The C-terminal domain of p53 catalyzes DNA-renaturation and strand exchange toward annealing between intact ssDNAs and toward eliminating damaged ssDNA from duplex formation through preferential recognition of damaged DNA by a duocarmycin

Mutat Res. 1998 Dec 14;409(3):147-62. doi: 10.1016/s0921-8777(98)00052-4.

Abstract

The C-terminal domain of p53 may bind single-stranded (ss) DNA ends and catalyze renaturation of ss complementary DNA molecules, suggesting a possible direct role for p53 in DNA repair (Proc. Natl. Acad. Sci. USA, 92, 9455-9459, 1995). We found that DU-86, a duocarmycin derivative which alkylates DNA, bound ssDNA and enhanced the DNA binding activity of the p53 C-terminus. DU-86 weakened p53-mediated catalysis of complementary ssDNA renaturation. p53 C-terminus catalyzed DNA strand transfer toward annealing between intact ssDNAs and toward eliminating DU-86-damaged ssDNA from duplex formation. These results suggest that p53, via the C-terminal domain, may play a direct role in DNA repair by preferential recognization and elimination of damaged DNA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antineoplastic Agents, Alkylating / pharmacology
  • DNA Adducts / metabolism
  • DNA Damage
  • DNA Repair*
  • DNA, Single-Stranded / metabolism*
  • Duocarmycins
  • Nucleic Acid Renaturation
  • Protein Binding
  • Pyrrolidinones / pharmacology*
  • Recombinant Fusion Proteins / metabolism
  • Recombination, Genetic*
  • Tumor Suppressor Protein p53 / genetics
  • Tumor Suppressor Protein p53 / metabolism*

Substances

  • Antineoplastic Agents, Alkylating
  • DNA Adducts
  • DNA, Single-Stranded
  • DU 86
  • Duocarmycins
  • Pyrrolidinones
  • Recombinant Fusion Proteins
  • Tumor Suppressor Protein p53