The basic N-terminal domain of TRF2 limits recombination endonuclease action at human telomeres.

@article{SaintLger2014TheBN,
  title={The basic N-terminal domain of TRF2 limits recombination endonuclease action at human telomeres.},
  author={Ad{\'e}la{\"i}de Saint-L{\'e}ger and M{\'e}lanie Koelblen and Livia Civitelli and Amadou A. Bah and Nadir Djerbi and Marie-Jos{\`e}phe Giraud-Panis and Arturo Londo{\~n}o-Vallejo and Fiorentina Ascenzioni and Eric Gilson},
  journal={Cell cycle},
  year={2014},
  volume={13 15},
  pages={2469-74}
}
The stability of mammalian telomeres depends upon TRF2, which prevents inappropriate repair and checkpoint activation. By using a plasmid integration assay in yeasts carrying humanized telomeres, we demonstrated that TRF2 possesses the intrinsic property to both stimulate initial homologous recombination events and to prevent their resolution via its basic N-terminal domain. In human cells, we further showed that this TRF2 domain prevents telomere shortening mediated by the resolvase-associated… CONTINUE READING
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