MassIVE MSV000099383

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RNase L regulates the antiviral proteome by accelerating mRNA decay, inhibiting nuclear mRNA export, and repressing RNAPII-mediated transcription

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Description

Ribonuclease L (RNase L) is an antiviral endoribonuclease that triggers widespread degradation of cellular mRNAs. Here, we show that the degradation of cellular mRNA by RNase L is a conserved response to flaviviruses, including Zika virus (ZIKV), dengue virus serotype 2 (DENV-2), and West Nile virus (WNV). Quantitative mass spectrometry in response to dsRNA or ZIKV infection shows that RNase L broadly downregulates the cellular proteome, reducing proteins with short half-lives involved in cell cycle progression, cellular metabolism, and protein synthesis. The mRNAs encoded by interferon-stimulated genes (ISGs) evade mRNA decay by RNase L, allowing for protein synthesis of ISG-encoding mRNAs. However, RNase L dampens ISG protein synthesis by triggering a block in nuclear mRNA export and repressing RNAPII-mediated transcription at later times during the antiviral response. These findings implicate reprograming of the cellular proteome as primary means by which RNase L combats viral infection, tumorigenesis, and immune dysregulation. [doi:10.25345/C5P844845] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: RNaseL ; Virus ; Innate Immunity ; mRNA ; dsRNA ; DatasetType:Proteomics

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Principal Investigators:
(in alphabetical order) 		Ciaran Seath, University of Florida, USA
James M. Burke, The Herbert Wertheim University of Florida Scripps Institute for Biomedical Innovation and Technology, USA
Submitting User: camerondouglas
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