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Molecular and Cellular Biology, November 2000, p. 8590-8601, Vol. 20, No. 22
Department of Biomolecular Chemistry,
University of Wisconsin
Received 20 July 2000/Accepted 17 August 2000
The matrix (M) protein of vesicular stomatitis virus (VSV) is a
potent inhibitor of bidirectional nuclear transport. Here we
demonstrate that inhibition occurs when M protein is in the nucleus of
Xenopus laevis oocytes and that M activity is readily reversed by a monoclonal antibody (
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
The Matrix Protein of Vesicular Stomatitis Virus
Inhibits Nucleocytoplasmic Transport When It Is in the Nucleus and
Associated with Nuclear Pore Complexes
Madison, Madison, Wisconsin 53706-1532
M). We identify a region of M
protein, amino acids 51 to 59, that is required both for inhibition of
transport and for efficient recognition by
M. When expressed in
transfected HeLa cells, M protein colocalizes with nuclear pore
complexes (NPCs) at the nuclear rim. Moreover, mutation of a single
amino acid, methionine 51, eliminates both transport inhibition and
targeting to NPCs. We propose that M protein inhibits bidirectional
transport by interacting with a component of the NPC or an
NPC-associated factor that participates in nucleocytoplasmic transport.
*
Corresponding author. Mailing address: Department of
Biomolecular Chemistry, University of Wisconsin
Madison, 1300 University Ave., Madison, WI 53706-1532. Phone: (608) 262-1459. Fax:
(608) 262-8704. E-mail: dahlberg{at}facstaff.wisc.edu.
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