Chatterjee P K, Cervera M M, Penman S
Mol Cell Biol. 1984 Oct;4(10):2231-4. doi: 10.1128/mcb.4.10.2231-2234.1984.
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.
通过使用去污剂提取感染的HeLa细胞并结合蛋白质交联技术，研究了水泡性口炎病毒N蛋白从合成到组装入衣壳的途径。新合成的N蛋白有一半与可溶性细胞蛋白一起被提取出来，当进行交联时，从未形成成熟核衣壳特有的N-N二聚体。相比之下，与细胞骨架结合的N蛋白首先显示出蛋白质-蛋白质交联的弥散谱，但在延迟40分钟后，呈现出核衣壳中N蛋白的交联模式。骨架上的N蛋白形成N-N交联二聚体的效率与来自成熟病毒的核衣壳中的N蛋白相同，这表明它们的构象非常相似。然而，结合在骨架框架上的N蛋白形成了一些在成熟病毒中未发现的额外交联，这些交联显然是与估计分子量约为46,000和60,000的细胞蛋白形成的。
