biostudies-literature00450Gotze MFondation ARC pour la Recherche sur le CancerFondation ARCDeutsche ForschungsgemeinschaftEquipe FRM 2013Association Nationale de la Recherche et de la TechnologieCNRS-University of MontpellierFondation pour la Recherche Médicale1552-1568https://www.ebi.ac.uk/biostudies/studies/S-EPMC5602113biostudies-literatureUnknown23(10)Translational repression of maternal mRNAs is an essential regulatory mechanism during early embryonic development. Repression of the <i>Drosophila nanos</i> 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 <i>nanos</i> 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 <i>nanos</i> 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.RNA (New York, N.Y.)Translational repression of the <i>Drosophila nanos</i> mRNA involves the RNA helicase Belle and RNA coating by Me31B and Trailer hitch.PMC5602113ANR-15-CE12-0019-01FOR 855UMR9002WA 548/13-2GRK 1591WA 548/16-1DEQ20130326534Temme CDufourt JRammelt CSambrani NGotze MPierson SIhling CWahle ESimonelig MSinz A45falseTranslational repression of the <i>Drosophila nanos</i> mRNA involves the RNA helicase Belle and RNA coating by Me31B and Trailer hitch.Translational repression of maternal mRNAs is an essential regulatory mechanism during early embryonic development. Repression of the <i>Drosophila nanos</i> 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 <i>nanos</i> 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 <i>nanos</i> 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.2017-01-01T00:00:00Z2017 Oct2024-11-09T09:23:20.39Z2019-03-26T23:58:43ZS-EPMC56021132870152110.1261/rna.062208.117