Chapter 8 - Tudor Domains as Methyl-Lysine and Methyl-Arginine Readers

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Abstract

The Tudor domain is a methyl-lysine and methyl-arginine binding domain present in proteins involved in cellular functions as diverse as DNA transcription, RNA metabolism, gene silencing, the transmission of epigenetic posttranslational modifications, and the maintenance of genomic stability. In this chapter, we review the different forms—single Tudor, tandem Tudor, hybrid Tudor, extended Tudor—and substrate binding modes, including methylation-state specificity, of the Tudor domain. Our focus is on proteins for which three-dimensional structures of Tudor domains in complex with lysine- or arginine-methylated substrates are available. The functional significance of Tudor proteins in chromatin signaling and possible involvement in diseases are highlighted.

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    The Tudor domain was first identified in the Tud protein from Drosophila, which is necessary for germ cell formation (Liu et al., 2010a; Ponting, 1997). Subsequently, a number of Tudor domains such as well-known double Tudor domains in JMJD2A which are involved in the regulation of gene transcription (Botuyan and Mer, 2016), and a Tudor domain in human SND1 which was shown to bind PIWIL1 in an methyl-arginine dependent manner in regulating piRNA pathway (Liu et al., 2010b), were discovered in various proteins. As another member of the Royal family, Chromo domain was also identified in a variety of proteins, including HP1 (heterochromatin-associated protein 1), CHD1, CHD7, etc.

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