Translational repression of the Drosophila nanos mRNA involves the RNA helicase Belle and RNA coating by Me31B and Trailer hitch

• Published in: RNA (Cambridge) 2017-10, Vol.23 (10), p.1552-1568
• Main Authors: Götze, Michael, Dufourt, Jérémy, Ihling, Christian, Rammelt, Christiane, Pierson, Stephanie, Sambrani, Nagraj, Temme, Claudia, Sinz, Andrea, Simonelig, Martine, Wahle, Elmar
• Format: Article
• Language: English
• Subjects: 3' Untranslated regions; Adenosine triphosphatase; Animals; DEAD-box RNA Helicases - genetics; DEAD-box RNA Helicases - metabolism; DNA helicase; Drosophila; Drosophila melanogaster - embryology; Drosophila melanogaster - genetics; Drosophila Proteins - genetics; Drosophila Proteins - metabolism; Embryo, Nonmammalian; Embryogenesis; Gene Expression Regulation; Genetics; Initiation factor eIF-4E; Insects; Life Sciences; mRNA; Multiprotein Complexes - genetics; Multiprotein Complexes - metabolism; Protein Biosynthesis; Repressor Proteins - genetics; Repressor Proteins - metabolism; Ribonucleoproteins - genetics; Ribonucleoproteins - metabolism; RNA helicase; RNA Helicases - genetics; RNA Helicases - metabolism; RNA, Messenger - chemistry; RNA, Messenger - genetics; RNA, Messenger - metabolism; RNA-Binding Proteins - genetics; RNA-Binding Proteins - metabolism
• ISSN: 1355-8382; 1469-9001
• DOI: 10.1261/rna.062208.117

Translational repression of maternal mRNAs is an essential regulatory mechanism during early embryonic development. Repression of the 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 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 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.