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Domains of tobacco mosaic virus movement protein essential for its membrane association

Masaaki Fujiki

Shigeki Kawakami

Ryan W. Kim

Donald Danforth Plant Science Center, 975 North Warson Road, St Louis, MO 63132, USA

Correspondence
Roger N. Beachy
rnbeachy{at}danforthcenter.org

A series of deletion mutants of tobacco mosaic virus movement protein (TMV-MP) was used to identify domains of the protein necessary for membrane association. A membrane fraction was isolated from tobacco BY-2 protoplasts infected with wild-type and mutant TMV that produce MP carrying a 3 aa deletion. Deletions that affected membrane association were clustered around the two major hydrophobic regions of MP that are predicted to be transmembrane. Deletions in other hydrophobic regions also reduced membrane association. In addition, a non-functional mutant of MP, in which one of the known phosphorylation sites was eliminated, was not associated with cellular membranes, while a functional second site revertant restored membrane association. This indicates that MP function requires interaction with membrane; however, membrane association was not sufficient for function. Results are consistent with the hypothesis that TMV-MP is an integral or tightly associated membrane protein that includes two hydrophobic transmembrane domains.

Present address: Fraunhofer USA Center for Molecular Biotechnology, 9 Innovation Way, Newark, DE 19711, USA.

Present address: Department of Biotechnology, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita 565-0871, Osaka, Japan.

Present address: W. M. Keck Center for Comparative and Functional Genomics, 329 Edward R. Madigan Laboratory (MC 051), 1201 West Gregory Drive, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.