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|Abstract:||Mammalian 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.|
|Citation:||Donovan, 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.062000.117|
|Pages:||1660 - 1671|
|Type of Material:||Journal Article|
|Version:||Final published version. This is an open access article.|
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