Roquin binding to target mRNAs involves a winged helix-turn-helix motif

Item Type:	Article
Title:	Roquin binding to target mRNAs involves a winged helix-turn-helix motif
Creators Name:	Schuetz, A. and Murakawa, Y. and Rosenbaum, E. and Landthaler, M. and Heinemann, U.
Abstract:	Roquin proteins mediate mRNA deadenylation by recognizing a conserved class of stem-loop RNA degradation motifs via their Roquin domain. Here we present the crystal structure of a Roquin domain, revealing a mostly helical protein fold bearing a winged helix-turn-helix motif. By combining structural, biochemical and mutation analyses, we gain insight into the mode of RNA binding. We show that the winged helix-turn-helix motif is involved in the binding of constitutive decay elements-containing stem-loop mRNAs. Moreover, we provide biochemical evidence that Roquin proteins are additionally able to bind to duplex RNA and have the potential to be functional in different oligomeric states.
Keywords:	Binding Sites, Double-Stranded RNA, Escherichia Coli, Gene Expression, Hydrolysis, Messenger RNA, Molecular Models, Nucleic Acid Conformation, Poly A, Protein Binding, RNA-Binding Proteins, Recombinant Proteins, Secondary Protein Structure, Tertiary Protein Structure, Ubiquitin-Protein Ligases, X-Ray Crystallography
Source:	Nature Communications
ISSN:	2041-1723
Publisher:	Nature Publishing Group
Volume:	5
Page Range:	5701
Date:	11 December 2014
Official Publication:	https://doi.org/10.1038/ncomms6701
PubMed:	View item in PubMed

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