Domains of the measles virus N protein required for binding to P protein and self-assembly
Domains of the measles virus N protein required for binding to P protein and self-assembly
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DOI：
10.1006/viro.1996.0060
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发表时间：
1996-02-01
期刊：
影响因子：
3.7
通讯作者：
Moyer, SA
中科院分区：
文献类型：
--
作者：
Bankamp, B;Horikami, SM;Moyer, SA
麻疹病毒的核衣壳蛋白(N，525个氨基酸)在病毒基因组RNA的复制中起着核心作用。它的功能需要与自身以及与其他病毒成分相互作用。N蛋白包裹基因组RNA，这一功能反映在它在没有其他病毒蛋白的情况下自组装成核衣壳样颗粒的能力。在RNA复制过程中，包装新生RNA的底物是N和磷蛋白(P)之间的复合体。N蛋白上促进与P蛋白结合和自我组装的结构域已经通过一系列N蛋白缺失得到了鉴定。N蛋白的4-188位氨基酸和304-373位氨基酸是形成可溶性N-P复合体所必需的两个非邻接区，189-239位氨基酸的缺失不影响N-P的结合。氨基酸240-303似乎是蛋白质稳定所必需的。N末端的398个氨基酸都是形成有组织的核衣壳样颗粒所必需的，因为189-373氨基酸的中心区的缺失完全取消了N-N相互作用，而4-188和374-492氨基酸的缺失导致了无结构聚集体的形成。(C)1996年学术出版社。
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. (C) 1996 Academic Press, Inc.