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J Biol Chem 2010 Mar 12;28511:8148-54. doi: 10.1074/jbc.M109.089821.
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Arginine methylation of vasa protein is conserved across phyla.

Kirino Y , Vourekas A , Kim N , de Lima Alves F , Rappsilber J , Klein PS , Jongens TA , Mourelatos Z .

Recent studies have uncovered an unexpected relationship between factors that are essential for germline development in Drosophila melanogaster: the arginine protein methyltransferase 5 (dPRMT5/Csul/Dart5) and its cofactor Valois, methylate the Piwi family protein Aub, enabling it to bind Tudor. The RNA helicase Vasa is another essential protein in germline development. Here, we report that mouse (mouse Vasa homolog), Xenopus laevis, and D. melanogaster Vasa proteins contain both symmetrical and asymmetrical dimethylarginines. We find that dPRMT5 is required for the production of sDMAs of Vasa in vivo. Furthermore, we find that the mouse Vasa homolog associates with Tudor domain-containing proteins, Tdrd1 and Tdrd6, as well as the Piwi proteins, Mili and Miwi. Arginine methylation is thus emerging as a conserved and pivotal post-translational modification of proteins that is essential for germline development.

PubMed ID: 20080973
PMC ID: PMC2832966
Article link: J Biol Chem
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: ddx4 piwil1 piwil2 tdrd1 tdrd6 wdr77

References [+] :
Anne, Valois, a component of the nuage and pole plasm, is involved in assembly of these structures, and binds to Tudor and the methyltransferase Capsuléen. 2005, Pubmed