylates arginine residues on histones H3 and H4, leading to changes in chromatin structure and gene expression. Such marks are thought to facilitate the recruitment of p300/CBP, leading to chromatin remodelling and transcriptional activation of estrogen-responsive genes. PRMT5, which catalyses SDMA marks, is often associated with transcriptional repression. It contributes to the formation of repressive chromatin structures by interacting with various chromatin binding proteins. For example, PRMT5 interacts with the SIN3A/HDAC complex to silence gene expression by promoting histone deacetylation. Dysregulation of CARM1 has been linked to cancer. In breast cancer for example, CARM1 promotes estrogen-dependent cell growth by methylating histone H3, resulting in the upregulation of estrogen-responsive genes. CARM1 also plays a more direct role in hormone receptor signalling pathways, in hormone-driven cancers like breast and prostate cancer. It can methylate nuclear hormone receptors such as estrogen receptor alpha (ERα) and androgen receptor (AR), increasing their transcriptional activity, and can methylate the p300 and CBP coactivators, influencing their roles in transcriptional regulation. PRMT5 and its associated proteins, such as SMN, are implicated in neurodegenerative diseases like spinal muscular atrophy (SMA). These proteins are crucial for RNA processing and splicing, highlighting the importance of methylarginine marks in neuronal function. Thus, methylarginine modifications on histones, specifically ADMA and SDMA, are important epigenetic marks that play significant roles in chromatin regulation and gene expression. These marks are recognized by specific chromatin binding proteins, and their interactions contribute to transcriptional activation or repression. Explore our full methyl arginine product range below and discover more, for less.