The Matrix Protein of Vesicular Stomatitis Virus Inhibits Nucleocytoplasmic Transport When It Is in the Nucleus and Associated with Nuclear Pore Complexes

doi:10.1128/MCB.20.22.8590-8601.2000

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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. Herewe demonstrate that inhibition occurs when M protein is in thenucleus of Xenopus laevis oocytes and that M activity is readilyreversed by a monoclonal antibody ( $alpha$ M). We identify a region ofM protein, amino acids 51 to 59, that is required both for inhibitionof transport and for efficient recognition by $alpha$ M. When expressedin transfected HeLa cells, M protein colocalizes with nuclearpore complexes (NPCs) at the nuclear rim. Moreover, mutation ofa single amino acid, methionine 51, eliminates both transportinhibition and targeting to NPCs. We propose that M protein inhibitsbidirectional transport by interacting with a component of theNPC or an NPC-associated factor that participates in nucleocytoplasmictransport.

^* Corresponding author. Mailing address: Department of Biomolecular Chemistry, University of Wisconsin $---$ Madison, 1300 UniversityAve., 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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