The maternal mRNA nanos is required for anterior-posterior patterning in the early Drosophila melanogaster development. The nanos-mRNA is translationally repressed and deadenylated during the first two hours of embryogenesis. A stem-loop structure in the 3'-UTR of this RNA (SRE - Smaug recogniiton element) is bound by the Smaug protein which recruits a protein complex to the RNA to sequester its translation and intiate transcript degradation via the ccr4/not-complex. To analyse the composition of this repressor complex, biotinylated RNAs carrying two SRE stem-loops were used for an affinity purification of bound proteins. As a negative control an RNA was used that contained two point mutations in the SRE loop, that abolish binding of Smaug. Seven subunits were identified as components of the repressor complex. The main deadenylase in Drosophila, the ccr4/not-complex was also significantly enriched.