Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

If You Use a Screen Reader

This content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.

Tobacco Mosaic Virus: A Pioneer of Cell-To-Cell Movement

Vitaly Citovsky
Philosophical Transactions: Biological Sciences
Vol. 354, No. 1383, Tobacco Mosaic Virus: Pioneering Research for a Century (Mar. 29, 1999), pp. 637-643
Published by: Royal Society
Stable URL: http://www.jstor.org/stable/56731
Page Count: 3
  • Read Online (Free)
  • Cite this Item
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Tobacco Mosaic Virus: A Pioneer of Cell-To-Cell Movement
Preview not available

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 carboxyterminus and minimizing P30-induced interference with plasmodesmatal permeability during viral infection.

Page Thumbnails

  • Thumbnail: Page 
637
    637
  • Thumbnail: Page 
638
    638
  • Thumbnail: Page 
639
    639