Abstract
The posttranslational modification (PTM) of protein motifs provides docking sites for a number of different protein domains. This facilitates signal transduction from the cell surface, through the cytoplasm and into the nucleus. Arginine methylation is just one of these PTMs, and it has been implicated in a number of cellular processes, including RNA processing, DNA repair, protein translation, and the regulation of gene expression. It is an abundant PTM that is enriched on RNA-binding proteins and on histones. To date, over twenty arginine m'ethylation sites have been cataloged on the different core histones. The only family of protein domains that is known to bind methylarginine motifs is the Tudor family. Tudor domains can be divided into methyllysine- and methylarginine- binding subtypes, with close to ten Tudor domain-containing proteins in each subtype. In this chapter, we will highlight the biological roles of the Tudor domains that interact with arginine-methylated peptide motifs.
Original language | English (US) |
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Title of host publication | Histone Recognition |
Publisher | Springer International Publishing |
Pages | 125-148 |
Number of pages | 24 |
ISBN (Electronic) | 9783319181028 |
ISBN (Print) | 9783319181011 |
DOIs | |
State | Published - Jan 1 2015 |
ASJC Scopus subject areas
- General Medicine
- General Biochemistry, Genetics and Molecular Biology