Achieving broad substrate specificity in damage recognition by binding accessible nondamaged DNA

Mol Cell. 2007 Oct 26;28(2):184-6. doi: 10.1016/j.molcel.2007.10.006.

Abstract

The structure of the Rad4/Rad23 protein, shown in a recent issue of Nature (Min and Pavletich, 2007), reveals how structurally diverse lesions are recognized in eukaryotic nucleotide excision repair: by probing for accessible nondamaged DNA opposite the lesion.

MeSH terms

  • DNA Damage*
  • DNA Repair*
  • DNA, Fungal / chemistry
  • DNA, Fungal / metabolism*
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism*
  • Models, Molecular
  • Nucleic Acid Conformation
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Transcription Factor TFIIH / metabolism

Substances

  • DNA, Fungal
  • DNA-Binding Proteins
  • RAD23 protein, S cerevisiae
  • Rad4 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Transcription Factor TFIIH