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RNase L reprograms translation by widespread mRNA turnover escaped by antiviral mRNAs

James M Burke, Stephanie L Moon, Evan T Lester, Tyler Matheny, Roy Parker
doi: https://doi.org/10.1101/486530
James M Burke
1Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA
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Stephanie L Moon
1Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA
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Evan T Lester
1Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA
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Tyler Matheny
1Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA
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Roy Parker
1Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309, USA
2Howard Hughes Medical Institute, University of Colorado, Boulder, CO 80309, USA
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  • For correspondence: roy.parker@colorado.edu
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SUMMARY

In response to foreign and endogenous double-stranded RNA (dsRNA), protein kinase R (PKR) and ribonuclease L (RNase L) reprogram translation in mammalian cells. PKR inhibits translation initiation through eIF2α phosphorylation, which triggers stress granule (SG) formation and promotes translation of stress responsive mRNAs. The mechanisms of RNase L-driven translation repression, its contribution to SG assembly, and its regulation of dsRNA stress-induced mRNAs are unknown. We demonstrate that RNase L drives translational shut-off in response to dsRNA by promoting widespread turnover of mRNAs. This alters stress granule assembly and reprograms translation by only allowing for the translation of mRNAs resistant to RNase L degradation, including numerous antiviral mRNAs such as IFN-β. Individual cells differentially activate dsRNA responses revealing variation that can affect cellular outcomes. This identifies bulk mRNA degradation and the resistance of antiviral mRNAs as the mechanism by which RNaseL reprograms translation in response to dsRNA.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC 4.0 International license.
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Posted December 04, 2018.
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RNase L reprograms translation by widespread mRNA turnover escaped by antiviral mRNAs
James M Burke, Stephanie L Moon, Evan T Lester, Tyler Matheny, Roy Parker
bioRxiv 486530; doi: https://doi.org/10.1101/486530
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RNase L reprograms translation by widespread mRNA turnover escaped by antiviral mRNAs
James M Burke, Stephanie L Moon, Evan T Lester, Tyler Matheny, Roy Parker
bioRxiv 486530; doi: https://doi.org/10.1101/486530

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