Structural highlights
Function
[STAU1_HUMAN] Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site.
Publication Abstract from PubMed
Staufen1 (STAU1) is a dsRNA binding protein mediating mRNA transport and localization, translational control and STAU1-mediated mRNA decay (SMD). The STAU1 binding site (SBS) within human ADP-ribosylation factor1 (ARF1) 3'UTR binds STAU1 and this downregulates ARF1 cytoplasmic mRNA levels by SMD. However, how STAU1 recognizes specific mRNA targets is still under debate. Our structure of the ARF1 SBS-STAU1 complex uncovers target recognition by STAU1. STAU1 dsRNA binding domain (dsRBD) 4 interacts with two pyrimidines and one purine from the minor groove side via helix alpha1, the beta1-beta2 loop anchors the dsRBD at the end of the dsRNA and lysines in helix alpha2 bind to the phosphodiester backbone from the major groove side. STAU1 dsRBD3 displays the same binding mode with specific recognition of one guanine base. Mutants disrupting minor groove recognition of ARF1 SBS affect in vitro binding and reduce SMD in vivo. Our data thus reveal how STAU1 recognizes minor groove features in dsRNA relevant for target selection.
Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition.,Yadav DK, Zigackova D, Zlobina M, Klumpler T, Beaumont C, Kubickova M, Vanacova S, Lukavsky PJ Nucleic Acids Res. 2020 Feb 28;48(4):2091-2106. doi: 10.1093/nar/gkz1163. PMID:31875226[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yadav DK, Zigackova D, Zlobina M, Klumpler T, Beaumont C, Kubickova M, Vanacova S, Lukavsky PJ. Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition. Nucleic Acids Res. 2020 Feb 28;48(4):2091-2106. doi: 10.1093/nar/gkz1163. PMID:31875226 doi:http://dx.doi.org/10.1093/nar/gkz1163
