AP-site cleavage activity of tyrosyl-DNA phosphodiesterase 1

FEBS Lett. 2011 Feb 18;585(4):683-6. doi: 10.1016/j.febslet.2011.01.032. Epub 2011 Jan 26.

Abstract

APE-independent base excision repair (BER) pathway plays an important role in the regulation of DNA repair mechanisms. In this study it has been found that recently discovered tyrosyl-DNA phosphodiesterase 1 (Tdp1) catalyzes the AP site cleavage reaction to generate breaks with the 3'- and 5'-phosphate termini. The removal of the 3'-phosphate is performed by polynucleotide kinase phosphatase (PNKP). Tdp1 is known to interact stably with BER proteins: DNA polymerase beta (Pol β), XRCC1, PARP1 and DNA ligase III. The data suggest a role of Tdp1 in the new APE-independent BER pathway in mammals.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • DNA Glycosylases / metabolism
  • DNA Repair Enzymes / metabolism
  • DNA Repair*
  • DNA-(Apurinic or Apyrimidinic Site) Lyase / metabolism
  • Humans
  • Phosphoric Diester Hydrolases / genetics
  • Phosphoric Diester Hydrolases / metabolism*
  • Phosphotransferases (Alcohol Group Acceptor) / metabolism
  • Polynucleotides / chemistry
  • Polynucleotides / metabolism*
  • Recombinant Proteins
  • Substrate Specificity

Substances

  • Polynucleotides
  • Recombinant Proteins
  • PNKP protein, human
  • Phosphotransferases (Alcohol Group Acceptor)
  • Phosphoric Diester Hydrolases
  • TDP1 protein, human
  • DNA Glycosylases
  • NEIL1 protein, human
  • APEX1 protein, human
  • DNA-(Apurinic or Apyrimidinic Site) Lyase
  • DNA Repair Enzymes