A viral deubiquitylating enzyme targets viral RNA-dependent RNA polymerase and affects viral infectivity.
نویسندگان
چکیده
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.
منابع مشابه
A viral deubiquitylating enzyme targets viral RNA - dependent RNA polymerase and affects viral
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A viral deubiquitylating enzyme stabilizes viral RNA- dependent RNA polymerase and affects viral infectivity
Thank you for submitting your manuscript on the identification of DUB function in the TYMV protease for consideration by The EMBO Journal. Three referees have now provided their comments, which are copied below. As you will see, the referees appreciate that your study (for the most part convincingly) establishes TYMV 98K as a bona fide new example of a viral DUB enzyme, although a few open ques...
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ورودعنوان ژورنال:
- The EMBO journal
دوره 31 3 شماره
صفحات -
تاریخ انتشار 2012