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J Virol, July 1998, p. 6004-6013, Vol. 72, No. 7
Howard Hughes Medical
Institute1 and
Departments of
Microbiology,2
Neurology,3 and
Medicine,4 University of
Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6148
Received 29 January 1998/Accepted 15 April 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.
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Interaction of the Human Immunodeficiency Virus
Type 1 Vpr Protein with the Nuclear Pore Complex
*
Corresponding author. Mailing address: Howard Hughes
Medical Institute and Departments of Microbiology and Medicine,
University of Pennsylvania School of Medicine, Philadelphia, PA
19104-6148. Phone: (215) 573-3493. Fax: (215) 573-2172. E-mail:
malim{at}hhmi.upenn.edu.
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