Telomere proteins POT1, TRF1 and TRF2 augment long-patch base excision repair in vitro.

@article{Miller2012TelomerePP,
  title={Telomere proteins POT1, TRF1 and TRF2 augment long-patch base excision repair in vitro.},
  author={Adam Scott Miller and Lata Balakrishnan and Noah A. Buncher and Patricia L Opresko and Robert A Bambara},
  journal={Cell cycle},
  year={2012},
  volume={11 5},
  pages={
          998-1007
        }
}
Human telomeres consist of multiple tandem hexameric repeats, each containing a guanine triplet. Guanosine-rich clusters are highly susceptible to oxidative base damage, necessitating base excision repair (BER). Previous demonstration of enhanced strand displacement synthesis by the BER component DNA polymerase β in the presence of telomere protein TRF2 suggests that telomeres employ long-patch (LP) BER. Earlier analyses in vitro showed that efficiency of BER reactions is reduced in the DNA… CONTINUE READING
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