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

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.
Mesh Terms:
Adenosine Diphosphate Ribose, Amino Acid Sequence, Animals, Ankyrins, Benzamides, Catalytic Domain, DNA, DNA-Binding Proteins, Enzyme Inhibitors, Fluorescent Antibody Technique, Indirect, Humans, Molecular Sequence Data, NAD, Poly(ADP-ribose) Polymerases, Protein Structure, Secondary, Recombinant Proteins, Repetitive Sequences, Amino Acid, Sequence Alignment, Sequence Homology, Amino Acid, Tankyrases, Telomere, Telomeric Repeat Binding Protein 1
Science
Date: Nov. 20, 1998
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