Abstract
The putative yeast post-transcriptional regulator Vts1p and its related protein Smaug, from Drosophila melanogaster, each use a sterile alpha motif (SAM) domain to bind an RNA hairpin termed the Smaug recognition element (SRE). Here, we present the NMR structures of the Vts1p–SRE complex and the free SRE. Structural highlights include the direct recognition of a guanine base and the formation or stabilization of a base pair in the SRE loop.
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Acknowledgements
We are grateful to A. Amborski, J. Kwan, M. Motamed and X. Zhao for their assistance. NMR datasets at 800 MHz were acquired at the National High Field NMR Centre and the Québec/Eastern Canada High Field NMR Facility. This work was supported by funding from the Canadian Institutes of Health Research to P.E.J. and L.W.D.
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Supplementary information
Supplementary Fig. 1
Superposition of ten structures comprising the Vts1–SRE structural ensemble (PDF 2663 kb)
Supplementary Fig. 2
The SAM domains of Vts1 and Smaug (PDF 1124 kb)
Supplementary Fig. 3
Observed intermolecular NOEs between Vts1 and the SRE RNA (PDF 699 kb)
Supplementary Fig. 4
Superposition of 10 structures comprising the free and Vts1-bound SRE RNA ensembles (PDF 1469 kb)
Supplementary Table 1
Statistics for the Vts1 SAM domain–SRE RNA ensemble of structures (PDF 44 kb)
Supplementary Table 2
Intermolecular NOEs observed between the Vts1 SAM domain and the SRE RNA (PDF 31 kb)
Supplementary Table 3
Statistics for the free SRE RNA ensemble of structures (PDF 31 kb)
Supplementary Table 4
Proton chemical shift changes in the SRE pentaloop upon binding the Vts1 SAM domain (PDF 29 kb)
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Johnson, P., Donaldson, L. RNA recognition by the Vts1p SAM domain. Nat Struct Mol Biol 13, 177–178 (2006). https://doi.org/10.1038/nsmb1039
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DOI: https://doi.org/10.1038/nsmb1039
