Plasmodesmal targeting and intercellular movement of potato mop-top pomovirus is mediated by a membrane anchored tyrosine-based motif on the lumenal side of the endoplasmic reticulum and the C-terminal transmembrane domain in the TGB3 movement protein

Jens Tilsner, G. H. Cowan, A. G. Roberts, S. N. Chapman, A. Ziegler, E. Savenkov, L. Torrance

Research output: Contribution to journalArticlepeer-review

27 Citations (Scopus)

Abstract

Live-cell fluorescence microscopy was used to investigate the third triple gene block protein (TGB3) of potato mop-top pomovirus and its role in assisted targeting of TGB2 to plasmodesmata (PD). Wild-type and mutant TGB3 proteins were expressed under the control of the 35 S promoter or from a virus reporter clone. Assisted targeting of TGB2 to PD was optimal when the proteins were expressed from a bicistronic plasmid in the relative ratios expected in a virus infection, suggesting that excess TGB3 inhibited PD localisation. Contrary to the generally accepted view, bimolecular fluorescence complementation showed that the TGB3 N terminus is located in the cytosol. Mutational analysis to dissect TGB3 sub domain functions showed that PD targeting was mediated by a composite signal comprising an ER-lumenal tyrosine-based motif and the C-terminal transmembrane domain. Mutation of either of these domains also abolished cell-to-cell movement of the virus. The results are discussed in the context of TGB3 membrane topology. (C) 2010 Elsevier Inc. All rights reserved.

Original languageEnglish
Pages (from-to)41-51
Number of pages11
JournalVirology
Volume402
Issue number1
DOIs
Publication statusPublished - 20 Jun 2010

Keywords

  • Triple gene block
  • Hordei-like virus movement proteins
  • Bimolecular fluorescence complementation
  • Green fluorescent protein
  • Red fluorescent protein
  • TRIPLE GENE BLOCK
  • TOBACCO-MOSAIC-VIRUS
  • POA SEMILATENT VIRUS
  • SUBCELLULAR-LOCALIZATION
  • CELL MOVEMENT
  • PLANT
  • RNA
  • PREDICTION
  • TOPOLOGY
  • REVEALS

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