Arginine methyltransferase Capsuléen is essential for methylation of spliceosomal Sm proteins and germ cell formation in Drosophila
2007
Although arginine modification has been implicated in a number of cellular
processes, the in vivo requirement of protein arginine methyltransferases
(PRMTs) in specific biological processes remain to be clarified. In this study
we characterize the Drosophila PRMT Capsuleen, homologous to
human PRMT5. During Drosophila oogenesis, catalytic activity of
Capsuleen is necessary for both the assembly of the nuage surrounding
nurse cell nuclei and the formation of the pole plasm at the posterior end of
the oocyte. In particular, we show that the nuage and pole plasm localization
of Tudor, an essential component for germ cell formation, are abolished in
csul mutant germ cells. We identify the spliceosomal Sm proteins as
in vivo substrates of Capsuleen and demonstrate that Capsuleen,
together with its associated protein Valois, is essential for the synthesis of
symmetric di-methylated arginyl residues in Sm proteins. Finally, we show that
Tudor can be targeted to the nuage in the absence of Sm methylation by
Capsuleen, indicating that Tudor localization and Sm methylation are
separate processes. Our results thus reveal the role of a PRMT in protein
localization in germ cells.
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