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首页> 外文期刊>Journal of Molecular Biology >Modular organization of rabies virus phosphoprotein.
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Modular organization of rabies virus phosphoprotein.

机译：狂犬病毒磷酸蛋白的模块化组织。

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摘要

A phosphoprotein (P) is found in all viruses of the Mononegavirales order. These proteins form homo-oligomers, fulfil similar roles in the replication cycles of the various viruses, but differ in their length and oligomerization state. Sequence alignments reveal no sequence similarity among proteins from viruses belonging to the same family. Sequence analysis and experimental data show that phosphoproteins from viruses of the Paramyxoviridae contain structured domains alternating with intrinsically disordered regions. Here, we used predictions of disorder of secondary structure, and an analysis of sequence conservation to predict the domain organization of the phosphoprotein from Sendai virus, vesicular stomatitis virus (VSV) and rabies virus (RV P). We devised a new procedure for combining the results from multiple prediction methods and locating the boundaries between disordered regions and structured domains. To validate the proposed modular organization predicted for RV P and to confirm that the putative structured domains correspond to autonomous folding units, we used two-hybrid and biochemical approaches to characterize the properties of several fragments of RV P. We found that both central and C-terminal domains can fold in isolation, that the central domain is the oligomerization domain, and that the C-terminal domain binds to nucleocapsids. Our results suggest a conserved organization of P proteins in the Rhabdoviridae family in concatenated functional domains resembling that of the P proteins in the Paramyxoviridae family.
机译：在所有莫农氏单胞菌病毒中都发现了磷蛋白（P）。这些蛋白质形成同源寡聚体，在各种病毒的复制周期中发挥相似的作用，但长度和寡聚化状态不同。序列比对揭示属于相同家族的病毒的蛋白质之间没有序列相似性。序列分析和实验数据表明，副粘病毒科病毒的磷蛋白含有与固有无序区交替的结构域。在这里，我们使用二级结构失调的预测和序列保守性分析来预测仙台病毒，水疱性口炎病毒（VSV）和狂犬病病毒（RV P）的磷酸化蛋白的结构域。我们设计了一种新的程序，用于组合来自多种预测方法的结果，并确定无序区域和结构域之间的边界。为了验证针对RV P预测的拟议模块化组织并确认推定的结构域与自主折叠单元相对应，我们使用了两种杂交和生化方法来表征RV P的多个片段的特性。我们发现中心和C -末端结构域可以独立折叠，中央结构域是寡聚结构域，并且C-末端结构域与核衣壳结合。我们的结果表明，Rhabdoviridae家族中P蛋白的保守组织在级联功能域中类似于Paramyxoviridae家族中P蛋白的保守组织。

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