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RNase L Reprograms Translation by Widespread mRNA Turnover Escaped by Antiviral mRNAs

Molecular cell, 2019-09, Vol.75 (6), p.1203-1217.e5 [Peer Reviewed Journal]

2019 Elsevier Inc. ;Copyright © 2019 Elsevier Inc. All rights reserved. ;ISSN: 1097-2765 ;EISSN: 1097-4164 ;DOI: 10.1016/j.molcel.2019.07.029 ;PMID: 31494035

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Title:
RNase L Reprograms Translation by Widespread mRNA Turnover Escaped by Antiviral mRNAs
Author: Burke, James M. ; Moon, Stephanie L. ; Matheny, Tyler ; Parker, Roy
Subjects: A549 Cells ; Cellular Reprogramming ; dsRNA ; eIF-2 Kinase - genetics ; eIF-2 Kinase - metabolism ; eIF2a ; Endoribonucleases - genetics ; Endoribonucleases - metabolism ; HEK293 Cells ; Humans ; innate immune response ; interferon ; Interferon-beta - biosynthesis ; Interferon-beta - genetics ; mRNA degradation ; mRNA metabolism ; PABPC1 ; PKR ; Protein Biosynthesis ; RNA Stability ; RNA, Double-Stranded - genetics ; RNA, Double-Stranded - metabolism ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; RNase L ; stress granule
Is Part Of: Molecular cell, 2019-09, Vol.75 (6), p.1203-1217.e5
Description: 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 allowing translation of mRNAs resistant to RNase L degradation, including numerous antiviral mRNAs such as interferon (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 RNase L reprograms translation in response to dsRNA. [Display omitted] •RNase L promotes rapid and widespread decay of basal mRNAs•RNase L limits SG assembly via turnover of SG-associated mRNAs•Degradation of mRNAs accounts for RNase L-mediated shutoff of translation•Antiviral mRNAs escape RNase L, permitting their translation during host shutoff Burke et al. demonstrate that RNase L reduces bulk translation and stress granule assembly in response to dsRNA via rapid and widespread decay of basal mRNAs. In contrast to basal mRNAs, antiviral mRNAs escape RNase L-mediated mRNA decay, which permits their translation during RNase L-mediated host shutoff.
Publisher: United States: Elsevier Inc
Language: English
Identifier: ISSN: 1097-2765
EISSN: 1097-4164
DOI: 10.1016/j.molcel.2019.07.029
PMID: 31494035
Source: Cell Press Free Archives
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RNase L Reprograms Translation by Widespread mRNA Turnover Escaped by Antiviral mRNAs

2019 Elsevier Inc. ;Copyright © 2019 Elsevier Inc. All rights reserved. ;ISSN: 1097-2765 ;EISSN: 1097-4164 ;DOI: 10.1016/j.molcel.2019.07.029 ;PMID: 31494035

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