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. 2019 Apr 10;10:1659. doi: 10.1038/s41467-019-09655-3

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — The dsRBD1–2 tandem domain of mStau2 binds RNA. a EMSAs with full-length mStau2 (mStau2 FL) and different SRS RNAs from the 3′UTR of the Rgs4 mRNA. b EMSAs with mStau2 tandem domains dsRBD1–2 or dsRBD3–4 and SRS2. c NMR titration experiments of mStau2 dsRBD1–2 with SRS2 RNA. d Crystal structure of SRS2 at 1.73 Å resolution. Iminos from c showing significant line broadening are indicated by colored (orange to red) spheres. e EMSAs with mStau2 tandem domains dsRBD 1–2 or dsRBD 3–4 and SRS2 RNA extended by five basepairs (SRS2 + 5). f NMR titration experiments of mStau2 dsRBD 1–2 with SRS2 + 5 RNA. Left: overlay of ¹H,¹⁵N-HSQC spectra of dsRBD1–2 in absence and presence of 2x excess SRS2 + 5 RNA. Resonance shifts and line broadening of several signals are observed. Right: comparison of 1D imino traces of SRS2 + 5 RNA at different stoichiometric ratios with dsRBD 1–2. Strong line broadening of imino signals is observed in presence of protein. Source data are provided as a Source Data file