Stability in vitro of the 69K movement protein of Turnip yellow mosaic virus is regulated by the ubiquitin-mediated proteasome pathway.
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.
Drugeon
Gabrièle
G
Laboratoire de Virologie Moléculaire, Institut Jacques Monod, UMR 7592, CNRS - Universités Paris 6-Paris 7, 2 place Jussieu, 75251 Paris Cedex 05, France1.
Jupin
Isabelle
I
Laboratoire de Virologie Moléculaire, Institut Jacques Monod, UMR 7592, CNRS - Universités Paris 6-Paris 7, 2 place Jussieu, 75251 Paris Cedex 05, France1.
D000818:Animals; D029688:Brassica napus / Q000821:virology*; D015967:Gene Expression Regulation, Viral; D010935:Plant Diseases / Q000821:virology; D053830:Plant Viral Movement Proteins; D010942:Plant Viruses / Q000378:metabolism / Q000472:pathogenicity; D014176:Protein Biosynthesis; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism; D017806:Tymovirus / Q000378:metabolism* / Q000472:pathogenicity; D025801:Ubiquitin / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*
D053830:Plant Viral Movement Proteins; D025801:Ubiquitin; D014764:Viral Proteins