RNA recognition by the Vts1p SAM domain
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Updated: Aug 13, 2026

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods
Published on: December 21, 2019
Philip E Johnson1, Logan W Donaldson
1Department of Chemistry, York University, 4700 Keele Street, Toronto, Ontario, Canada, M3J 1P3. pjohnson@yorku.ca <pjohnson@yorku.ca>
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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