A viral deubiquitylating enzyme targets viral RNA-dependent RNA polymerase and affects viral infectivity |
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Authors: | Chenon Mélanie Camborde Laurent Cheminant Soizic Jupin Isabelle |
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Affiliation: | Laboratoire de Virologie Moléculaire, CNRS-Univ Paris Diderot, Institut Jacques Monod, Cell Biology Department, UMR 7592, Paris, France. |
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Abstract: | Selective protein degradation via the ubiquitin-proteasome system (UPS) plays an essential role in many major cellular processes, including host-pathogen interactions. We previously reported that the tightly regulated viral RNA-dependent RNA polymerase (RdRp) of the positive-strand RNA virus Turnip yellow mosaic virus (TYMV) is degraded by the UPS in infected cells, a process that affects viral infectivity. Here, we show that the TYMV 98K replication protein can counteract this degradation process thanks to its proteinase domain. In-vitro assays revealed that the recombinant proteinase domain is a functional ovarian tumour (OTU)-like deubiquitylating enzyme (DUB), as is the 98K produced during viral infection. We also demonstrate that 98K mediates in-vivo deubiquitylation of TYMV RdRp protein--its binding partner within replication complexes--leading to its stabilization. Finally, we show that this DUB activity contributes to viral infectivity in plant cells. The identification of viral RdRp as a specific substrate of the viral DUB enzyme thus reveals the intricate interplay between ubiquitylation, deubiquitylation and the interaction between viral proteins in controlling levels of RdRp and viral infectivity. |
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Keywords: | deubiquitylating enzyme RNA‐dependent RNA polymerase ubiquitin‐proteasome system viral replication |
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