Interaction of the La-related protein Slf1 with colliding ribosomes maintains translation of oxidative-stress responsive mRNAs
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| Title: | Interaction of the La-related protein Slf1 with colliding ribosomes maintains translation of oxidative-stress responsive mRNAs |
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| Authors: | Martin D Jennings, Priya Srivastava, Christopher J Kershaw, David Talavera, Christopher M Grant, Graham D Pavitt |
| Source: | Nucleic Acids Res Jennings, M, Srivastava, P, Kershaw, C J, Talavera, D, Grant, C & Pavitt, G 2023, 'Interaction of the La-related protein Slf1 with colliding ribosomes maintains translation of oxidative-stress responsive mRNAs.', Nucleic Acids Res, vol. 51, no. 11, pp. 5755–5773. https://doi.org/10.1093/nar/gkad272, https://doi.org/10.1093/nar/gkad272 |
| Publisher Information: | Oxford University Press (OUP), 2023. |
| Publication Year: | 2023 |
| Subject Terms: | RNA, Messenger/genetics, Antioxidants/metabolism, Oxidative Stress/genetics, Saccharomyces cerevisiae, Antioxidants, Saccharomyces cerevisiae/genetics, Oxidative Stress, Protein Biosynthesis, Ribosomes/genetics, RNA and RNA-protein complexes, RNA, Messenger/genetics, RNA, Messenger, Ribosomes |
| Description: | In response to oxidative stress cells reprogram gene expression to enhance levels of antioxidant enzymes and promote survival. In Saccharomyces cerevisiae the polysome-interacting La-related proteins (LARPs) Slf1 and Sro9 aid adaptation of protein synthesis during stress by undetermined means. To gain insight in their mechanisms of action in stress responses, we determined LARP mRNA binding positions in stressed and unstressed cells. Both proteins bind within coding regions of stress-regulated antioxidant enzyme and other highly translated mRNAs in both optimal and stressed conditions. LARP interaction sites are framed and enriched with ribosome footprints suggesting ribosome–LARP–mRNA complexes are identified. Although stress-induced translation of antioxidant enzyme mRNAs is attenuated in slf1Δ, these mRNAs remain on polysomes. Focusing further on Slf1, we find it binds to both monosomes and disomes following RNase treatment. slf1Δ reduces disome enrichment during stress and alters programmed ribosome frameshifting rates. We propose that Slf1 is a ribosome-associated translational modulator that stabilises stalled/collided ribosomes, prevents ribosome frameshifting and so promotes translation of a set of highly-translated mRNAs that together facilitate cell survival and adaptation to stress. |
| Document Type: | Article Other literature type |
| Language: | English |
| ISSN: | 1362-4962 0305-1048 |
| DOI: | 10.1093/nar/gkad272 |
| Access URL: | https://pubmed.ncbi.nlm.nih.gov/37070186 |
| Rights: | CC BY URL: http://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
| Accession Number: | edsair.doi.dedup.....3af404b8973844e50e1fb43a1e6aaa2c |
| Database: | OpenAIRE |
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Nájsť tento článok vo Web of Science | Abstract: | In response to oxidative stress cells reprogram gene expression to enhance levels of antioxidant enzymes and promote survival. In Saccharomyces cerevisiae the polysome-interacting La-related proteins (LARPs) Slf1 and Sro9 aid adaptation of protein synthesis during stress by undetermined means. To gain insight in their mechanisms of action in stress responses, we determined LARP mRNA binding positions in stressed and unstressed cells. Both proteins bind within coding regions of stress-regulated antioxidant enzyme and other highly translated mRNAs in both optimal and stressed conditions. LARP interaction sites are framed and enriched with ribosome footprints suggesting ribosome–LARP–mRNA complexes are identified. Although stress-induced translation of antioxidant enzyme mRNAs is attenuated in slf1Δ, these mRNAs remain on polysomes. Focusing further on Slf1, we find it binds to both monosomes and disomes following RNase treatment. slf1Δ reduces disome enrichment during stress and alters programmed ribosome frameshifting rates. We propose that Slf1 is a ribosome-associated translational modulator that stabilises stalled/collided ribosomes, prevents ribosome frameshifting and so promotes translation of a set of highly-translated mRNAs that together facilitate cell survival and adaptation to stress. |
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| ISSN: | 13624962 03051048 |
| DOI: | 10.1093/nar/gkad272 |