CNRS UPR 2301, Chimie et biochimie structurales, Institut de Chimie des Substances Naturelles, Centre de recherche de Gif-sur-Yvette, 91190 Gif-sur-Yvette, France.
J Struct Biol. 2011 Apr;174(1):245-51. doi: 10.1016/j.jsb.2010.10.011. Epub 2010 Oct 23.
MED25 (ARC92/ACID1) is a 747 residues subunit specific to higher eukaryote Mediator complex, an essential component of the RNA polymerase II general transcriptional machinery. MED25 is a target of the Herpes simplex virus transactivator protein VP16. MED25 interacts with VP16 through a central MED25 PTOV (Prostate tumour overexpressed)/ACID (Activator interacting domain) domain of unknown structure. As a first step towards understanding the mechanism of recruitment of transactivation domains by MED25, we report here the NMR structure of the MED25 ACID domain. The domain architecture consists of a closed β-barrel with seven strands (Β1-Β7) and three α-helices (H1-H3), an architecture showing similarities to that of the SPOC (Spen paralog and ortholog C-terminal domain) domain-like superfamily. Preliminary NMR chemical shift mapping showed that VP16 H2 (VP16C) interacts with MED25 ACID through one face of the β-barrel, defined by strands B4-B7-B6.
MED25(ARC92/ACID1)是一个 747 个残基的亚基,特异性存在于高等真核生物中介体复合物中,是 RNA 聚合酶 II 一般转录机制的必需组成部分。MED25 是单纯疱疹病毒转录激活蛋白 VP16 的靶标。MED25 通过中央 MED25 PTOV(前列腺肿瘤过表达)/ACID(激活剂相互作用结构域)结构域与 VP16 相互作用,该结构域的结构未知。为了深入了解 MED25 募集转录激活结构域的机制,我们在此报告 MED25 ACID 结构域的 NMR 结构。该结构域的架构由一个封闭的β桶组成,包含七个β链(Β1-Β7)和三个α螺旋(H1-H3),其结构与 SPOC(Spen 同源和异源 C 端结构域)结构域样超家族的结构相似。初步的 NMR 化学位移映射显示,VP16 H2(VP16C)通过β桶的一个面与 MED25 ACID 相互作用,该面由β链 B4-B7-B6 定义。