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- W2148542918 abstract "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." @default.
- W2148542918 created "2016-06-24" @default.
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- W2148542918 creator A5044416499 @default.
- W2148542918 date "2002-12-01" @default.
- W2148542918 modified "2023-09-30" @default.
- W2148542918 title "Stability in vitro of the 69K movement protein of Turnip yellow mosaic virus is regulated by the ubiquitin-mediated proteasome pathway" @default.
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- W2148542918 doi "https://doi.org/10.1099/0022-1317-83-12-3187" @default.
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