Ku acts in a unique way at the mammalian telomere to prevent end joining.

@article{Hsu2000KuAI,
  title={Ku acts in a unique way at the mammalian telomere to prevent end joining.},
  author={Hsin Ling Hsu and David A Gilley and Sanjeev Galande and Manoor Prakash Hande and Beth Allen and Seung Heuk Kim and Gloria C. Li and Judith Campisi and Terumi Kohwi-Shigematsu and David J. Chen},
  journal={Genes & development},
  year={2000},
  volume={14 22},
  pages={2807-12}
}
Telomeres are specialized DNA/protein structures that act as protective caps to prevent end fusion events and to distinguish the chromosome ends from double-strand breaks. We report that TRF1 and Ku form a complex at the telomere. The Ku and TRF1 complex is a specific high-affinity interaction, as demonstrated by several in vitro methods, and exists in human cells as determined by coimmunoprecipitation experiments. Ku does not bind telomeric DNA directly but localizes to telomeric repeats via… CONTINUE READING
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