Oei Shiao Li, Keil Claudia, Ziegler Mathias
Freie Universität Berlin, Institut für Biochemie, Germany.
Biochem Cell Biol. 2005 Jun;83(3):263-9. doi: 10.1139/o05-039.
Poly(ADP-ribose) polymerases (PARPs) catalyze the synthesis of ADP-ribose polymers and attach them to specific target proteins. To date, 6 members of this protein family in humans have been characterized. The best-known PARP, PARP-1, is located within the nucleus and has a major function in DNA repair but also in the execution of cell death pathways. Other PARP enzymes appear to carry out highly specific functions. Most prominently, the tankyrases modify telomere-binding proteins and thereby regulate telomere maintenance. Since only a single enzyme, poly(ADP-ribose) glycohydrolase (PARG), has been identified, which degrades poly(ADP-ribose), it is expected that this protein has important roles in PARP-mediated regulatory processes. This review summarizes recent observations indicating that poly(ADP-ribosylation) represents a major mechanism to regulate genomic stability both when DNA is damaged by exogenous agents and during cell division.
聚（ADP - 核糖）聚合酶（PARP）催化ADP - 核糖聚合物的合成，并将它们连接到特定的靶蛋白上。迄今为止，人类中该蛋白家族的6个成员已被鉴定。最著名的PARP，即PARP - 1，位于细胞核内，在DNA修复中起主要作用，但也参与细胞死亡途径的执行。其他PARP酶似乎执行高度特异性的功能。最突出的是，端粒酶修饰端粒结合蛋白，从而调节端粒的维持。由于仅鉴定出一种降解聚（ADP - 核糖）的酶，即聚（ADP - 核糖）糖苷水解酶（PARG），因此预计该蛋白在PARP介导的调节过程中具有重要作用。本综述总结了最近的观察结果，表明聚（ADP - 核糖基化）在外源因子损伤DNA时以及细胞分裂过程中都是调节基因组稳定性的主要机制。
