Holding damaged DNA together

Nat Struct Biol. 1999 Sep;6(9):805-6. doi: 10.1038/12257.

Abstract

The mammalian X-ray cross-complementing group 1 protein (XRCC1) is an important player in base excision repair of damaged DNA. Two new findings help to elucidate its role - biochemical data suggest that this multidomain protein interacts not only with three different enzymes, but also with the nicked DNA itself, and NMR data reveal the structure of the domain that interacts with both DNA polymerase beta and DNA.

Publication types

  • News
  • Comment

MeSH terms

  • DNA / genetics
  • DNA / metabolism*
  • DNA Damage / genetics*
  • DNA Ligase ATP
  • DNA Ligases / metabolism
  • DNA Polymerase beta / metabolism*
  • DNA Repair*
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism*
  • Humans
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Poly(ADP-ribose) Polymerases / metabolism
  • Poly-ADP-Ribose Binding Proteins
  • Protein Binding
  • Protein Conformation
  • X-ray Repair Cross Complementing Protein 1
  • Xenopus Proteins

Substances

  • DNA-Binding Proteins
  • Poly-ADP-Ribose Binding Proteins
  • X-ray Repair Cross Complementing Protein 1
  • XRCC1 protein, human
  • Xenopus Proteins
  • DNA
  • Poly(ADP-ribose) Polymerases
  • DNA Polymerase beta
  • DNA Ligases
  • DNA Ligase ATP
  • DNA ligase III alpha protein, Xenopus