The polyanionic C-terminal tail of human Rad17 regulates interaction with the 9-1-1 complex

Biochem Biophys Res Commun. 2017 Sep 2;490(4):1147-1153. doi: 10.1016/j.bbrc.2017.06.159. Epub 2017 Jun 28.

Abstract

In the activation and maintenance of ATR-dependent DNA damage checkpoint, the interaction between the Rad17-RFC2-5 and 9-1-1 complexes is essential, however, the regulatory mechanism of the interaction is not known. Here we show that vertebrate Rad17 proteins contain a polyanionic 12-amino acid sequence in the C-terminal ends that is important for the 9-1-1 interaction. We demonstrate that the C-terminal tail contains a conserved sequence designated iVERGE that must be intact for the 9-1-1 interaction and contains potential posttranslational modification sites. Our data raise a possibility that the Rad17 C-terminal tail is a molecular switch that regulates the 9-1-1 interaction and the ATR pathway.

Keywords: ATR; Cell cycle checkpoint; DNA damage response; Rad17; The 9–1–1 complex.

MeSH terms

  • Cell Cycle Proteins / chemistry
  • Cell Cycle Proteins / metabolism*
  • Cells, Cultured
  • Exonucleases / metabolism
  • Humans
  • Multiprotein Complexes / chemistry
  • Multiprotein Complexes / metabolism*
  • Polyelectrolytes
  • Polymers / metabolism*

Substances

  • Cell Cycle Proteins
  • HUS1B protein, human
  • Multiprotein Complexes
  • Polyelectrolytes
  • Polymers
  • Rad17 protein, human
  • polyanions
  • rad9 protein
  • Exonucleases
  • Rad1 protein, human