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Nanos proteins repress the expression of target  mRNA s by recruiting effector complexes through non‐conserved N‐terminal regions. In vertebrates, Nanos proteins interact with the  NOT 1 subunit of the  CCR 4– NOT  effector complex through a  NOT 1 interacting motif ( NIM ), which is absent in Nanos orthologs from several invertebrate species. Therefore, it has remained unclear whether the Nanos repressive mechanism is conserved and whether it also involves direct interactions with the  CCR 4– NOT  deadenylase complex in invertebrates. Here, we identify an effector domain ( NED ) that is necessary for the  Drosophila melanogaster  ( Dm ) Nanos to repress  mRNA  targets. The  NED  recruits the  CCR 4– NOT  complex through multiple and redundant binding sites, including a central region that interacts with the  NOT  module, which comprises the C‐terminal domains of  NOT 1–3. The crystal structure of the  NED  central region bound to the  NOT  module reveals an unanticipated bipartite binding interface that contacts  NOT 1 and  NOT 3 and is distinct from the  NIM  of vertebrate Nanos. Thus, despite the absence of sequence conservation, the N‐terminal regions of Nanos proteins recruit  CCR 4– NOT  to assemble analogous repressive complexes.

Distinct modes of recruitment of the CCR 4– NOT complex by Drosophila and vertebrate Nanos