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PDBsum entry 6h0r
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DOI no:
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Nat Commun
10:1659
(2019)
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PubMed id:
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Staufen2-mediated RNA recognition and localization requires combinatorial action of multiple domains.
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S.Heber,
I.Gáspár,
J.N.Tants,
J.Günther,
S.M.F.Moya,
R.Janowski,
A.Ephrussi,
M.Sattler,
D.Niessing.
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ABSTRACT
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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 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.
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');
}
}
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