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    Science. 1998 Nov 20;282(5393):1484-7.

    Tankyrase, a poly(ADP-ribose) polymerase at human telomeres.

    Smith S, Giriat I, Schmitt A, de Lange T.

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    The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.

    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.

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    PMID:
    9822378
    [PubMed - indexed for MEDLINE]

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