Methylarginine recognition by tudor domains

Research output: Chapter in Book/Report/Conference proceedingChapter

2 Scopus citations

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 languageEnglish (US)
Title of host publicationHistone Recognition
PublisherSpringer International Publishing
Pages125-148
Number of pages24
ISBN (Electronic)9783319181028
ISBN (Print)9783319181011
DOIs
StatePublished - Jan 1 2015

ASJC Scopus subject areas

  • General Medicine
  • General Biochemistry, Genetics and Molecular Biology

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