RT Journal Article
T1 Staufen2-mediated RNA recognition and localization requires combinatorial action of multiple domains
A1 Heber, Simone
A1 Gáspár, Imre
A1 Tants, Jack-Niklas
A1 Günther, Johannes
A1 Fernandez Moya, Sandra Maria
A1 Janowski, Robert
A1 Ephrussi, Anne
A1 Sattler, Michael
A1 Niessing, Diessing
K1 Interacciones ARN-proteína
AB 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.
PB Springer Nature
YR 2019
FD 2019-04-10
LK https://hdl.handle.net/10630/45381
UL https://hdl.handle.net/10630/45381
LA eng
NO Heber, S., Gáspár, I., Tants, JN. et al. Staufen2-mediated RNA recognition and localization requires combinatorial action of multiple domains. Nat Commun 10, 1659 (2019). https://doi.org/10.1038/s41467-019-09655-3
NO Deutsche Forschungsgemeinschaft
DS RIUMA. Repositorio Institucional de la Universidad de Málaga
RD 4 mar 2026