拟南芥共激活因子ALY样蛋白DIP1和DIP2与锌指聚（ADP-核糖）聚合酶的DNA结合结构域发生物理相互作用。
Arabidopsis coactivator ALY-like proteins, DIP1 and DIP2, interact physically with the DNA-binding domain of the Zn-finger poly(ADP-ribose) polymerase.
作者信息
Storozhenko S, Inzé D, Van Montagu M, Kushnir S
机构信息
Vakgroep Moleculaire Genetica, Departement Plantengenetica, Vlaams Interuniversitair Instituut voor Biotechnologie, Universiteit Gent, KL Ledeganckstraat 35, B-9000 Gent, Belgium.
出版信息
J Exp Bot. 2001 Jun;52(359):1375-80.
PMID:11432957
Abstract
Two novel homologous Arabidopsis proteins, DIP1 and DIP2, interact with the DNA-binding domain of plant poly(ADP-ribose) polymerase (PARP) in the yeast two-hybrid system and in vitro. Their homology to the transcriptional coactivator ALY suggests that plant PARP may play a role in the regulation of transcription.
摘要
在酵母双杂交系统和体外实验中，两种新的拟南芥同源蛋白DIP1和DIP2与植物多聚（ADP - 核糖）聚合酶（PARP）的DNA结合结构域相互作用。它们与转录共激活因子ALY的同源性表明，植物PARP可能在转录调控中发挥作用。
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