The human checkpoint sensor and alternative DNA clamp Rad9-Rad1-Hus1 modulates the activity of DNA ligase I, a component of the long-patch base excision repair machinery

Biochem J. 2005 Jul 1;389(Pt 1):13-7. doi: 10.1042/BJ20050211.

Abstract

The human checkpoint sensor and alternative clamp Rad9-Rad1-Hus1 can interact with and specifically stimulate DNA ligase I. The very recently described interactions of Rad9-Rad1-Hus1 with MutY DNA glycosylase, DNA polymerase beta and Flap endonuclease 1 now complete our view that the long-patch base excision machinery is an important target of the Rad9-Rad1-Hus1 complex, thus enhancing the quality control of DNA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Cycle Proteins / metabolism*
  • DNA Damage
  • DNA Ligase ATP
  • DNA Ligases / metabolism*
  • DNA Repair / physiology*
  • Enzyme Activation
  • Exonucleases / metabolism*
  • Humans
  • Multiprotein Complexes / metabolism
  • Proliferating Cell Nuclear Antigen / metabolism
  • Protein Binding
  • Schizosaccharomyces pombe Proteins / metabolism*

Substances

  • Cell Cycle Proteins
  • LIG1 protein, human
  • Multiprotein Complexes
  • Proliferating Cell Nuclear Antigen
  • Schizosaccharomyces pombe Proteins
  • hus1 protein, S pombe
  • rad9 protein
  • Exonucleases
  • Rad1 protein, human
  • DNA Ligases
  • DNA Ligase ATP