Structural highlights
Function
VTS1_YEAST RNA-binding protein involved in post-transcriptional regulation through transcript degradation of SRE (SMG-recognition elements) bearing mRNAs. May be involved in vacuolar protein transport.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
RNA recognition by the Vts1p SAM domain.,Johnson PE, Donaldson LW Nat Struct Mol Biol. 2006 Feb;13(2):177-8. Epub 2006 Jan 22. PMID:16429155[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dilcher M, Kohler B, von Mollard GF. Genetic interactions with the yeast Q-SNARE VTI1 reveal novel functions for the R-SNARE YKT6. J Biol Chem. 2001 Sep 14;276(37):34537-44. Epub 2001 Jul 9. PMID:11445562 doi:http://dx.doi.org/10.1074/jbc.M101551200
- ↑ Aviv T, Lin Z, Lau S, Rendl LM, Sicheri F, Smibert CA. The RNA-binding SAM domain of Smaug defines a new family of post-transcriptional regulators. Nat Struct Biol. 2003 Aug;10(8):614-21. PMID:12858164 doi:10.1038/nsb956
- ↑ Johnson PE, Donaldson LW. RNA recognition by the Vts1p SAM domain. Nat Struct Mol Biol. 2006 Feb;13(2):177-8. Epub 2006 Jan 22. PMID:16429155 doi:10.1038/nsmb1039
