scholarly journals Stability in vitro of the 69K movement protein of Turnip yellow mosaic virus is regulated by the ubiquitin-mediated proteasome pathway

2002 ◽  
Vol 83 (12) ◽  
pp. 3187-3197 ◽  
Author(s):  
Gabrièle Drugeon ◽  
Isabelle Jupin
Keyword(s):  
Mosaic Virus ◽  
Movement Protein ◽  
Cell Movement ◽  
Plant Viruses ◽  
Yellow Mosaic Virus ◽  
Turnip Yellow Mosaic Virus ◽  
Movement Proteins ◽  
Transient Nature ◽  
Reticulocyte Lysate

Plant viruses move to adjacent cells with the use of virus-encoded cell-to-cell movement proteins. Using proteins produced by in vitro translation, we present evidence that the ‘69K’ movement protein of Turnip yellow mosaic virus (TYMV) is recognized as a substrate for the attachment of polyubiquitin chains and for subsequent rapid and selective proteolysis by the proteasome, the ATP-dependent proteolytic system present in reticulocyte lysate. Truncation of the 69K protein suggests the existence of two degradation signals within its sequence. We propose that selective degradation of virus movement proteins may contribute to the previously reported transient nature of their accumulation during infection.

scholarly journals Towards plant resistance to viruses using protein-only RNase P

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Anthony Gobert ◽  
Yifat Quan ◽  
Mathilde Arrivé ◽  
Florent Waltz ◽  
Nathalie Da Silva ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Virus Replication ◽  
Yield Loss ◽  
Rnase P ◽  
Plant Viruses ◽  
Yellow Mosaic Virus ◽  
Resistance To Viruses ◽  
Target Plant

AbstractPlant viruses cause massive crop yield loss worldwide. Most plant viruses are RNA viruses, many of which contain a functional tRNA-like structure. RNase P has the enzymatic activity to catalyze the 5′ maturation of precursor tRNAs. It is also able to cleave tRNA-like structures. However, RNase P enzymes only accumulate in the nucleus, mitochondria, and chloroplasts rather than cytosol where virus replication takes place. Here, we report a biotechnology strategy based on the re-localization of plant protein-only RNase P to the cytosol (CytoRP) to target plant viruses tRNA-like structures and thus hamper virus replication. We demonstrate the cytosol localization of protein-only RNase P in Arabidopsis protoplasts. In addition, we provide in vitro evidences for CytoRP to cleave turnip yellow mosaic virus and oilseed rape mosaic virus. However, we observe varied in vivo results. The possible reasons have been discussed. Overall, the results provided here show the potential of using CytoRP for combating some plant viral diseases.

scholarly journals Actin Cytoskeleton Is Involved in Targeting of a Viral Hsp70 Homolog to the Cell Periphery

2005 ◽  
Vol 79 (22) ◽  
pp. 14421-14428 ◽  
Author(s):  
Alexey I. Prokhnevsky ◽  
Valera V. Peremyslov ◽  
Valerian V. Dolja
Keyword(s):  
Actin Cytoskeleton ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Movement Protein ◽  
Fluorescent Proteins ◽  
Cell Movement ◽  
Plant Viruses ◽  
Cell Periphery ◽  
Virus Particles ◽  
Shock Proteins

ABSTRACT The cell-to-cell movement of plant viruses involves translocation of virus particles or nucleoproteins to and through the plasmodesmata (PDs). As we have shown previously, the movement of the Beet yellows virus requires the concerted action of five viral proteins including a homolog of cellular ∼70-kDa heat shock proteins (Hsp70h). Hsp70h is an integral component of the virus particles and is also found in PDs of the infected cells. Here we investigate subcellular distribution of Hsp70h using transient expression of Hsp70h fused to three spectrally distinct fluorescent proteins. We found that fluorophore-tagged Hsp70h forms motile granules that are associated with actin microfilaments, but not with microtubules. In addition, immobile granules were observed at the cell periphery. A pairwise appearance of these granules at the opposite sides of cell walls and their colocalization with the movement protein of Tobacco mosaic virus indicated an association of Hsp70h with PDs. Treatment with various cytoskeleton-specific drugs revealed that the intact actomyosin motility system is required for trafficking of Hsp70h in cytosol and its targeting to PDs. In contrast, none of the drugs interfered with the PD localization of Tobacco mosaic virus movement protein. Collectively, these findings suggest that Hsp70h is translocated and anchored to PDs in association with the actin cytoskeleton.

scholarly journals Conversion in the Requirement of Coat Protein in Cell-to-Cell Movement Mediated by the Cucumber Mosaic Virus Movement Protein

2001 ◽  
Vol 75 (17) ◽  
pp. 8045-8053 ◽  
Author(s):  
Hideaki Nagano ◽  
Kazuyuki Mise ◽  
Iwao Furusawa ◽  
Tetsuro Okuno
Keyword(s):  
Amino Acids ◽  
Coat Protein ◽  
Cucumber Mosaic Virus ◽  
Mosaic Virus ◽  
Movement Protein ◽  
Cell Movement ◽  
Plant Viruses ◽  
Brome Mosaic Virus ◽  
Viral Movement ◽  
Intercellular Movement

ABSTRACT Plant viruses have movement protein (MP) gene(s) essential for cell-to-cell movement in hosts. Cucumber mosaic virus (CMV) requires its own coat protein (CP) in addition to the MP for intercellular movement. Our present results using variants of both CMV and a chimeric Brome mosaic virus with the CMV MP gene revealed that CMV MP truncated in its C-terminal 33 amino acids has the ability to mediate viral movement independently of CP. Coexpression of the intact and truncated CMV MPs extremely reduced movement of the chimeric viruses, suggesting that these heterogeneous CMV MPs function antagonistically. Sequential deletion analyses of the CMV MP revealed that the dispensability of CP occurred when the C-terminal deletion ranged between 31 and 36 amino acids and that shorter deletion impaired the ability of the MP to promote viral movement. This is the first report that a region of MP determines the requirement of CP in cell-to-cell movement of a plant virus.

Sign in / Sign up

Export Citation Format

Share Document