A multipronged approach to understanding the form and function of hStaufen protein

• Published in: RNA (Cambridge) Vol. 26; no. 3; pp. 265 - 277
• Main Authors: Visentin, Silvia, Cannone, Giuseppe, Doutch, James, Harris, Gemma, Gleghorn, Michael L, Clifton, Luke, Smith, Brian O, Spagnolo, Laura
• Format: Journal Article
• Language: English
• Published: United States Cold Spring Harbor Laboratory Press 01-03-2020
• Subjects: Amino Acid Sequence - genetics; Cytoskeletal Proteins - chemistry; Cytoskeletal Proteins - ultrastructure; Double-stranded RNA; Functional plasticity; Humans; mRNA turnover; Nucleic Acid Conformation; Protein Biosynthesis; Protein Conformation; Protein interaction; Protein Interaction Domains and Motifs - genetics; Proteins; RNA Stability - genetics; RNA transport; RNA-Binding Proteins - chemistry; RNA-Binding Proteins - ultrastructure; structural biology; dsRNA-binding domain; SAXS; Staufen
• ISSN: 1355-8382; 1469-9001
• DOI: 10.1261/rna.072595.119

Staufen is a dsRNA-binding protein involved in many aspects of RNA regulation, such as mRNA transport, Staufen-mediated mRNA decay and the regulation of mRNA translation. It 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 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 hStaufen1
, showing that its domains are arranged as beads-on-a-string connected by flexible linkers. In analogy with other nucleic acid-binding proteins, this could underpin Stau1 functional plasticity.