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

Visentin, S., Cannone, G., Doutch, J., Harris, G., Gleghorn, M. L., Clifton, L., Smith, B. O. and Spagnolo, L. (2020) A multi-pronged approach to understanding the form and function of hStaufen protein. RNA, 26(3), pp. 265-277. (doi: 10.1261/rna.072595.119)

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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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Cannone, Dr Giuseppe and Spagnolo, Professor Laura and Visentin, Miss Silvia
Authors: Visentin, S., Cannone, G., Doutch, J., Harris, G., Gleghorn, M. L., Clifton, L., Smith, B. O., and Spagnolo, L.
College/School:College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
Journal Name:RNA
Publisher:Cold Spring Harbor Laboratory Press
ISSN:1355-8382
ISSN (Online):1469-9001
Published Online:18 December 2019
Copyright Holders:Copyright © 2019 RNA Society
First Published:First published in RNA 26(3):265-277
Publisher Policy:Reproduced in accordance with the copyright policy of the publisher

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