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

Huawei Xin, Dan Liu, Ma Wan, Amin Safari, Hyeung Kim, Wen Sun, Matthew S. O’Connor and Zhou Songyang ()
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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

Nature, 2007, vol. 445, issue 7127, 559-562

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.

Date: 2007
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DOI: 10.1038/nature05469

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