@article{56,
  author = {Zala Sekne and George Ghanim and Anne-Marie van Roon and Thi Nguyen},
  title = {Structural basis of human telomerase recruitment by TPP1-POT1.},
  abstract = {<p>Telomerase maintains genome stability by extending the 3{\textquoteright} telomeric repeats at eukaryotic chromosome ends, thereby counterbalancing progressive loss caused by incomplete genome replication. In mammals, telomerase recruitment to telomeres is mediated by TPP1, which assembles as a heterodimer with POT1. We report structures of DNA-bound telomerase in complex with TPP1 and with TPP1-POT1 at 3.2- and 3.9-angstrom resolution, respectively. Our structures define interactions between telomerase and TPP1-POT1 that are crucial for telomerase recruitment to telomeres. The presence of TPP1-POT1 stabilizes the DNA, revealing an unexpected path by which DNA exits the telomerase active site and a DNA anchor site on telomerase that is important for telomerase processivity. Our findings rationalize extensive prior genetic and biochemical findings and provide a framework for future mechanistic work on telomerase regulation.</p>},
  year = {2022},
  journal = {Science (New York, N.Y.)},
  volume = {375},
  pages = {1173-1176},
  month = {03/2022},
  issn = {1095-9203},
  doi = {10.1126/science.abn6840},
  language = {eng},
}