scholarly journals Depletion of the Photosystem II Core Complex in Mature Tobacco Leaves Infected by the Flavum Strain of Tobacco mosaic virus

2003 ◽  
Vol 16 (12) ◽  
pp. 1135-1144 ◽  
Author(s):  
Kirsi Lehto ◽  
Mikko Tikkanen ◽  
Jean-Baptiste Hiriart ◽  
Virpi Paakkarinen ◽  
Eva-Mari Aro

The flavum strain of Tobacco mosaic virus (TMV) differs from the wild-type (wt) virus by causing strong yellow and green mosaic in the systemically infected developing leaves, yellowing in the fully expanded leaves, and distinct malformations of chloroplasts in both types of infected tissues. Analysis of the thylakoid proteins of flavum strain-infected tobacco leaves indicated that the chlorosis in mature leaves was accompanied by depletion of the entire photosystem II (PSII) core complexes and the 33-kDa protein of the oxygen evolving complex. The only change observed in the thyla-koid proteins of the corresponding wt TMV-infected leaves was a slight reduction of the α and β subunits of the ATP synthase complex. The coat proteins of different yellowing strains of TMV are known to effectively accumulate inside chloroplasts, but in this work, the viral movement protein also was detected in association with the thylakoid membranes of flavum strain-infected leaves. The mRNAs of different enzymes involved in the chlorophyll biosynthesis pathway were not reduced in the mature chlorotic leaves. These results suggest that the chlorosis was not caused by reduction of pigment biosynthesis, but rather, by reduction of specific proteins of the PSII core complexes and by consequent break-down of the pigments.

2001 ◽  
Vol 14 (7) ◽  
pp. 914-917 ◽  
Author(s):  
Harald Jockusch ◽  
Christiane Wiegand ◽  
Birgit Mersch ◽  
Daniela Rajes

We analyzed, with respect to heat shock proteins (HSPs), systemically reacting tobacco leaves inoculated with Tobacco mosaic virus (TMV), wild-type vulgare, and temperature-sensitive coat protein (CP) mutants Ni 118 (P20L) and flavum (D19A), kept at 23 or 30°C. HSP18 and HSP70 mRNAs and proteins were induced with temperature-sensitive CP mutants after 1 to 2 days at 30°C. After 4 to 6 days, HSP70 was also induced at 23°C. The induction of HSPs paralleled the amount of insoluble TMV CP in leaf extracts, indicating that denatured TMV CP by itself induces a heat-shock response.


ACS Nano ◽  
2020 ◽  
Author(s):  
Jing Dai ◽  
Gavin J. Knott ◽  
Wen Fu ◽  
Tiffany W. Lin ◽  
Ariel L. Furst ◽  
...  

1999 ◽  
Vol 354 (1383) ◽  
pp. 637-643 ◽  
Author(s):  
Vitaly Citovsky

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 cytoskeleton. Prior to passage through a plasmodesma, the plasmodesmal channel is dilated by the movement protein. It is proposed that targeting of P30–TMV RNA complexes to plasmodesmata involves binding to a specific cell wall–associated receptor molecule. In addition, a cell wall–associated protein kinase, phosphorylates P30 at its carboxy–terminus and minimizes P30–induced interference with plasmodesmatal permeability during viral infection.


1969 ◽  
Vol 45 (10) ◽  
pp. 919-924 ◽  
Author(s):  
Yuko OHASHI ◽  
Takeshi OHNO ◽  
Yuzo NOZU ◽  
Yoshimi OKADA

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