RecA-dependent incision of psoralen-crosslinked DNA by (A)BC excinuclease

Nucleic Acids Res. 1991 Feb 11;19(3):657-63. doi: 10.1093/nar/19.3.657.

Abstract

Previous work to elucidate the mechanism of crosslink repair by (A)BC excinuclease has shown that a psoralen-crosslinked duplex is selectively incised in the furan-side strand, while a three-stranded structure is incised in the pyrone-side strand of the crosslink. These observations support a sequential incision and recombination model for the complete error-free repair of a psoralen crosslink. The work presented here extends these findings by demonstrating that in the presence of RecA protein and a homologous DNA oligonucleotide, (A)BC excinuclease is induced to incise the pyrone-side strand of a crosslinked double-stranded plasmid molecule. This finding adds further support to the current model for error-free crosslink repair.

Publication types

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

MeSH terms

  • Base Sequence
  • Cloning, Molecular
  • Coliphages
  • Cross-Linking Reagents
  • DNA Repair*
  • DNA, Viral / genetics
  • Endodeoxyribonucleases / metabolism*
  • Escherichia coli Proteins*
  • Furocoumarins
  • In Vitro Techniques
  • Molecular Sequence Data
  • Rec A Recombinases / metabolism*

Substances

  • Cross-Linking Reagents
  • DNA, Viral
  • Escherichia coli Proteins
  • Furocoumarins
  • Rec A Recombinases
  • Endodeoxyribonucleases
  • endodeoxyribonuclease uvrABC