Arginine Methylation of Vasa Protein Is Conserved across Phyla |
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| Authors: | Yohei Kirino Anastassios Vourekas Namwoo Kim Flavia de Lima Alves Juri Rappsilber Peter S Klein Thomas A Jongens and Zissimos Mourelatos |
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| Institution: | From the Departments of ‡Pathology and Laboratory Medicine, Division of Neuropathology, ;**Genetics, ;¶Medicine, and ;‖Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104 and ;the §Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh EH8 9YL, Scotland, United Kingdom |
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| Abstract: | 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. |
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| Keywords: | Drosophila MicroRNA Protein Methylation RNA-Binding Protein Spermatogenesis Piwi Tudor Protein Vasa Helicase Drosophila Oogenesis PiRNA |
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