Orientation of the central domains of KSRP and its implications for the interaction with the RNA targets

Nucleic Acids Res. 2010 Aug;38(15):5193-205. doi: 10.1093/nar/gkq216. Epub 2010 Apr 12.

Abstract

KSRP is a multi-domain RNA-binding protein that recruits the exosome-containing mRNA degradation complex to mRNAs coding for cellular proliferation and inflammatory response factors. The selectivity of this mRNA degradation mechanism relies on KSRP recognition of AU-rich elements in the mRNA 3'UTR, that is mediated by KSRP's KH domains. Our structural analysis shows that the inter-domain linker orients the two central KH domains of KSRP-and their RNA-binding surfaces-creating a two-domain unit. We also show that this inter-domain arrangement is important to the interaction with KSRP's RNA targets.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3' Untranslated Regions*
  • Amino Acid Sequence
  • Binding Sites
  • Cell Line
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Interaction Domains and Motifs
  • RNA / chemistry
  • RNA / metabolism
  • RNA-Binding Proteins / chemistry*
  • RNA-Binding Proteins / metabolism
  • Trans-Activators / chemistry
  • Trans-Activators / metabolism

Substances

  • 3' Untranslated Regions
  • KHSRP protein, human
  • RNA-Binding Proteins
  • Trans-Activators
  • RNA

Associated data

  • PDB/2JVZ
  • PDB/2OPV