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| Item Type: | Article |
|---|---|
| Title: | Roquin binding to target mRNAs involves a winged helix-turn-helix motif |
| Creators Name: | Schuetz, A., Murakawa, Y., Rosenbaum, E., Landthaler, M. and Heinemann, U. |
| Abstract: | Roquin proteins mediate mRNA deadenylation by recognizing a conserved class of stem-loop RNA degradation motifs via their Roquin domain. Here we present the crystal structure of a Roquin domain, revealing a mostly helical protein fold bearing a winged helix-turn-helix motif. By combining structural, biochemical and mutation analyses, we gain insight into the mode of RNA binding. We show that the winged helix-turn-helix motif is involved in the binding of constitutive decay elements-containing stem-loop mRNAs. Moreover, we provide biochemical evidence that Roquin proteins are additionally able to bind to duplex RNA and have the potential to be functional in different oligomeric states. |
| Keywords: | Binding Sites, Double-Stranded RNA, Escherichia Coli, Gene Expression, Hydrolysis, Messenger RNA, Molecular Models, Nucleic Acid Conformation, Poly A, Protein Binding, RNA-Binding Proteins, Recombinant Proteins, Secondary Protein Structure, Tertiary Protein Structure, Ubiquitin-Protein Ligases, X-Ray Crystallography |
| Source: | Nature Communications |
| ISSN: | 2041-1723 |
| Publisher: | Nature Publishing Group |
| Volume: | 5 |
| Page Range: | 5701 |
| Date: | 11 December 2014 |
| Official Publication: | https://doi.org/10.1038/ncomms6701 |
| PubMed: | View item in PubMed |
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