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The  Drosophila argonaute2  ( ago2 ) gene plays a major role in siRNA mediated RNA silencing pathways. Unlike mammalian Argonaute proteins, the  Drosophila  protein has an unusual amino-terminal domain made up largely of multiple copies of glutamine-rich repeats (GRRs). We report here that the  ago2  locus produces an alternative transcript that encodes a putative short isoform without this amino-terminal domain. Several  ago2  mutations previously reported to be null alleles only abolish expression of the long, GRR-containing isoform. Analysis of  drop out  ( dop ) mutations had previously suggested that variations in GRR copy number result in defects in RNAi and embryonic development. However, we find that  dop  mutations genetically complement transcript-null alleles of  ago2  and that  ago2  alleles with variant GRR copy numbers support normal development. In addition, we show that the assembly of the central RNAi machinery, the RISC (RNA induced silencing complex), is unimpaired in embryos when GRR copy number is altered. In fact, we find that GRR copy number is highly variable in natural  D. melanogaster  populations as well as in laboratory strains. Finally, while many other insects share an extensive, glutamine-rich Ago2 amino-terminal domain, its primary sequence varies drastically between species. Our data indicate that GRR variation does not modulate an essential function of Ago2 and that the amino-terminal domain of Ago2 is subject to rapid evolution.

Natural Variation of the Amino-Terminal Glutamine-Rich Domain in Drosophila Argonaute2 Is Not Associated with Developmental Defects