Interaction of human Ku70 with TRF2

FEBS Lett. 2000 Sep 8;481(1):81-5. doi: 10.1016/s0014-5793(00)01958-x.

Abstract

Ku, a heterodimer of 70- and 80-kDa subunits, plays a general role in the metabolism of DNA ends in eukaryotic cells, including double-strand DNA break repair, V(D)J recombination, and maintenance of telomeres. We have utilized the yeast two-hybrid system to identify Ku70-interacting proteins other than Ku80. Two reactive clones were found to encode the dimerization domain of TRF2, a mammalian telomeric protein that binds to duplex TTAGGG repeats at chromosome ends. This interaction was confirmed using bacterial fusion proteins and co-immunoprecipitations from eukaryotic cells overexpressing TRF2. The transfected TFR2 colocalized with Ku70.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antigens, Nuclear*
  • Base Sequence
  • Binding Sites
  • COS Cells
  • DNA Helicases*
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Dimerization
  • Fluorescent Antibody Technique
  • Humans
  • Ku Autoantigen
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Precipitin Tests
  • Protein Binding
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / metabolism
  • Repetitive Sequences, Amino Acid
  • Saccharomyces cerevisiae Proteins*
  • Telomere / genetics
  • Telomere / metabolism
  • Telomeric Repeat Binding Protein 2
  • Transfection
  • Two-Hybrid System Techniques

Substances

  • Antigens, Nuclear
  • DNA-Binding Proteins
  • Nuclear Proteins
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae Proteins
  • Telomeric Repeat Binding Protein 2
  • high affinity DNA-binding factor, S cerevisiae
  • DNA Helicases
  • XRCC5 protein, human
  • Xrcc6 protein, human
  • Ku Autoantigen