Bankamp B, Horikami S M, Thompson P D, Huber M, Billeter M, Moyer S A
Department of Molecular Genetics and Microbiology, University of Florida College of Medicine, Gainesville 32610-0266, USA.
Virology. 1996 Feb 1;216(1):272-7. doi: 10.1006/viro.1996.0060.
The nucleocapsid protein (N, 525 amino acids) of measles virus plays a central role in the replication of the viral genomic RNA. Its functions require interactions with itself and with other viral components. The N protein encapsidates genomic RNA, a function reflected in its ability to self-assemble into nucleocapsid-like particles in the absence of other viral proteins. The substrate for the packaging of nascent RNA during RNA replication is a complex between the N and phosphoprotein (P). The domains on the N protein that promote binding to P protein and self-assembly have been identified utilizing a series of N protein deletions. Two noncontiguous regions, amino acids 4-188 and 304-373 of N protein, are required for the formation of the soluble N-P complex, while deletion of amino acids 189-239 did not affect N-P binding. Amino acids 240-303 appear to be necessary for the stability of the protein. The N-terminal 398 amino acids are all required for the formation of organized nucleocapsid-like particles, since deletion of the central region from amino acids 189-373 completely abolished N-N interaction, and deletion of amino acids 4-188 and 374-492 caused the formation of unstructured aggregates.
麻疹病毒的核衣壳蛋白（N，525个氨基酸）在病毒基因组RNA的复制中起核心作用。其功能需要自身以及与其他病毒成分之间的相互作用。N蛋白包裹基因组RNA，这一功能体现在其在没有其他病毒蛋白的情况下能够自组装成核衣壳样颗粒的能力上。RNA复制过程中新生RNA包装的底物是N蛋白和磷蛋白（P）之间的复合物。利用一系列N蛋白缺失突变体，已确定了N蛋白上促进与P蛋白结合和自组装的结构域。N蛋白的两个不连续区域，即氨基酸4 - 188和304 - 373，是形成可溶性N - P复合物所必需的，而缺失氨基酸189 - 239并不影响N - P结合。氨基酸240 - 303似乎对该蛋白的稳定性是必需的。N端的398个氨基酸对于形成有组织的核衣壳样颗粒都是必需的，因为从氨基酸189 - 373缺失中央区域会完全消除N - N相互作用，而缺失氨基酸4 - 188和374 - 492会导致形成无结构的聚集体。
