Abstract
Cell-to-cell movement of tobacco mosaic virus (TMV) is used to illustrate macromolecular traffic through plant intercellular connections, the plasmodesmata. This transport process is mediated by a specialized viral movement protein, P30. In the initially infected cell, P30 is produced by transcription of a subgenomic RNA derived from the invading virus. Presumably, P30 then associates with a certain proportion of the viral RNA molecules, sequestering them from replication and mediating their transport into neighbouring uninfected host cells. This nucleoprotein complex is targeted to plasmodesmata, possibly via interaction with the host cell's cytoskeleton. Prior to passage through a plasmodesma, the plasmodesmatal channel is dilated by the movement protein. It is proposed that targeting of P30-TMV RNA complexes to plasmodesmatal involves binding to a specific cell-wall-associated receptor molecule. This protein, designated p38, also functions as a protein kinase, phosphorylating P30 at its carboxy-terminus and minimizing P30-induced interference with plasmodesmatal permeability during viral infection.
| Original language | English |
|---|---|
| Pages (from-to) | 637-643 |
| Number of pages | 7 |
| Journal | Philosophical Transactions of the Royal Society B: Biological Sciences |
| Volume | 354 |
| Issue number | 1383 |
| DOIs | |
| State | Published - 1999 |
Keywords
- Movement protein
- Phosphorylation
- Plasmodesma targeting signals
- Plasmodesmata
- Protein-nucleic acid complexes
- Regulation of plasmodesmatal permeability
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