Ordered conformational changes in damaged DNA induced by nucleotide excision repair factors

J Biol Chem. 2004 Apr 30;279(18):19074-83. doi: 10.1074/jbc.M312611200. Epub 2004 Feb 23.

Abstract

In response to genotoxic attacks, cells activate sophisticated DNA repair pathways such as nucleotide excision repair (NER), which consists of damage removal via dual incision and DNA resynthesis. Using permanganate footprinting as well as highly purified factors, we show that NER is a dynamic process that takes place in a number of successive steps during which the DNA is remodeled around the lesion in response to the various NER factors. XPC/HR23B first recognizes the damaged structure and initiates the opening of the helix from position -3 to +6. TFIIH is then recruited and, in the presence of ATP, extends the opening from position -6 to +6; it also displaces XPC downstream from the lesion, thereby providing the topological structure for recruiting XPA and RPA, which will enlarge the opening. Once targeted by XPG, the damaged DNA is further melted from position -19 to +8. XPG and XPF/ERCC1 endonucleases then cut the damaged DNA at the limit of the opened structure that was previously "labeled" by the positioning of XPC/HR23B and TFIIH.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate
  • DNA / chemistry*
  • DNA / genetics*
  • DNA / metabolism
  • DNA Damage
  • DNA Repair Enzymes
  • DNA Repair*
  • DNA-Binding Proteins / genetics
  • Endonucleases
  • Humans
  • Nuclear Proteins
  • Nucleic Acid Conformation
  • Replication Protein A
  • Transcription Factor TFIIH
  • Transcription Factors
  • Transcription Factors, TFII / genetics
  • Xeroderma Pigmentosum Group A Protein

Substances

  • DNA excision repair protein ERCC-5
  • DNA-Binding Proteins
  • Nuclear Proteins
  • RPA1 protein, human
  • Replication Protein A
  • Transcription Factors
  • Transcription Factors, TFII
  • XPA protein, human
  • Xeroderma Pigmentosum Group A Protein
  • Transcription Factor TFIIH
  • RAD23A protein, human
  • Adenosine Triphosphate
  • DNA
  • Endonucleases
  • DNA Repair Enzymes