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• W2092194403 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. Roquin proteins mediate the degradation of mRNAs through the recognition of stem-loop structures present within their 3′ UTR. Here Schuetz et al. present the crystal structure of a Roquin domain and, through complementary biochemical analyses, provide insight into Roquin's mode of RNA binding through a winged helix-turn-helix motif." @default.
• W2092194403 created "2016-06-24" @default.
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• W2092194403 date "2014-12-11" @default.
• W2092194403 modified "2023-09-26" @default.
• W2092194403 title "Roquin binding to target mRNAs involves a winged helix-turn-helix motif" @default.
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• W2092194403 doi "https://doi.org/10.1038/ncomms6701" @default.
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