PuSH - Publication Server of Helmholtz Zentrum München

Heber, S. ; Gáspár, I.* ; Tants, J.-N. ; Günther, J. ; Fernandez Moya, S.M.* ; Janowski, R. ; Ephrussi, A.* ; Sattler, M. ; Niessing, D.

Staufen2-mediated RNA recognition and localization requires combinatorial action of multiple domains.

Nat. Commun. 10:1659 (2019)
Publ. Version/Full Text Research data DOI
Open Access Gold
Creative Commons Lizenzvertrag
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 Cterminal 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.
Additional Metrics?
Edit extra informations Login
Publication type Article: Journal article
Document type Scientific Article
Keywords Double-stranded-rna; Binding-protein Staufen2; Somatodendritic Domain; Secondary Structures; Mammalian Staufen; Nmr; Segregation; Platform; Distinct; Neurons
ISSN (print) / ISBN 2041-1723
e-ISSN 2041-1723
Quellenangaben Volume: 10, Issue: 1, Pages: , Article Number: 1659 Supplement: ,
Publisher Nature Publishing Group
Publishing Place London
Reviewing status Peer reviewed