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Interaction of human Ku70 with TRF2
Author(s) -
Song Kyuyoung,
Jung Donghae,
Jung Yusun,
Lee Seong-Gene,
Lee Inchul
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01958-x
Subject(s) - ku70 , telomere , dna , transfection , yeast , fusion protein , biology , microbiology and biotechnology , ku80 , saccharomyces cerevisiae , dna repair , chemistry , recombinant dna , genetics , dna binding protein , gene , transcription factor
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.