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Proc Natl Acad Sci U S A. 2007 Jan 2;104(1):151-6. Epub 2006 Dec 21.

The zinc-finger antiviral protein recruits the RNA processing exosome to degrade the target mRNA.

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1
Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.

Abstract

Zinc-finger antiviral protein (ZAP) is a host antiviral factor that specifically inhibits the replication of Moloney murine leukemia virus (MLV) and Sindbis virus (SIN) by preventing accumulation of the viral mRNA in the cytoplasm. In previous studies, we demonstrated that ZAP directly binds to its specific target mRNAs. In this article, we provide evidence indicating that ZAP recruits the RNA processing exosome to degrade the target RNA. ZAP comigrated with the exosome in sucrose or glycerol velocity gradient centrifugation. Immunoprecipitation of ZAP coprecipitated the exosome components. In vitro pull-down assays indicated that ZAP directly interacted with the exosome component hRrp46p and that the binding region of ZAP was mapped to amino acids 224-254. Depletion of the exosome component hRrp41p or hRrp46p with small interfering RNA significantly reduced ZAP's destabilizing activity. These findings suggest that ZAP is a trans-acting factor that modulates mRNA stability.

PMID:
17185417
PMCID:
PMC1765426
DOI:
10.1073/pnas.0607063104
[Indexed for MEDLINE]
Free PMC Article
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