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

被引：869
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
收藏
页码：1484 / 1487
页数：4
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