Karlin David, Ferron François, Canard Bruno, Longhi Sonia
Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS et Université Aix-Marseille I et II, ESIL, Campus de Luminy, 13288 Marseille Cedex 09, France.
J Gen Virol. 2003 Dec;84(Pt 12):3239-3252. doi: 10.1099/vir.0.19451-0.
The existence and extent of disorder within the replicative complex (N, P and the polymerase, L) of Paramyxovirinae were investigated, drawing on the discovery that the N-terminal moiety of the phosphoprotein (P) and the C-terminal moiety of the nucleoprotein (N) of measles virus are intrinsically unstructured. We show that intrinsic disorder is a widespread property within Paramyxovirinae N and P, using a combination of different computational approaches relying on different physico-chemical concepts. Notably, experimental support that has often gone unnoticed for most of the predictions has been found in the literature. Identification of disordered regions allows the unveiling of a common organization in all Paramyxovirinae P, which are composed of six modules defined on the basis of structure or sequence conservation. The possible functional significance of intrinsic disorder is discussed in the light of experimental data, which show that unstructured regions of P and N are involved in numerous interactions with several protein and protein-RNA partners. This study provides a contribution to the rather poorly investigated field of intrinsically disordered proteins and helps in targeting protein domains for structural studies.
鉴于发现麻疹病毒磷蛋白（P）的N端部分和核蛋白（N）的C端部分本质上是无序的，我们对副粘病毒亚科复制复合体（N、P和聚合酶L）内无序的存在情况和程度进行了研究。我们使用了基于不同物理化学概念的多种计算方法，结果表明，内在无序是副粘病毒亚科N和P的普遍特性。值得注意的是，在文献中发现了对大多数预测常常未被注意到的实验支持。无序区域的鉴定揭示了所有副粘病毒亚科P的共同组织方式，这些P由基于结构或序列保守性定义的六个模块组成。根据实验数据讨论了内在无序可能的功能意义，实验数据表明P和N的无序区域参与了与多种蛋白质及蛋白质-RNA伙伴的众多相互作用。这项研究为内在无序蛋白质这一研究较少的领域做出了贡献，并有助于确定用于结构研究的蛋白质结构域。
