Volume 1 Issue 10
Oct.  2010
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Peiying Ye, Shufeng Liu, Yiping Zhu, Guifang Chen, Guangxia Gao. DEXH-Box protein DHX30 is required for optimal function of the zinc-finger antiviral protein[J]. Protein&Cell, 2010, 1(10): 956-964. doi: 10.1007/s13238-010-0117-8
Citation: Peiying Ye, Shufeng Liu, Yiping Zhu, Guifang Chen, Guangxia Gao. DEXH-Box protein DHX30 is required for optimal function of the zinc-finger antiviral protein[J]. Protein&Cell, 2010, 1(10): 956-964. doi: 10.1007/s13238-010-0117-8

DEXH-Box protein DHX30 is required for optimal function of the zinc-finger antiviral protein

doi: 10.1007/s13238-010-0117-8
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We thank Jing Sun and Yihui Xu for technical support and Dr. Fuquan Yang for help with the MALDI-TOF analyses. This work was in part supported by the grant to Guangxia Gao from National Science Foundation of China (Grant No. 81030030), and by the grant to Guifang Chen from National Science Foundation (Grant No. 30800053).

  • Received Date: 2010-08-29
  • Rev Recd Date: 2010-09-26
  • The zinc-finger antiviral protein (ZAP) is a host factor that specifically inhibits the replication of certain viruses by eliminating viral mRNAs in the cytoplasm. In previous studies, we demonstrated that ZAP directly binds to the viral mRNAs and recruits the RNA exosome to degrade the target RNA. In this article, we provide evidence that a DEXH box RNA helicase, DHX30, is required for optimal antiviral activity of ZAP. Pull-down and co-immunoprecipitation assays demonstrated that DHX30 and ZAP interacted with each other via their N terminal domains. Downregulation of DHX30 with shRNAs reduced ZAP's antiviral activity. These data implicate that DHX30 is a cellular factor involved in the antiviral function of ZAP.
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