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首页> 外文期刊>EMBO Journal >The Mdm2 RING domain C-terminus is required for supramolecular assembly and ubiquitin ligase activity
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The Mdm2 RING domain C-terminus is required for supramolecular assembly and ubiquitin ligase activity

机译：Mdm2环域需要糖超分子组装和泛素连接酶活动

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摘要

Mdm2, a key negative regulator of the p53 tumor suppressor, is a RING-type E3 ubiquitin ligase. The Mdm2 RING domain can be biochemically fractionated into two discrete species, one of which exists as higher order oligomers that are visible by electron microscopy, whereas the other is a monomer. Both fractions are ATP binding and E3 ligase activity competent, although the oligomeric fraction exhibits lower dependence on the E2 component of ubiquitin polymerization reactions. The extreme C-terminal five amino acids of Mdm2 are essential for E3 ligase activity in vivo and in vitro, as well as for oligomeric assembly of the protein. A single residue (phenylalanine 490) in that sequence is critical for both properties. Interestingly, the C-terminus of the Mdm2 homologue, MdmX (itself inert as an E3 ligase), can fully substitute for the equivalent segment of Mdm2 and restore its E3 activity. We further show that the Mdm2 C-terminus is involved in intramolecular interactions and can set up a platform for direct protein-protein interactions with the E2.
机译：Mdm2、p53肿瘤的关键-调节器抑制器,是一个环形E3泛素连接酶。Mdm2环域可以生化反应分离成两个离散的物种之一这存在高阶低聚物,是吗通过电子显微镜可见的,而另一个是一个单体。E3连接酶的活动能力,虽然低聚物的部分展品的依赖降低泛素聚合的E2组件反应。酸的E3连接酶Mdm2是必不可少的活动在体内和体外,以及寡聚蛋白质的组装。残渣(苯丙氨酸490)序列这两个属性的关键。Mdm2同系物的糖基,MdmX(本身惰性是E3连接酶),可以完全替代段相当于Mdm2和恢复它的E3活动。糖基参与分子内直接交互,可以建立一个平台与E2蛋白质-蛋白质之间的关系。

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