4.6 Article

Relocalization of Translation Termination and Ribosome Recycling Factors to Stress Granules Coincides with Elevated Stop-Codon Readthrough and Reinitiation Rates upon Oxidative Stress

Journal

CELLS
Volume 12, Issue 2, Pages -

Publisher

MDPI
DOI: 10.3390/cells12020259

Keywords

stress granules; translation termination; ribosome recycling; translation reinitiation; ETF1; GSPT1; MCTS1; ligatin; oxidative stress; upstream open reading frames uORFs

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Upon oxidative stress, mammalian cells reprogram their translation and form stress granules (SGs). Arsenite-induced stress increases stop-codon readthrough rate and translation reinitiation levels on uORF-containing and bicistronic mRNAs. Translation termination factors, ribosome recycling, and translation reinitiation factors are recruited to SGs during arsenite treatment. This spatial redistribution of translation factors may contribute to mRNA translation resumption and suggest the presence of post-termination, recycling, or reinitiation complexes in SGs.
Upon oxidative stress, mammalian cells rapidly reprogram their translation. This is accompanied by the formation of stress granules (SGs), cytoplasmic ribonucleoprotein condensates containing untranslated mRNA molecules, RNA-binding proteins, 40S ribosomal subunits, and a set of translation initiation factors. Here we show that arsenite-induced stress causes a dramatic increase in the stop-codon readthrough rate and significantly elevates translation reinitiation levels on uORF-containing and bicistronic mRNAs. We also report the recruitment of translation termination factors eRF1 and eRF3, as well as ribosome recycling and translation reinitiation factors ABCE1, eIF2D, MCT-1, and DENR to SGs upon arsenite treatment. Localization of these factors to SGs may contribute to a rapid resumption of mRNA translation after stress relief and SG disassembly. It may also suggest the presence of post-termination, recycling, or reinitiation complexes in SGs. This new layer of translational control under stress conditions, relying on the altered spatial distribution of translation factors between cellular compartments, is discussed.

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