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TPP1 is a homologue of ciliate TEBP-β and interacts with POT1 to recruit telomerase

Author

Listed:
  • Huawei Xin

    (Baylor College of Medicine)

  • Dan Liu

    (Baylor College of Medicine)

  • Ma Wan

    (Baylor College of Medicine)

  • Amin Safari

    (Baylor College of Medicine)

  • Hyeung Kim

    (Baylor College of Medicine)

  • Wen Sun

    (Baylor College of Medicine)

  • Matthew S. O’Connor

    (Baylor College of Medicine)

  • Zhou Songyang

    (Baylor College of Medicine)

Abstract

End of the line Telomeres, the tips of linear chromosomes, are protected by various binding proteins including, in ciliates, the telomere-binding complex TBPα/β. Humans have a TBPα homologue, POT1, but TBPβ has not been found outside of ciliates. Now two groups have separately identified the elusive TBPβ homologue in humans as TPP1. Surprisingly, when the POT1–TPP1 complex binds to telomeric DNA, it does not inhibit telomerase activity, as other telomere binding proteins do. Instead, it stimulates telomerase activity and processivity, the rate of nucleotide addition by the core telomerase enzyme.

Suggested Citation

  • Huawei Xin & Dan Liu & Ma Wan & Amin Safari & Hyeung Kim & Wen Sun & Matthew S. O’Connor & Zhou Songyang, 2007. "TPP1 is a homologue of ciliate TEBP-β and interacts with POT1 to recruit telomerase," Nature, Nature, vol. 445(7127), pages 559-562, February.
    • Handle: RePEc:nat:nature:v:445:y:2007:i:7127:d:10.1038_nature05469
    DOI: 10.1038/nature05469
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    Cited by:

    1. Qadar Pasha & Manjari Rain & Sana Tasnim & Hema Kanipakam & Tashi Thinlas & Ghulam Mohammad, 2023. "The Telomere-Telomerase System Is Detrimental to Health at High-Altitude," IJERPH, MDPI, vol. 20(3), pages 1-22, January.

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