LifeB | Laboratory of interaction and function of essential biomolecules


Human Rap1 modulates TRF2 attraction to telomeric DNA

Our quantitative functional studies explain how telomeric proteins cooperate in order to selectively recognize human telomeric DNA. We investigated human Rap1–TRF2–DNA interactions by quantitative approaches. Our findings could be applied on all proteins that recognize DNA selectively and preserve genome stability.


  • Rap1 reduces DNA duplex binding of TRF2
  • Rap1 improves TRF2 selectivity for telomeric DNA
    by reduction of non-specific electrostatic interactions
  • Rap1 induces a partial release of TRF2 from telomeric DNA duplex

We suggested a possible mechanism of how Rap1 affects the recognition of telomeric DNA by TRF2


Contributions of the TEL-patch Amino Acid Cluster on TPP1 to Telomeric DNA Synthesis by Human Telomerase

These quantitative observations describe how the TEL-patch part of telomeric protein TPP1 stabilizes telomerase on telomeric DNA and explains its contributions to telomerase recruitment and action.


  • The TEL-patch on TPP1 promotes telomerase translocation
  • The TEL-patch of TPP1 reduces telomerase dissociation from DNA
  • We developed an in vitro assay for telomerase recruitment to DNA
  • Telomerase interacts with TPP1 to preferentially bind and extend telomeric DNA