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Rapid RNase L-driven arrest of protein synthesis in the dsRNA response without degradation of translation machinery

Author(s): Donovan, Jesse; Rath, Sneha; Kolet-Mandrikov, David; Korennykh, Alexei

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DC FieldValueLanguage
dc.contributor.authorDonovan, Jesse-
dc.contributor.authorRath, Sneha-
dc.contributor.authorKolet-Mandrikov, David-
dc.contributor.authorKorennykh, Alexei-
dc.date.accessioned2020-02-26T19:48:28Z-
dc.date.available2020-02-26T19:48:28Z-
dc.date.issued2017-11en_US
dc.identifier.citationDonovan, Jesse, Rath, Sneha, Kolet-Mandrikov, David, Korennykh, Alexei. (2017). Rapid RNase L-driven arrest of protein synthesis in the dsRNA response without degradation of translation machinery.. RNA, 23 (11), 1660 - 1671. doi:10.1261/rna.062000.117en_US
dc.identifier.issn1355-8382-
dc.identifier.urihttp://arks.princeton.edu/ark:/88435/pr11n4x-
dc.description.abstractMammalian cells respond to double-stranded RNA (dsRNA) by activating a translation-inhibiting endoribonuclease, RNase L. Consensus in the field indicates that RNase L arrests protein synthesis by degrading ribosomal RNAs (rRNAs) and messenger RNAs (mRNAs). However, here we provide evidence for a different and far more efficient mechanism. By sequencing abundant RNA fragments generated by RNase L in human cells, we identify site-specific cleavage of two groups of noncoding RNAs: Y-RNAs, whose function is poorly understood, and cytosolic tRNAs, which are essential for translation. Quantitative analysis of human RNA cleavage versus nascent protein synthesis in lung carcinoma cells shows that RNase L stops global translation when tRNAs, as well as rRNAs and mRNAs, are still intact. Therefore, RNase L does not have to degrade the translation machinery to stop protein synthesis. Our data point to a rapid mechanism that transforms a subtle RNA cleavage into a cell-wide translation arrest.en_US
dc.format.extent1660 - 1671en_US
dc.languageengen_US
dc.language.isoen_USen_US
dc.relation.ispartofRNAen_US
dc.rightsFinal published version. This is an open access article.en_US
dc.titleRapid RNase L-driven arrest of protein synthesis in the dsRNA response without degradation of translation machineryen_US
dc.typeJournal Articleen_US
dc.identifier.doidoi:10.1261/rna.062000.117-
dc.identifier.eissn1469-9001-
pu.type.symplectichttp://www.symplectic.co.uk/publications/atom-terms/1.0/journal-articleen_US

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