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

Anja Schuetz, Yasuhiro Murakawa, Eva Rosenbaum, Markus Landthaler and Udo Heinemann ()
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Anja Schuetz: Helmholtz Protein Sample Production Facility, Max Delbrück Center for Molecular Medicine
Yasuhiro Murakawa: Laboratory for RNA Biology and Posttranscriptional Regulation, Berlin Institute for Medical Systems Biology, Max Delbrück Center for Molecular Medicine
Eva Rosenbaum: Structure and Membrane Interaction of G-Proteins, Max Delbrück Center for Molecular Medicine
Markus Landthaler: Laboratory for RNA Biology and Posttranscriptional Regulation, Berlin Institute for Medical Systems Biology, Max Delbrück Center for Molecular Medicine
Udo Heinemann: Helmholtz Protein Sample Production Facility, Max Delbrück Center for Molecular Medicine

Nature Communications, 2014, vol. 5, issue 1, 1-7

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms6701

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