Arginine Methylation of Aubergine Mediates Tudor Binding and Germ Plasm Localization

RNA. 2010 Jan;16(1):70-8. doi: 10.1261/rna.1869710. Epub 2009 Nov 19.


Piwi proteins such as Drosophila Aubergine (Aub) and mouse Miwi are essential for germline development and for primordial germ cell (PGC) specification. They bind piRNAs and contain symmetrically dimethylated arginines (sDMAs), catalyzed by dPRMT5. PGC specification in Drosophila requires maternal inheritance of cytoplasmic factors, including Aub, dPRMT5, and Tudor (Tud), that are concentrated in the germ plasm at the posterior end of the oocyte. Here we show that Miwi binds to Tdrd6 and Aub binds to Tudor, in an sDMA-dependent manner, demonstrating that binding of sDMA-modified Piwi proteins with Tudor-domain proteins is an evolutionarily conserved interaction in germ cells. We report that in Drosophila tud(1) mutants, the piRNA pathway is intact and most transposons are not de-repressed. However, the localization of Aub in the germ plasm is severely reduced. These findings indicate that germ plasm assembly requires sDMA modification of Aub by dPRMT5, which, in turn, is required for binding to Tudor. Our study also suggests that the function of the piRNA pathway in PGC specification may be independent of its role in transposon control.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arginine / metabolism*
  • Cytoplasm / metabolism
  • Drosophila / metabolism
  • Drosophila Proteins / metabolism*
  • Female
  • Germ Cells / metabolism*
  • Male
  • Membrane Transport Proteins / metabolism*
  • Methylation
  • Mice
  • Models, Biological
  • Molecular Sequence Data
  • Peptide Initiation Factors / metabolism*
  • Protein Binding
  • Protein Methyltransferases / metabolism
  • Protein-Arginine N-Methyltransferases / metabolism*
  • Tissue Distribution


  • Drosophila Proteins
  • Membrane Transport Proteins
  • Peptide Initiation Factors
  • aub protein, Drosophila
  • tud protein, Drosophila
  • Arginine
  • Protein Methyltransferases
  • Protein-Arginine N-Methyltransferases
  • csul protein, Drosophila