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

Nat Commun. 2014 Dec 11:5:5701. 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Crystallography, X-Ray
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Gene Expression
  • Humans
  • Hydrolysis
  • Models, Molecular
  • Nucleic Acid Conformation
  • Poly A / chemistry*
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • RNA, Double-Stranded / chemistry*
  • RNA, Messenger / chemistry*
  • RNA-Binding Proteins / chemistry*
  • RNA-Binding Proteins / genetics
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Ubiquitin-Protein Ligases / chemistry*
  • Ubiquitin-Protein Ligases / genetics

Substances

  • RC3H1 protein, human
  • RNA, Double-Stranded
  • RNA, Messenger
  • RNA-Binding Proteins
  • Recombinant Proteins
  • Poly A
  • Ubiquitin-Protein Ligases

Associated data

  • PDB/4ULW