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Molecular and Cellular Biology, November 2000, p. 8590-8601, Vol. 20, No. 22
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

Jeannine M. Petersen, Lu-Shuin Her, Virgil Varvel, Elsebet Lund, and James E. Dahlberg*

Department of Biomolecular Chemistry, University of Wisconsin---Madison, Madison, Wisconsin 53706-1532

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 (alpha 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 alpha 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.

Molecular and Cellular Biology, November 2000, p. 8590-8601, Vol. 20, No. 22
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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