Tankyrase, a poly(ADP-ribose) polymerase at human telomeres
Tankyrase, a poly(ADP-ribose) polymerase at human telomeres
复制标题
DOI：
10.1126/science.282.5393.1484
复制
发表时间：
1998-11-20
期刊：
影响因子：
56.9
通讯作者：
de Lange, T
中科院分区：
文献类型：
--
作者：
Smith, S;Giriat, I;de Lange, T
端锚聚合酶是一种与锚蛋白和聚（二磷酸腺苷-核糖）聚合酶（PARP）催化结构域具有同源性的蛋白质，已被鉴定并定位于人类端粒。端锚聚合酶与端粒蛋白TRF 1（端粒重复序列结合因子-1）结合，TRF 1是端粒长度维持的负调节因子。与锚蛋白一样，端锚聚合酶在负责与TRF 1相互作用的结构域中含有24个锚蛋白重复序列。发现重组端锚聚合酶在体外具有PARP活性，TRF 1和端锚聚合酶都作为腺苷二磷酸（ADP）-核糖基化的受体发挥作用。TRF 1的ADP-核糖基化降低了其在体外与端粒DNA结合的能力，表明人类细胞中端粒的功能受聚（ADP-核糖基）化的调节。
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.