[Investigation of the interaction of repair DNA polymerase beta and autonomous 3' --> 5'-exonucleases TREX1 and TREX2]

Izv Akad Nauk Ser Biol. 2010 Sep-Oct;(5):547-53.
[Article in Russian]

Abstract

The possibility of interaction of recombinant proteins of human repair DNA polymerase beta with proofreading 3' --> 5'-exonucleases TREX1 and TREX2 was investigated in vitro for the first time. The results of gel filtration analysis show the formation of a complex between 3' --> 5' -exonucleases mTREX1 and hTREX2 and DNA polymerase beta. DNA polymerase activity is shown to increase four-fold in the presence of 3' --> 5'-exonuclease TREX2. The experiments with the use of immunodot and Western blot assays on the binding of DNA-polymerase beta with 3' --> 5'-exonucleases TREX1 and TREX2 immobilized on a nitrocellulose membrane provided additional evidence on the direct association of the above proteins in complexes.

MeSH terms

  • Animals
  • DNA Polymerase beta / chemistry*
  • DNA Polymerase beta / genetics
  • DNA Repair Enzymes / chemistry*
  • DNA Repair Enzymes / genetics
  • DNA Repair*
  • Electrophoresis, Agar Gel
  • Escherichia coli / genetics
  • Exodeoxyribonucleases / chemistry*
  • Exodeoxyribonucleases / genetics
  • Humans
  • Immunoblotting
  • Mice
  • Phosphoproteins / chemistry*
  • Phosphoproteins / genetics
  • Protein Binding
  • Protein Interaction Mapping
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics

Substances

  • Phosphoproteins
  • Recombinant Proteins
  • DNA Polymerase beta
  • Exodeoxyribonucleases
  • TREX2 protein, human
  • three prime repair exonuclease 1
  • DNA Repair Enzymes