Higher plants possess two structurally different poly(ADP-ribose) polymerases
Higher plants possess two structurally different poly(ADP-ribose) polymerases
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DOI：
10.1046/j.1365-313x.1998.00240.x
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发表时间：
1998-09-01
期刊：
影响因子：
7.2
通讯作者：
Kushnir, S
中科院分区：
文献类型：
--
作者：
Babiychuk, E;Cottrill, PB;Kushnir, S
哺乳动物细胞对许多环境应激的直接反应之一是由聚（ADP-核糖）聚合酶（PARP）催化的聚（ADP-核糖）的大量合成。大多数归因于PARP的生物学功能是从哺乳动物细胞的实验中推断出来的。在植物中，PARP的生物学可能比以前认为的更复杂和多样。在植物中发现了两种聚（ADP-核糖）聚合酶同源物，经典的含锌指聚合酶（ZAP）和结构上非经典的PARP蛋白（APP和NAP），它们缺乏特征性的N-末端锌指结构域。通过酶学和细胞学实验表明，重组APP蛋白位于细胞核中，并具有DNA依赖的聚（ADP-核糖）聚合酶活性在酵母中。通过分析表达APP和细菌β-葡萄糖醛酸酶之间的翻译基因融合的转基因烟草植物进一步证实了核定位。APP启动子在由于DNA连接酶I缺陷而预先确定死亡的细胞中转录上调。
One of the immediate reactions of the mammalian cell to many environmental stresses is a massive synthesis of poly(ADP-ribose), catalyzed by poly(ADP-ribose) polymerase (PARP). Most of the biological functions attributed to PARP are inferred from experimentation with mammalian cells. In plants, the biology of PARP may be more complicated and diverse than was previously thought. Two poly(ADP-ribose) polymerase homologues were found in plants, the classical Zn-finger-containing polymerase (ZAP) and the structurally non-classical PARP proteins (APP and NAP), which lack the characteristic N-terminal Zn-finger domain. By enzymatic and cytological experiments the recombinant APP protein was shown to be located in the nucleus and to possess DNA-dependent poly(ADP-ribose) polymerase activity in yeast. The nuclear localization was further confirmed by the analysis of transgenic tobacco plants that expressed a translational gene fusion between APP and the bacterial beta-glucuronidase, The app promoter was transcriptionally up-regulated in cells pre-determined to die because of deficiency in a DNA ligase I.