Anti-mutagenic activity of DNA damage-binding proteins mediated by direct inhibition of translesion replication

J Biol Chem. 1997 Nov 14;272(46):28906-11. doi: 10.1074/jbc.272.46.28906.

Abstract

DNA lesions that block replication can be bypassed in Escherichia coli by a special DNA synthesis process termed translesion replication. This process is mutagenic due to the miscoding nature of the DNA lesions. We report that the repair enzyme formamido-pyrimidine DNA glycosylase and the general DNA damage recognition protein UvrA each inhibit specifically translesion replication through an abasic site analog by purified DNA polymerases I and II, and DNA polymerase III (alpha subunit) from E. coli. In vivo experiments suggest that a similar inhibitory mechanism prevents at least 70% of the mutations caused by ultraviolet light DNA lesions in E. coli. These results suggest that DNA damage-binding proteins regulate mutagenesis by a novel mechanism that involves direct inhibition of translesion replication. This mechanism provides anti-mutagenic defense against DNA lesions that have escaped DNA repair.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Antimutagenic Agents / metabolism*
  • Bacterial Proteins / metabolism
  • DNA Damage*
  • DNA Replication*
  • DNA, Single-Stranded / metabolism
  • DNA-Binding Proteins / metabolism*
  • DNA-Formamidopyrimidine Glycosylase
  • Deoxyribodipyrimidine Photo-Lyase / metabolism
  • Escherichia coli Proteins*
  • Mutagenesis
  • N-Glycosyl Hydrolases / metabolism
  • Ultraviolet Rays

Substances

  • Antimutagenic Agents
  • Bacterial Proteins
  • DNA, Single-Stranded
  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • N-Glycosyl Hydrolases
  • DNA-Formamidopyrimidine Glycosylase
  • DNA-formamidopyrimidine glycosylase, E coli
  • UvrA protein, E coli
  • Adenosine Triphosphatases
  • Deoxyribodipyrimidine Photo-Lyase