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Tankyrase, a Poly(ADP-Ribose) Polymerase at Human Telomeres

1998; American Association for the Advancement of Science; Volume: 282; Issue: 5393 Linguagem: Inglês

10.1126/science.282.5393.1484

1095-9203

Susan Smith, Izabela Giriat, Anja Schmitt, Titia de Lange,

DNA Repair Mechanisms

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.