Tankyrase, a poly(ADP-ribose) polymerase at human telomeres
- PMID: 9822378
- DOI: 10.1126/science.282.5393.1484
Tankyrase, a poly(ADP-ribose) polymerase at human telomeres
Abstract
Tankyrase, a protein with homology to ankyrins and to the catalytic domain of poly(adenosine diphosphate-ribose) polymerase (PARP), was identified and localized to human telomeres. Tankyrase binds to the telomeric protein TRF1 (telomeric repeat binding factor-1), a negative regulator of telomere length maintenance. Like ankyrins, tankyrase contains 24 ankyrin repeats in a domain responsible for its interaction with TRF1. Recombinant tankyrase was found to have PARP activity in vitro, with both TRF1 and tankyrase functioning as acceptors for adenosine diphosphate (ADP)-ribosylation. ADP-ribosylation of TRF1 diminished its ability to bind to telomeric DNA in vitro, suggesting that telomere function in human cells is regulated by poly(ADP-ribosyl)ation.
Comment on
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A possible new partner for telomerase.Science. 1998 Nov 20;282(5393):1395, 1397. doi: 10.1126/science.282.5393.1395. Science. 1998. PMID: 9867637 No abstract available.
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