Arginine methylation of vasa protein is conserved across phyla.
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.
Kirino
Yohei
Y
Department of Pathology and Laboratory Medicine, Division of Neuropathology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104, USA.
Vourekas
Anastassios
A
Kim
Namwoo
N
de Lima Alves
Flavia
F
Rappsilber
Juri
J
Klein
Peter S
PS
Jongens
Thomas A
TA
Mourelatos
Zissimos
Z
D000818:Animals; D000911:Antibodies, Monoclonal; D000918:Antibody Specificity; D001120:Arginine / Q000031:analogs & derivatives / Q000378:metabolism*; D060565:Argonaute Proteins; D018797:Cell Cycle Proteins; D053487:DEAD-box RNA Helicases / Q000235:genetics* / Q000276:immunology / Q000378:metabolism*; D029721:Drosophila Proteins / Q000235:genetics* / Q000276:immunology / Q000378:metabolism*; D004331:Drosophila melanogaster; D005260:Female; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D008297:Male; D008745:Methylation; D051379:Mice; D009866:Oogenesis / Q000502:physiology; D010802:Phylogeny; D011496:Protein Methyltransferases / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D011484:Protein-Arginine N-Methyltransferases; D011506:Proteins / Q000378:metabolism; D012261:Ribonucleoproteins / Q000378:metabolism; D017411:Ribonucleoproteins, Small Nuclear / Q000378:metabolism; D013091:Spermatogenesis / Q000502:physiology; D029867:Xenopus Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D014982:Xenopus laevis
D000911:Antibodies, Monoclonal; D060565:Argonaute Proteins; D018797:Cell Cycle Proteins; C086637:DDX4 protein, Xenopus; D029721:Drosophila Proteins; C448522:Piwil1 protein, mouse; C448521:Piwil2 protein, mouse; D011506:Proteins; D012261:Ribonucleoproteins; D017411:Ribonucleoproteins, Small Nuclear; C517521:TDRD6 protein, mouse; C488681:Tdrd1 protein, mouse; D029867:Xenopus Proteins; C018524:N,N-dimethylarginine; D001120:Arginine; D011496:Protein Methyltransferases; D011484:Protein-Arginine N-Methyltransferases; C512734:csul protein, Drosophila; C090864:Ddx4 protein, mouse; C088269:vas protein, Drosophila; D053487:DEAD-box RNA Helicases