DNA damage-dependent recruitment of nucleotide excision repair and transcription proteins to Escherichia coli inner membranes

Nucleic Acids Res. 1997 Aug 1;25(15):3151-8. doi: 10.1093/nar/25.15.3151.


The entire process of nucleotide excision repair (NER) in Escherichia coli has been reconstituted in vitro from purified proteins and defined DNA substrates. However, how this system is organized in vivo in unclear. We report here the isolation and characterization of macromolecular assemblies containing NER and transcription proteins from E. coli. This ensemble consists of at least 17 proteins. They are recruited, as a consequence of DNA damage induced by UV irradiation, to the inner membrane. The UV-induced 6-4 photoproducts are also relocated to the inner membrane following UV-irradiation of the cells. This recruitment process is dependent on the uvrA, uvrC and recA gene products. These results suggest that at least part of the repair process may associate with the inner membrane and also provide insights into understanding the cellular organization of repair processes.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / biosynthesis
  • Adenosine Triphosphatases / metabolism*
  • Bacterial Proteins / biosynthesis
  • Bacterial Proteins / metabolism*
  • Cell Membrane / metabolism
  • Chromosomes, Bacterial
  • DNA Damage*
  • DNA Helicases*
  • DNA Repair*
  • DNA-Binding Proteins / biosynthesis
  • DNA-Binding Proteins / metabolism*
  • Endodeoxyribonucleases*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Escherichia coli / radiation effects
  • Escherichia coli / ultrastructure
  • Escherichia coli Proteins*
  • Mutation
  • Transcription, Genetic
  • Ultraviolet Rays


  • Bacterial Proteins
  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • UvrB protein, E coli
  • Endodeoxyribonucleases
  • UvrC protein, E coli
  • UvrA protein, E coli
  • Adenosine Triphosphatases
  • DNA Helicases