Site-specific characterization of the Asp- and Glu-ADP-ribosylated proteome
Site-specific characterization of the Asp- and Glu-ADP-ribosylated proteome
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DOI：
10.1038/nmeth.2603
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发表时间：
2013-10-01
期刊：
影响因子：
48
通讯作者：
Yu, Yonghao
中科院分区：
文献类型：
--
作者：
Zhang, Yajie;Wang, Jianqi;Yu, Yonghao
多聚(ADP-核糖基)是由一种称为PAPS的酶家族催化的。我们描述了一种鉴定人类天冬氨酸和谷氨酸-ADP核糖化蛋白质组的方法。我们在340个蛋白质上确定了1,048个ADADP-核糖化位点，涉及广泛的核功能；其中包括许多以前未知的PARP下游靶点，它们的ADP-核糖化对PARP抑制剂处理敏感。我们还证实了iniparib对完整细胞中PARP活性的影响可以忽略不计。
Poly(ADP-ribosyl)ation is catalyzed by a family of enzymes known as PARPs. We describe a method to characterize the human aspartic acid- and glutamic acid-ADP-ribosylated proteome. We identified 1,048 ADADP-ribosylation sites on 340 proteins involved in a wide array of nuclear functions; among these were many previously unknown PARP downstream targets whose ADP-ribosylation was sensitive to PARP inhibitor treatment. We also confirmed that iniparib had a negligible effect on PARP activity in intact cells.