The telomeric Cdc13 protein interacts directly with the telomerase subunit Est1 to bring it to telomeric DNA ends in vitro.

@article{Wu2011TheTC,
  title={The telomeric Cdc13 protein interacts directly with the telomerase subunit Est1 to bring it to telomeric DNA ends in vitro.},
  author={Yun Wu and Virginia A. Zakian},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2011},
  volume={108 51},
  pages={20362-9}
}
In Saccharomyces cerevisiae, a Cdc13-Est1 interaction is proposed to mediate recruitment of telomerase to DNA ends. Here we provide unique in vitro evidence for this model by demonstrating a direct interaction between purified Cdc13 and Est1. The Cdc13-Est1 interaction is specific and requires the in vivo defined Cdc13 recruitment domain. Moreover, in the absence of this interaction, Est1 is excluded from telomeric single-stranded (ss)DNA. The apparent association constand (K(d)) between Est1… CONTINUE READING
Recent Discussions
This paper has been referenced on Twitter 2 times over the past 90 days. VIEW TWEETS
24 Citations
64 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 24 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 64 references

Structural bases of dimerization of yeast telomere protein Cdc 13 and its interaction with the catalytic subunit of DNA polymerase α

  • J Sun
  • Cell Res
  • 2011

Structural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase

  • J Sun
  • α. Cell Res
  • 2011

Reduced Rif2 and lack of Mec1 target short telomeres for elongation rather than double-strand break repair

  • JS McGee
  • Nat Struct Mol Biol
  • 2010

Similar Papers

Loading similar papers…