Human homologs of Schizosaccharomyces pombe rad1, hus1, and rad9 form a DNA damage-responsive protein complex

J Biol Chem. 1999 Jan 8;274(2):567-70. doi: 10.1074/jbc.274.2.567.

Abstract

DNA damage activates cell cycle checkpoints in yeast and human cells. In the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe checkpoint-deficient mutants have been characterized, and the corresponding genes have been cloned. Searches for human homologs of S. pombe rad1, rad9, and hus1 genes identified the potential human homologs hRad1, hRad9, and hHus1; however, little is known about the roles of these proteins in human cells. The present studies demonstrate that hRad1 and hHus1 associate in a complex that interacts with a highly modified form of hRad9, but hHus1 and hRad1 do not associate with hRad17. In addition to being a key participant in complex formation, hRad9 is phosphorylated in response to DNA damage. Together, these results suggest that hRad9, hRad1, and hHus1 are central components of a DNA damage-responsive protein complex in human cells.

MeSH terms

  • Cell Cycle Proteins / metabolism*
  • Cell Line
  • DNA Damage*
  • DNA Repair Enzymes
  • DNA-Binding Proteins*
  • Endonucleases / metabolism*
  • Epitopes / metabolism
  • Fungal Proteins / metabolism*
  • Humans
  • Phosphorylation
  • Protein Binding
  • Protein Processing, Post-Translational
  • Recombinant Proteins / metabolism
  • Saccharomyces cerevisiae Proteins
  • Schizosaccharomyces / metabolism*
  • Schizosaccharomyces pombe Proteins

Substances

  • Cell Cycle Proteins
  • DNA-Binding Proteins
  • Epitopes
  • Fungal Proteins
  • Recombinant Proteins
  • Saccharomyces cerevisiae Proteins
  • Schizosaccharomyces pombe Proteins
  • hus1 protein, S pombe
  • rad9 protein
  • Endonucleases
  • RAD1 protein, S cerevisiae
  • rad1 protein, S pombe
  • DNA Repair Enzymes