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

Author

Listed:
  • 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
    Chemistry and Biochemistry Institute, Freie Universität Berlin)

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.

Suggested Citation

  • Anja Schuetz & Yasuhiro Murakawa & Eva Rosenbaum & Markus Landthaler & Udo Heinemann, 2014. "Roquin binding to target mRNAs involves a winged helix-turn-helix motif," Nature Communications, Nature, vol. 5(1), pages 1-7, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms6701
    DOI: 10.1038/ncomms6701
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