A new Drosophila ultraviolet light-damaged DNA recognition endonuclease that selectively nicks a (6-4) photoproduct site

Biochim Biophys Acta. 1998 Apr 29;1397(2):180-8. doi: 10.1016/s0167-4781(97)00215-7.

Abstract

We have previously described the purification of an ultraviolet light (UV) damage-specific DNA-binding protein from Drosophila melanogaster, designated D-DDB P1 [Nucleic Acids Res., 23 (1995) 2600-2607]. Here, we obtained highly purified D-DDB P1 from Drosophila Kc cells, and we found that D-DDB P1 is also a nuclease. D-DDB P1 can selectively bind to pyrimidine (6-4) pyrimidone photoproducts, and in the presence of Mg++, D-DDB P1 can catalyze an incision immediately on the 3' and 5' sides of the (6-4) photoproduct site.

MeSH terms

  • Animals
  • Base Sequence
  • DNA Damage*
  • DNA Repair
  • DNA, Bacterial / radiation effects*
  • DNA-Binding Proteins / genetics*
  • Drosophila Proteins*
  • Drosophila melanogaster / enzymology
  • Drosophila melanogaster / genetics*
  • Endodeoxyribonucleases / isolation & purification*
  • Molecular Sequence Data
  • Ultraviolet Rays*

Substances

  • DNA, Bacterial
  • DNA-Binding Proteins
  • Drosophila Proteins
  • Endodeoxyribonucleases
  • DdbP1 protein, Drosophila