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首页> 外文期刊>Molecular and Cellular Biology >Formation of vesicular stomatitis virus nucleocapsid from cytoskeletal framework-bound N protein: possible model for structure assembly.
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Formation of vesicular stomatitis virus nucleocapsid from cytoskeletal framework-bound N protein: possible model for structure assembly.

机译：由细胞骨架框架结合的N蛋白形成水泡性口腔炎病毒核衣壳：结构装配的可能模型。

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The pathway of vesicular stomatitis virus N protein from synthesis to assembly into capsids was studied by use of detergent extraction of infected HeLa cells together with protein cross-linking. One half of the newly synthesized N protein was extracted with the soluble cell proteins and, when cross-linked, never formed the N-N dimer characteristic of mature nucleocapsids. In contrast, the cytoskeleton-bound N protein first showed a diffuse spectrum of protein-protein cross-links but, after a lag of 40 min, assumed the cross-link pattern of N protein in nucleocapsids. The efficiency of forming N-N cross-linked dimers is the same for N protein on the skeleton as in nucleocapsids derived from mature virus, suggesting very similar configurations. However, the N protein bound on the skeletal framework formed several additional cross-links that were not found in mature virus and were apparently formed to cellular proteins estimated to be ca. approximately 46,000 and 60,000 in molecular weight.
机译：通过使用去污剂提取感染的HeLa细胞并进行蛋白交联，研究了水泡性口炎病毒N蛋白从合成到组装成衣壳的途径。新合成的N蛋白的一半是用可溶性细胞蛋白提取的，当交联时，它从未形成成熟核衣壳的N-N二聚体特征。相反，细胞骨架结合的N蛋白首先显示出蛋白质-蛋白质交联的扩散光谱，但是在40分钟的滞后之后，假定了N蛋白质在核衣壳中的交联模式。对于骨架上的N蛋白而言，形成N-N交联二聚体的效率与衍生自成熟病毒的核衣壳中的N相同，表明其构型非常相似。但是，结合在骨骼骨架上的N蛋白形成了一些其他的交联键，这些交联键在成熟病毒中没有发现，并且显然形成了估计为ca的细胞蛋白。分子量约为46,000和60,000。

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