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Translational Repression Of The Drosophila nanos mRNA Involves The RNA Helicase Belle And RNA Coating By Me31B And Trailer hitch

By Michael Götze, Jérémy Dufourt, Christian Ihling, Christiane Rammelt, Stéphanie Pierson, Nagraj Sambrani, Claudia Temme, Andrea Sinz, Martine Simonelig, Elmar Wahle

Posted 24 May 2017
bioRxiv DOI: 10.1101/141655 (published DOI: 10.1261/rna.062208.117)

Translational repression of maternal mRNAs is an essential regulatory mechanism during early embryonic development. Repression of the Drosophila nanos mRNA, required for the formation of the anterior-posterior body axis, depends on the protein Smaug binding to two Smaug recognition elements (SREs) in the nanos 3′ UTR. In a comprehensive mass spectrometric analysis of the SRE-dependent repressor complex, we identified Smaug, Cup, Me31B, Trailer hitch, eIF4E and PABPC, in agreement with earlier data. As a novel component, the RNA-dependent ATPase Belle (DDX3) was found, and its involvement in deadenylation and repression of nanos was confirmed in vivo. Smaug, Cup and Belle bound stoichiometrically to the SREs, independently of RNA length. Binding of Me31B and Tral was also SRE-dependent, but their amounts were proportional to the length of the RNA and equimolar to each other. We suggest that ‘coating’ of the RNA by a Me31B·Tral complex may be at the core of repression.

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