组蛋白尾巴促进核小体中PARP1依赖性的结构重排。
Histone Tails Promote PARP1-Dependent Structural Rearrangements in Nucleosomes.
作者信息
Maluchenko N V, Sultanov D S, Kotova E Yu, Kirpichnikov M P, Studitsky V M, Feofanov A V
机构信息
Moscow State University, 119234, Moscow, Russia.
Fox Chase Cancer Center, Philadelphia, USA.
出版信息
Dokl Biochem Biophys. 2019 Nov;489(1):377-379. doi: 10.1134/S1607672919060061. Epub 2020 Mar 4.
PARP 1 alters the wrapping of nucleosomal DNA on the histone octamer, thereby modulating the accessibility of different genome sites to nuclear protein factors. Here, we show that non-structured histone tails are involved in the PARP1-induced structural rearrangements in nucleosomes, facilitate and stabilize them, but do not affect the enzymatic activity of PARP1.
聚（ADP - 核糖）聚合酶1（PARP 1）改变核小体DNA在组蛋白八聚体上的缠绕方式，从而调节不同基因组位点对核蛋白因子的可及性。在此，我们表明非结构化的组蛋白尾巴参与了PARP1诱导的核小体结构重排，促进并稳定这些重排，但不影响PARP1的酶活性。
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