Pedraza-Reyes M, Alvarez-Gonzalez R
Department of Microbiology and Immunology, Texas College of Osteopathic Medicine, Fort Worth 76107-2690.
FEBS Lett. 1990 Dec 17;277(1-2):88-92. doi: 10.1016/0014-5793(90)80815-z.
It has previously been shown that the levels of poly(ADP-ribose)polymerase and polymers of ADP-ribose that co-purify with the nuclear matrix in regenerating liver fluctuate with the levels of in vivo DNA replication [(1988) FEBS Lett. 236, 362-366]. We have now electrophoretically identified lamins A and C, and poly(ADP-ribose)polymerase as the main protein targets for poly(ADP-ribosyl)ation in isolated nuclear matrices from adult rat liver. The identification of these protein acceptors was facilitated by the utilization of 32P-radiolabeled 3'-deoxyNAD as a substrate for nuclear matrix extracts in the presence of exogenously added DNA-dependent poly(ADP-ribose)polymerase from calf thymus. The extent of protein modification was time- and substrate concentration-dependent. These results are consistent with the hypothesis that the poly(ADP-ribose) modification of the lamins A and C and poly(ADP-ribose)polymerase are important to modulate chromatin-nuclear matrix interactions in rat liver.
先前的研究表明，在再生肝脏中，与核基质共纯化的聚（ADP-核糖）聚合酶和ADP-核糖聚合物的水平会随着体内DNA复制水平的波动而波动[（1988年）《欧洲生物化学学会联合会快报》236, 362 - 366]。我们现在已经通过电泳鉴定出，在成年大鼠肝脏分离的核基质中，核纤层蛋白A和C以及聚（ADP-核糖）聚合酶是聚（ADP-核糖基）化的主要蛋白质靶点。通过使用32P放射性标记的3'-脱氧NAD作为核基质提取物的底物，并在存在从牛胸腺中提取的外源DNA依赖性聚（ADP-核糖）聚合酶的情况下，促进了这些蛋白质受体的鉴定。蛋白质修饰的程度取决于时间和底物浓度。这些结果与以下假设一致，即核纤层蛋白A和C以及聚（ADP-核糖）聚合酶的聚（ADP-核糖）修饰对于调节大鼠肝脏中的染色质 - 核基质相互作用很重要。
