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Readers of histone methylarginine marks.

Authors: Gayatri, S  Bedford, MT 
Citation: Gayatri S and Bedford MT, Biochim Biophys Acta. 2014 Aug;1839(8):702-710. doi: 10.1016/j.bbagrm.2014.02.015. Epub 2014 Feb 28.
Pubmed: (View Article at PubMed) PMID:24583552
DOI: Full-text: DOI:10.1016/j.bbagrm.2014.02.015

Arginine methylation is a common posttranslational modification (PTM) that alters roughly 0.5% of all arginine residues in the cells. There are three types of arginine methylation: monomethylarginine (MMA), asymmetric dimethylarginine (ADMA), and symmetric dimethylarginine (SDMA). These three PTMs are enriched on RNA-binding proteins and on histones, and also impact signal transduction cascades. To date, over thirty arginine methylation sites have been cataloged on the different core histones. These modifications alter protein structure, impact interactions with DNA, and also generate docking sites for effector molecules. The primary "readers" of methylarginine marks are Tudor domain-containing proteins. The complete family of thirty-six Tudor domain-containing proteins has yet to be fully characterized, but at least ten bind methyllysine motifs and eight bind methylarginine motifs. In this review, we will highlight the biological roles of the Tudor domains that interact with arginine methylated motifs, and also address other types of interactions that are regulated by these particular PTMs. This article is part of a Special Issue entitled: Molecular mechanisms of histone modification function.


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CRRD Object Information
CRRD ID: 9479047
Created: 2014-08-26
Species: All species
Last Modified: 2014-08-26
Status: ACTIVE


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