Structural insights into the human GW182-PABC interaction in microRNA-mediated deadenylation

Nat Struct Mol Biol. 2010 Feb;17(2):238-40. doi: 10.1038/nsmb.1768. Epub 2010 Jan 24.

Abstract

GW182-family proteins are essential for microRNA-mediated translational repression and deadenylation in animal cells. Here we show that a conserved motif in the human GW182 paralog TNRC6C interacts with the C-terminal domain of polyadenylate binding protein 1 (PABC) and present the crystal structure of the complex. Mutations at the complex interface impair mRNA deadenylation in mammalian cell extracts, suggesting that the GW182-PABC interaction contributes to microRNA-mediated gene silencing.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution / genetics
  • Crystallography, X-Ray
  • Humans
  • MicroRNAs / metabolism*
  • Models, Molecular
  • Mutagenesis, Site-Directed
  • Poly(A)-Binding Protein I / chemistry*
  • Poly(A)-Binding Protein I / metabolism*
  • Protein Binding
  • Protein Interaction Mapping
  • Protein Structure, Quaternary
  • RNA, Messenger / metabolism*
  • RNA-Binding Proteins / chemistry*
  • RNA-Binding Proteins / metabolism*

Substances

  • MicroRNAs
  • Poly(A)-Binding Protein I
  • RNA, Messenger
  • RNA-Binding Proteins
  • TNRC6C protein, human

Associated data

  • PDB/2X04