2. Academic Validation
  3. Roquin binding to target mRNAs involves a winged helix-turn-helix motif

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

  • Nat Commun. 2014 Dec 11;5:5701. doi: 10.1038/ncomms6701.
Anja Schuetz 1,  Yasuhiro Murakawa 2,  Eva Rosenbaum 3,  Markus Landthaler 2,  Udo Heinemann 4
Affiliations

Affiliations

  • 1 Helmholtz Protein Sample Production Facility, Max Delbrück Center for Molecular Medicine, 13092 Berlin, Germany.
  • 2 Laboratory for RNA Biology and Posttranscriptional Regulation, Berlin Institute for Medical Systems Biology, Max Delbrück Center for Molecular Medicine, 13092 Berlin, Germany.
  • 3 Structure and Membrane Interaction of G-Proteins, Max Delbrück Center for Molecular Medicine, 13092 Berlin, Germany.
  • 4 1] Helmholtz Protein Sample Production Facility, Max Delbrück Center for Molecular Medicine, 13092 Berlin, Germany [2] Chemistry and Biochemistry Institute, Freie Universität Berlin, 14195 Berlin, Germany.
PMID: 25504471 DOI: 10.1038/ncomms6701
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.

Figures