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The Plant Cell, Vol. 14, 1207-1222, June 2002, Copyright © 2002,
American Society of Plant Biologists

Functional Analysis of a DNA-Shuffled Movement Protein Reveals That Microtubules Are Dispensable for the Cell-to-Cell Movement of Tobacco mosaic virus

Trudi Gillespie, Petra Boevink, Sophie Haupt, Alison G. Roberts, Rachel Toth, Tracy Valentine, Sean Chapman and Karl J. Oparka1

Unit of Cell Biology, Scottish Crop Research Institute, Invergowrie, Dundee DD2 5DA, United Kingdom

1 To whom correspondence should be addressed. E-mail kopark{at}scri.sari.ac.uk; fax 44-1382-562426

Microtubules interact strongly with the viral movement protein (MP) of Tobacco mosaic virus (TMV) and are thought to transport the viral genome between plant cells. We describe a functionally enhanced DNA-shuffled movement protein (MPR3) that remained bound to the vertices of the cortical endoplasmic reticulum, showing limited affinity for microtubules. A single amino acid change was shown to confer the MPR3 phenotype. Disruption of the microtubule cytoskeleton in situ with pharmacological agents, or by silencing of the {alpha}-tubulin gene, had no significant effect on the spread of TMV vectors expressing wild-type MP (MPWT) and did not prevent the accumulation of MPWT in plasmodesmata. Thus, cell-to-cell trafficking of TMV can occur independently of microtubules. The MPR3 phenotype was reproduced when infection sites expressing MPWT were treated with a specific proteasome inhibitor, indicating that the degradation of MPR3 is impaired. We suggest that the improved viral transport functions of MPR3 arise from evasion of a host degradation pathway.




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