A multi-pronged approach to understanding the form and function of hStaufen protein
- Silvia Visentin1,
- Giuseppe Cannone2,
- James Doutch3,
- Gemma Harris4,
- Michael L. Gleghorn5,
- Luke Clifton3,
- Brian O. Smith6 and
- Laura Spagnolo7,8
- 1 University of Glasgow, Institute of Molecular, Cell and Systems Biology;
- 2 MRC Laboratory of Molecular Biology, Cambridge, UK;
- 3 ISIS Pulsed Neutron and Muon Source, Science and Technology Facilities Council (STFC), Rutherford Appleton Laboratory, Didcot, OX11 OQX, UK;
- 4 Research Complex at Harwell, Rutherford Appleton Laboratory, Research Complex at Harwell, Didcot, OX11 0FA, UK;
- 5 School of Chemistry and Materials Science, College of Science, Rochester Institute of Technology, Rochester, New York 14623, USA;
- 6 University of Glasgow; Institute of Molecular, Cell and Systems Biology;
- 7 University of Glasgow, UK Institute of Molecular, Cell and Systems Biology
- ↵* Corresponding author; email: laura.spagnolo{at}glasgow.ac.uk
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.
Keywords
- Received July 3, 2019.
- Accepted December 9, 2019.
- Published by Cold Spring Harbor Laboratory Press for the RNA Society
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