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RNA binding proteins Smaug and Cup induce CCR4-NOT-dependent deadenylation of the nanos mRNA in a reconstituted system

View ORCID ProfileFilip Pekovic, Christiane Rammelt, Jana Kubíková, View ORCID ProfileJutta Metz, View ORCID ProfileMandy Jeske, View ORCID ProfileElmar Wahle
doi: https://doi.org/10.1101/2022.05.11.491288
Filip Pekovic
1Institute of Biochemistry and Biotechnology and Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, Kurt-Mothes-Strasse 3a, 06120 Halle, Germany
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Christiane Rammelt
1Institute of Biochemistry and Biotechnology and Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, Kurt-Mothes-Strasse 3a, 06120 Halle, Germany
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Jana Kubíková
2Heidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, 69120 Heidelberg, Germany
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Jutta Metz
2Heidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, 69120 Heidelberg, Germany
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Mandy Jeske
2Heidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, 69120 Heidelberg, Germany
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  • For correspondence: ewahle@biochemtech.uni-halle.de jeske@bzh.uni-heidelberg.de
Elmar Wahle
1Institute of Biochemistry and Biotechnology and Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, Kurt-Mothes-Strasse 3a, 06120 Halle, Germany
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  • For correspondence: ewahle@biochemtech.uni-halle.de jeske@bzh.uni-heidelberg.de
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ABSTRACT

Posttranscriptional regulation of the maternal nanos mRNA is essential for the development of the anterior – posterior axis of the Drosophila embryo. The nanos RNA is regulated by the protein Smaug. Binding to Smaug recognition elements (SREs) in the nanos 3’-UTR, Smaug nucleates the assembly of a larger repressor complex including the eIF4E-T paralog Cup and five additional proteins. The Smaug-dependent complex represses translation of nanos and induces its deadenylation by the CCR4-NOT deadenylase. Here we report an in vitro reconstitution of the Drosophila CCR4-NOT complex and Smaug-dependent deadenylation. We find that Smaug by itself is sufficient to cause deadenylation by the Drosophila or human CCR4-NOT complexes in an SRE-dependent manner. CCR4-NOT subunits NOT10 and NOT11 are dispensable, but the NOT module, consisting of NOT2, NOT3 and the C-terminal part of NOT1, is required. Smaug interacts with the C-terminal domain of NOT3. Both catalytic subunits of CCR4-NOT contribute to Smaug-dependent deadenylation. Whereas the CCR4-NOT complex itself acts distributively, Smaug induces a processive behavior. The cytoplasmic poly(A) binding protein (PABPC) has but a minor effect on Smaug-dependent deadenylation. Among the additional constituents of the Smaug-dependent repressor complex, Cup also facilitates CCR4-NOT-dependent deadenylation, both independently and in cooperation with Smaug.

Competing Interest Statement

The authors have declared no competing interest.

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Posted May 11, 2022.
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RNA binding proteins Smaug and Cup induce CCR4-NOT-dependent deadenylation of the nanos mRNA in a reconstituted system
Filip Pekovic, Christiane Rammelt, Jana Kubíková, Jutta Metz, Mandy Jeske, Elmar Wahle
bioRxiv 2022.05.11.491288; doi: https://doi.org/10.1101/2022.05.11.491288
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RNA binding proteins Smaug and Cup induce CCR4-NOT-dependent deadenylation of the nanos mRNA in a reconstituted system
Filip Pekovic, Christiane Rammelt, Jana Kubíková, Jutta Metz, Mandy Jeske, Elmar Wahle
bioRxiv 2022.05.11.491288; doi: https://doi.org/10.1101/2022.05.11.491288

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