Fouchier R A, Meyer B E, Simon J H, Fischer U, Albright A V, González-Scarano F, Malim M H
Howard Hughes Medical Institute, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6148, USA.
J Virol. 1998 Jul;72(7):6004-13. doi: 10.1128/JVI.72.7.6004-6013.1998.
The Vpr protein of human immunodeficiency virus type 1 (HIV-1) performs a number of functions that are associated with the nucleus. Vpr enhances the nuclear import of postentry viral nucleoprotein complexes, arrests proliferating cells in the G2 phase of the cell cycle, and acts as a modest transcriptional activator. For this paper, we have investigated the nuclear import of Vpr. Although Vpr does not encode a sequence that is recognizable as a nuclear localization signal (NLS), Vpr functions as a transferable NLS both in somatic cells and in Xenopus laevis oocytes. In certain contexts, Vpr also mediates substantial accumulation at the nuclear envelope and, in particular, at nuclear pore complexes (NPCs). Consistent with this, Vpr is shown to interact specifically with nucleoporin phenylalanine-glycine (FG)-repeat regions. These findings not only demonstrate that Vpr harbors a bona fide NLS but also raise the possibility that one (or more) of Vpr's functions may take place at the NPC.
人类免疫缺陷病毒1型（HIV-1）的Vpr蛋白具有多种与细胞核相关的功能。Vpr增强了病毒进入后核蛋白复合物的核输入，使增殖细胞停滞在细胞周期的G2期，并作为一种适度的转录激活因子。在本文中，我们研究了Vpr的核输入。尽管Vpr没有编码可识别为核定位信号（NLS）的序列，但Vpr在体细胞和非洲爪蟾卵母细胞中均作为可转移的NLS发挥作用。在某些情况下，Vpr还介导在核膜尤其是核孔复合体（NPC）处大量积聚。与此一致的是，Vpr被证明与核孔蛋白苯丙氨酸-甘氨酸（FG）重复区域特异性相互作用。这些发现不仅证明Vpr含有真正的NLS，还增加了Vpr的一种（或多种）功能可能在NPC处发生的可能性。
