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

被引：866

作者：

Smith, S ^{[1
]}

Giriat, I ^{[1
]}

Schmitt, A ^{[1
]}

de Lange, T ^{[1
]}

机构：

[1] Rockefeller Univ, New York, NY 10021 USA

来源：

SCIENCE | 1998年 / 282卷 / 5393期

关键词：

D O I：

10.1126/science.282.5393.1484

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 accepters 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.

引用

页码：1484 / 1487

页数：4

共 20 条

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