LifeB | Laboratory of interaction and function of essential biomolecules


Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas RAP1 restores it

We explain how telomeric proteins TRF2 and RAP1 modify BLM helicase activity and processing of displacement loop (D-loop) during replication of telomeres.  We addressed the role of the basic domain (B-domain) of TRF2 in the stabilization of DNA loops.


  • The B-domain of TRF2 stabilizes of the D-loop and diminishes DNA unwinding
  • The B- domain upon binding to DNA forms a rigid complex
  • Rap1 complexation with TRF2 restores D-loop susceptibility to unwinding

We suggested a mechanism for how the B-domain stabilizes D-loop and how RAP1 reverts the stabilization.


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
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