Journal
RNA
Volume 23, Issue 10, Pages 1552-1568Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1261/rna.062208.117
Keywords
translational repression; maternal RNA; deadenylation
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Funding
- Deutsche Forschungsgemeinschaft [WA 548/13-2, FOR 855, WA 548/16-1, GRK 1591]
- CNRS-University of Montpellier [UMR9002]
- Association Nationale de la Recherche et de la Technologie [ANR-15-CE12-0019-01]
- Fondation pour la Recherche Medicale (Equipe FRM) [DEQ20130326534]
- Fondation ARC pour la Recherche sur le Cancer (ARC Libre) [3192]
- Fondation ARC
- Agence Nationale de la Recherche (ANR) [ANR-15-CE12-0019] Funding Source: Agence Nationale de la Recherche (ANR)
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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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