Degradation of tobacco mosaic virus movement protein by the 26S proteasome

Citation
C. Reichel et Rn. Beachy, Degradation of tobacco mosaic virus movement protein by the 26S proteasome, J VIROLOGY, 74(7), 2000, pp. 3330-3337
Citations number
56
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Microbiology
Journal title
JOURNAL OF VIROLOGY
ISSN journal
0022-538X → ACNP
Volume
74
Issue
7
Year of publication
2000
Pages
3330 - 3337
Database
ISI
SICI code
0022-538X(200004)74:7<3330:DOTMVM>2.0.ZU;2-U
Abstract
Cell-to-cell spread of tobacco mosaic virus is facilitated by the virus-enc oded 30-kDa movement protein (MP). This process involves interaction of vir al proteins with host components, including the cytoskeleton and the endopl asmic reticulum (ER). During virus infection, high-molecular-weight forms o f MP were detected in tobacco BY-2 protoplasts. Inhibition of the 26S prote asome by MG115 and clasto-lactacystin-beta-laetone enhanced the accumulatio n of high-molecular-weight forms of MP and led to increased stability of th e MP. Such treatment also increased the apparent accumulation of polyubiqui tinated host proteins. Ey fusion of MP with the jellyfish green fluorescent protein (GFP), we demonstrated that inhibition of the 26S proteasome led t o accumulation of the MP-GFP fusion preferentially on the ER, particularly the perinuclear ER. We suggest that polyubiquitination of MP and subsequent degradation by the 26S proteasome may play a substantial role in regulatio n of virus spread by reducing the damage caused by the MP on the structure of cortical ER.