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Staufen1 reads out structure and sequence features in ARF1 dsRNA for target recognition
DK. Yadav, D. Zigáčková, M. Zlobina, T. Klumpler, C. Beaumont, M. Kubíčková, Š. Vaňáčová, PJ. Lukavsky,
Jazyk angličtina Země Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem
Free Medical Journals od 1996
PubMed Central od 1974
Europe PubMed Central od 1974
Open Access Digital Library od 1996-01-01 do 2030-12-31
Open Access Digital Library od 1974-01-01
Open Access Digital Library od 1996-01-01
Open Access Digital Library od 1996-01-01
Medline Complete (EBSCOhost) od 1996-01-01
Oxford Journals Open Access Collection od 1996-01-01
ROAD: Directory of Open Access Scholarly Resources od 1974
Odkazy
PubMed
31875226
DOI
10.1093/nar/gkz1163
Knihovny.cz E-zdroje
- MeSH
- ADP-ribosylační faktor 1 chemie genetika MeSH
- cytoplazma chemie genetika MeSH
- cytoskeletální proteiny chemie genetika MeSH
- dvouvláknová RNA chemie genetika MeSH
- konformace proteinů MeSH
- lidé MeSH
- proteiny vázající RNA chemie genetika MeSH
- stabilita RNA genetika MeSH
- vazebná místa genetika MeSH
- vazebný motiv pro dvoušroubovici RNA genetika MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
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 α1, the β1-β2 loop anchors the dsRBD at the end of the dsRNA and lysines in helix α2 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.
Central European Institute of Technology Masaryk University Kamenice 753 5 62500 Brno Czech Republic
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