Localization by immunogold cytochemistry of the virus-coded 30K protein in plasmodesmata of leaves infected with tobacco mosaic virus

Tomenius, K.; Clapham, David; Meshi, Tetsuo

doi:10.1016/0042-6822(87)90007-9

Cited by 251 publications

(143 citation statements)

References 21 publications

Supporting

Mentioning

132

Contrasting

Unclassified

Order By: Relevance

“…The protein localizes to plasmodesmata in infected plants (Tomenius et al, 1987) and in transgenic plants that accumulate the MP, and induces the formation of fibrous material within the plasmodesmata (Ding et al, 1992;Moore et al, 1992). The MP alters the molecular size exclusion limit of plasmodesmata, increasing the limit from about 750 Da in non-transgenic plants to greater than 10 kDa in transgenic plants (Wolf et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

Domains of the TMV movement protein involved in subcellular localization

et al. 1998

View full text Add to dashboard Cite

SummaryTo identify and map functionally important regions of the tobacco mosaic virus movement protein, deletions of three amino acids were introduced at intervals of 10 amino acids throughout the protein. Mutations located between amino acids 1 and 160 abolished the capacity of the protein to transport virus from cell to cell, while some of the mutations in the C-terminal third of the protein permitted function. Despite extensive tests, no examples were found of intermolecular complementation between mutants, suggesting that function requires each movement protein molecule to be fully competent. Many of the mutants were fused to green fluorescent protein, and their subcellular localizations were determined by fluorescence microscopy in infected plants and protoplasts. Most mutants lost the ability to accumulate in one or more of the multiple subcellular sites targeted by wild-type movement protein, suggesting that specific functional domains were disrupted. The order in which accumulation at subcellular sites occurs during infection does not represent a targeting pathway. Association of the movement protein with microtubules or with plasmodesmata can occur in the absence of other associations. The region of the protein around amino acids 9-11 may be involved in targeting the protein to cortical bodies (probably associated with the endoplasmic reticulum) and to plasmodesmata. The region around residues 49-51 may be involved in co-alignment of the protein with microtubules. The region around residues 88-101 appears to play a role in targeting to both the cortical bodies and microtubules. Thus, the movement protein contains independently functional domains.

show abstract

Section: Introductionmentioning

confidence: 99%

Domains of the TMV movement protein involved in subcellular localization

et al. 1998

View full text Add to dashboard Cite

show abstract

“…Recently, we have isolated a plant cell receptor for P30. Because P30 has been shown to localize to plasmodesmata within plant cell walls (Tomenius et al 1987;Ding et al 1992), it may speci¢cally interact directly with a cell-wall-associated receptor. Thus, we developed a renatured blot overlay-binding assay for interaction between P30 and cell-wall proteins.…”

Section: Interaction With a Cell-wall-associated Receptormentioning

confidence: 99%

Tobacco mosaic virus: a pioneer to cell–to–cell movement

Citovsky

1999

Phil. Trans. R. Soc. Lond. B

View full text Add to dashboard Cite

Cell-to-cell movement of tobacco mosaic virus (TMV) is used to illustrate macromolecular tra¤c 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 speci¢c 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.

show abstract

“…Immunocytological studies have shown that the movement protein of tobacco mosaic virus (TMV) is localized in the plasmodesmata, both in infected plants and in uninfected transgenic plants expressing the movement protein from a chromosomally inserted gene (Tomenius et al, 1987;Atkins et al, 1991), and that the protein is found in a cell wall-enriched fraction after subcellular fractionation of tissue from infected plants (Moser et al, 1988;Lehto et al, 1990). Putative movement proteins of a number of other viruses, e.g.…”

mentioning

confidence: 99%