Role of ATP hydrolysis by UvrA and UvrB during nucleotide excision repair

Res Microbiol. Apr-May 2001;152(3-4):401-9. doi: 10.1016/s0923-2508(01)01211-6.

Abstract

Nucleotide excision repair in eubacteria is a process that repairs DNA damages by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.

Publication types

  • Review

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism*
  • DNA Damage
  • DNA Helicases / metabolism*
  • DNA Repair*
  • DNA Replication
  • DNA, Bacterial / biosynthesis
  • DNA, Bacterial / metabolism*
  • DNA, Bacterial / radiation effects
  • DNA-Binding Proteins / metabolism*
  • Endodeoxyribonucleases / metabolism
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / metabolism

Substances

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