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The DnaQ-H family exonuclease Snipper (Snp) is a 33-kDa  Drosophila melanogaster  homolog of 3′hExo and ERI-1, exoribonucleases implicated in the degradation of histone mRNA in mammals and in the negative regulation of RNA interference (RNAi) in  Caenorhabditis elegans , respectively. In metazoans, Snp, Exod1, 3′hExo, ERI-1, and the prpip nucleases define a new subclass of structure-specific 3′-5′ exonucleases that bind and degrade double-stranded RNA and/or DNA substrates with 3′ overhangs of 2–5 nucleotides (nt) in the presence of Mg 2+  with no apparent sequence specificity. These nucleases are also capable of degrading linear substrates. Snp efficiently degrades structured RNA and DNA substrates as long as there exists a minimum 3′ overhang of 2 nt to initiate degradation. We identified a  Snp  mutant and used it to test whether Snp plays a role in regulating histone mRNA degradation or RNAi in vivo.  Snp  mutant flies are viable, and display no obvious developmental abnormalities. The expression pattern and level of histone H3 mRNA in  Snp  mutant embryos and third instar imaginal eye discs was indistinguishable from wild type, suggesting that Snp does not play a significant role in the turnover of histone mRNA at the end of the S phase. The loss of  Snp  was also unable to enhance the silencing capability of two different RNAi transgenes targeting the  white  and  yellow  genes, suggesting that Snp does not negatively modulate RNAi. Therefore, Snp is a nonessential exonuclease that is not a functional ortholog of either 3′hExo or ERI-1.

Genetic and biochemical characterization ofDrosophilaSnipper: A promiscuous member of the metazoan 3′hExo/ERI-1 family of 3′ to 5′ exonucleases