Staufen2 mediated RNA recognition and localization requires combinatorial action of multiple domains
| Autor: | Imre Gaspar, Jan-Niklas Tants, Simone Heber, Robert Janowski, Dierk Niessing, Johannes C. Günther, Sandra M. Fernández Moya, Michael Sattler, Anne Ephrussi |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Embryo Nonmammalian Mutant General Physics and Astronomy 02 engineering and technology Plasma protein binding medicine.disease_cause Animals Genetically Modified Drosophila Proteins lcsh:Science Mutation Multidisciplinary biology Chemistry RNA-Binding Proteins 021001 nanoscience & nanotechnology Recombinant Proteins ddc Cell biology Drosophila melanogaster Female 0210 nano-technology Protein Binding Cell type animal structures Science Nerve Tissue Proteins Mrna binding Article General Biochemistry Genetics and Molecular Biology Double-stranded RNA binding 03 medical and health sciences Protein Domains medicine Animals RNA Messenger RNA Double-Stranded Messenger RNA Mutagenesis RNA General Chemistry biology.organism_classification 030104 developmental biology Mutagenesis Site-Directed Oocytes lcsh:Q Function (biology) |
| Zdroj: | Nature Communications, Vol 10, Iss 1, Pp 1-16 (2019) Nat. Commun. 10:1659 (2019) Nature Communications 'Nature Communications ', vol: 10, pages: 1659-1-1659-16 (2019) |
| ISSN: | 2041-1723 |
| DOI: | 10.1101/396994 |
| Popis: | Throughout metazoans, Staufen (Stau) proteins are core factors of mRNA localization particles. They consist of three to four double-stranded RNA binding domains (dsRBDs) and a C-terminal dsRBD-like domain. Mouse Staufen2 (mStau2)-like Drosophila Stau (dmStau) contains four dsRBDs. Existing data suggest that only dsRBDs 3–4 are necessary and sufficient for mRNA binding. Here, we show that dsRBDs 1 and 2 of mStau2 bind RNA with similar affinities and kinetics as dsRBDs 3 and 4. While RNA binding by these tandem domains is transient, all four dsRBDs recognize their target RNAs with high stability. Rescue experiments in Drosophila oocytes demonstrate that mStau2 partially rescues dmStau-dependent mRNA localization. In contrast, a rescue with mStau2 bearing RNA-binding mutations in dsRBD1–2 fails, confirming the physiological relevance of our findings. In summary, our data show that the dsRBDs 1–2 play essential roles in the mRNA recognition and function of Stau-family proteins of different species. The Staufen family of RNA-binding proteins are conserved microtubule dependent mRNA transporter factors. Here the authors use biochemical and functional approaches to characterize the RNA-binding properties of mouse Staufen 2 and study the mRNA binding capacity of its two domains dsRBDs 1 and 2. |
| Databáze: | OpenAIRE |
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