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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 PMC
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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.
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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
Language english
Publication Year 2019
HGF-reported in Year 2019
ISSN (print) / ISBN 2041-1723
e-ISSN 2041-1723
Journal Nature Communications
Quellenangaben Volume: 10, Issue: 1, Pages: , Article Number: 1659 Supplement: ,
Publisher Nature Publishing Group
Publishing Place London
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)
POF-Topic(s) 30203 - Molecular Targets and Therapies
Research field(s) Enabling and Novel Technologies
PSP Element(s) G-503091-001
G-503000-001
DOI 10.1038/s41467-019-09655-3
WOS ID WOS:000463984400008
Scopus ID 85064721418
PubMed ID 30971701
Erfassungsdatum 2019-04-11
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