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A multi-pronged approach to understanding the form and function of hStaufen protein

DOI: 10.1261/rna.072595.119 DOI Help

Authors: Silvia Visentin (University of Glasgow) , Giuseppe Cannone (University of Glasgow) , James Doutch (ISIS Pulsed Neutron and Muon Source) , Gemma Harris (Research Complex at Harwell) , Michael L. Gleghorn (Rochester Institute of Technology) , Luke Clifton (ISIS Pulsed Neutron and Muon Source) , Brian O. Smith (University of Glasgow) , Laura Spagnolo (University of Glasgow)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Rna

State: Published (Approved)
Published: December 2019
Diamond Proposal Number(s): 21035

Abstract: Staufen is a dsRNA binding protein that plays an essential role in many aspects of RNA regulation, such as mRNA transport, Staufen-mediated mRNA decay and the regulation of mRNA translation. Staufen is a modular protein characterized by the presence of conserved consensus amino acid sequences that fold into double-stranded RNA binding domains (RBDs) as well as degenerated RBDs that maintain the α-β-β-β-α fold but are unable to bind RNA and are instead involved in protein-protein interactions. The variety of biological processes in which Staufen participates in the cell suggests that this protein associates with many diverse RNA targets, some of which have been identified experimentally. Staufen binding mediates the recruitment of effectors via protein-protein and protein-RNA interactions. The structural determinants of a number of these interactions, as well as the structure of full-length Staufen, remain unknown. Here, we present the first solution structure models for full-length human Staufen155, showing that its domains are arranged as beads-on-a-string in the absence of RNA.

Journal Keywords: SAXS; Staufen; dsRNA binding domain; structural biology

Subject Areas: Biology and Bio-materials


Instruments: B21-High Throughput SAXS