Morbillivirus nucleoprotein possesses a novel nuclear localization signal and a CRM1-independent nuclear export signal
Morbillivirus nucleoprotein possesses a novel nuclear localization signal and a CRM1-independent nuclear export signal
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DOI：
10.1016/j.virol.2006.04.013
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发表时间：
2006-08-15
期刊：
影响因子：
3.7
通讯作者：
Kai, Chieko
中科院分区：
文献类型：
--
作者：
Sato, Hiroki;Masuda, Munemitsu;Kai, Chieko
麻疹病毒属于单负加病毒目，在宿主细胞的细胞质中复制其RNA基因组。然而，它们也在感染的细胞中形成特征性的核内包涵体，由核蛋白（N）组成。为分析犬瘟热病毒（CDV）N蛋白的核质转运机制，通过对N蛋白进行缺失突变和丙氨酸取代，研究了N蛋白的核定位（NLS）和核输出（内斯）信号。NLS在第70-77位具有新的富含亮氨酸/异亮氨酸的基序（TGILISIL），而内斯在第4-11位由富含亮氨酸的基序（LLRSLTLF）组成。本文还对麻疹病毒（MV）和牛瘟病毒（RPV）的N蛋白进行了NLS和内斯分析。CDV-N蛋白的NLS与MV-N蛋白的NLS相同，而MV-N蛋白的内斯位于C端。R-PV-N蛋白的内斯也位于与CDV-N蛋白相同的位置，而NLS基序不仅存在于与CDV-N蛋白相同的位点，而且还存在于其他位点。有趣的是，所有这些N蛋白的核输出似乎通过CRM 1独立途径进行。(c)2006年爱思唯尔公司All rights reserved.
Morbilliviruses, which belong to the Mononegavirales, replicate its RNA genome in the cytoplasm of the host cell. However, they also form characteristic intranuclear inclusion bodies, consisting of nucleoprotein (N), in infected cells. To analyze the mechanisms of nucleocytoplasmic transport of N protein, we characterized the nuclear localization (NLS) and nuclear export (NES) signals of canine distemper virus (CDV) N protein by deletion mutation and alanine substitution of the protein. The NLS has a novel leucine/isoleucine-rich motif (TGILISIL) at positions 70-77, whereas the NES is composed of a leucine-rich motif (LLRSLTLF) at positions 4-11. The NLS and NES of the N proteins of other morbilliviruses, that is, measles virus (MV) and rinderpest virus (RPV), were also analyzed. The NLS of CDV-N protein is conserved at the same position in MV-N protein, whereas the NES of MV-N protein is located in the C-tenninal region. The NES of R-PV-N protein is also located at the same position as CDV-N protein, whereas the NLS motif is present not only at the same locus as CDV-N protein but also at other sites. Interestingly, the nuclear export of all these N proteins appears to proceed via a CRM1-independent pathway. (c) 2006 Elsevier Inc. All rights reserved.