The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Heat shock induces silent ribosomes and reorganizes mRNA turnover
Open accessPublished version of a preprint
Abstract
mRNAs associate with single or multiple ribosomes; these ribosomal assemblies-monosomes and polysomes-translate the mRNAs before degradation. The impact of heat stress on this mRNA turnover remains unclear. We show that in heat-shocked yeast cells, the proportion of monosomes increases without a corresponding rise in the number of associated mRNAs. Consequently, most monosomes are devoid of mRNAs and silent, lacking translational initiation factors and proteins facilitating posttranslational folding. Such silent monosomes also appear under other stress conditions, with proportions varying according to stress type, suggesting that they represent a general feature of cellular adaptation. In parallel with the induction of silent ribosomes, elevated temperatures reduce the overall rate of mRNA-ribosome association with few exceptions. Notably, heat shock promotes the ribosomal association of transcripts encoding heat shock proteins, without extension of the half-lives of these mRNAs. These mechanisms dynamically reorganize mRNA turnover to prioritize the translation of heat shock proteins over other proteins.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Global quantification of mammalian gene expression control
Schwanhäusser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., Chen, W., & Selbach, M. (2011) · Nature · doi:10.1038/nature10098 · Cited by 6,566
Flagged first, then by citations
Research works printed but not linked: 66
- Wang, 2022, Rapid 40S scanning and its regulation by mRNA structure during eukaryotic translation initiation, Cell, 185, 4474, 10.1016/j.cell.2022.10.005 · DOI
- Berthelot, 2004, Dynamics and processivity of 40S ribosome scanning on mRNA in yeast, Mol. Microbiol., 51, 987, 10.1046/j.1365-2958.2003.03898.x · DOI
- Hu, 2009, Co-translational mRNA decay in Saccharomyces cerevisiae, Nature, 461, 225, 10.1038/nature08265 · DOI
- Tuck, 2020, Mammalian RNA Decay Pathways Are Highly Specialized and Widely Linked to Translation, Mol. Cell, 77, 1222, 10.1016/j.molcel.2020.01.007 · DOI
- Tomecki, 2023, SKI complex: A multifaceted cytoplasmic RNA exosome cofactor in mRNA metabolism with links to disease, developmental processes, and antiviral responses, Wiley Interdiscip. Rev. RNA, 14, 10.1002/wrna.1795 · DOI · Paper page
- Heyer, 2016, Redefining the Translational Status of 80S Monosomes, Cell, 164, 757, 10.1016/j.cell.2016.01.003 · DOI
- Biever, 2020, Monosomes actively translate synaptic mRNAs in neuronal processes, Science, 367, 10.1126/science.aay4991 · DOI
- Rahaman, 2023, Polysome propensity and tunable thresholds in coding sequence length enable differential mRNA stability, Sci. Adv., 9, 10.1126/sciadv.adh9545 · DOI
- Bae, 2022, Codon optimality-mediated mRNA degradation: Linking translational elongation to mRNA stability, Mol. Cell, 82, 1467, 10.1016/j.molcel.2022.03.032 · DOI
- Shalgi, 2013, Widespread Regulation of Translation by Elongation Pausing in Heat Shock, Mol. Cell, 49, 439, 10.1016/j.molcel.2012.11.028 · DOI
- Hernandez-Elvira, 2022, Post-transcriptional regulation during stress, FEMS Yeast Res., 22, 10.1093/femsyr/foac025 · DOI
- Cherkasov, 2015, Systemic control of protein synthesis through sequestration of translation and ribosome biogenesis factors during severe heat stress, FEBS Lett., 589, 3654, 10.1016/j.febslet.2015.10.010 · DOI
- Becskei, 2022, The life and death of RNA across temperatures, Comput. Struct. Biotechnol. J., 20, 4325, 10.1016/j.csbj.2022.08.008 · DOI
- Merret, 2015, Heat-induced ribosome pausing triggers mRNA co-translational decay in Arabidopsis thaliana, Nucleic Acids Res., 43, 4121, 10.1093/nar/gkv234 · DOI
- Meier, 2006, Sphingoid base is required for translation initiation during heat stress in Saccharomyces cerevisiae, Mol. Biol. Cell, 17, 1164, 10.1091/mbc.e05-11-1039 · DOI
- Muhlhofer, 2019, The Heat Shock Response in Yeast Maintains Protein Homeostasis by Chaperoning and Replenishing Proteins, Cell Rep., 29, 4593, 10.1016/j.celrep.2019.11.109 · DOI
- Smith, 2022, The space between notes: emerging roles for translationally silent ribosomes, Trends Biochem. Sci., 47, 477, 10.1016/j.tibs.2022.02.003 · DOI
- Krokowski, 2011, Characterization of hibernating ribosomes in mammalian cells, Cell Cycle, 10, 2691, 10.4161/cc.10.16.16844 · DOI
- Gomez Ramos, 2016, Yeast rRNA Expansion Segments: Folding and Function, J. Mol. Biol., 428, 4048, 10.1016/j.jmb.2016.08.008 · DOI
- Krauer, 2021, tRNA Synthetases Are Recruited to Yeast Ribosomes by rRNA Expansion Segment 7L but Do Not Require Association for Functionality, Noncoding. RNA, 7
- Cui, 2021, Regulation of ex-translational activities is the primary function of the multi-tRNA synthetase complex, Nucleic Acids Res., 49, 3603, 10.1093/nar/gkaa1183 · DOI
- Bresson, 2020, Stress-Induced Translation Inhibition through Rapid Displacement of Scanning Initiation Factors, Mol. Cell, 80, 470, 10.1016/j.molcel.2020.09.021 · DOI
- Wang, 2018, Multi-protein bridging factor 1(Mbf1), Rps3 and Asc1 prevent stalled ribosomes from frameshifting, eLife, 7, 10.7554/eLife.39637 · DOI
- Shetty, 2023, TORC1 phosphorylates and inhibits the ribosome preservation factor Stm1 to activate dormant ribosomes, EMBO J., 42, 10.15252/embj.2022112344 · DOI · Paper page
- Wells, 2020, Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes, PLoS Biol., 18, 10.1371/journal.pbio.3000780 · DOI
- van den Elzen, 2014, Dom34-Hbs1 mediated dissociation of inactive 80S ribosomes promotes restart of translation after stress, EMBO J., 33, 265, 10.1002/embj.201386123 · DOI
- Wang, 2018, Lso2 is a conserved ribosome-bound protein required for translational recovery in yeast, PLoS Biol., 16, 10.1371/journal.pbio.2005903 · DOI
- Wegener, 2022, The mutual interaction of glycolytic enzymes and RNA in post-transcriptional regulation, RNA, 28, 1446, 10.1261/rna.079210.122 · DOI
- Matia-Gonzalez, 2021, Oxidative stress induces coordinated remodeling of RNA-enzyme interactions, iScience, 24, 10.1016/j.isci.2021.102753 · DOI
- Glauninger, 2024, Transcriptome-wide mRNA condensation precedes stress granule formation and excludes stress-induced transcripts, bioRxiv
- Dea, 2024, The Heat Shock Response as a Condensate Cascade, J. Mol. Biol., 436, 10.1016/j.jmb.2024.168642 · DOI
- Jain, 2016, ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure, Cell, 164, 487, 10.1016/j.cell.2015.12.038 · DOI
- Kato, 2011, Severe ethanol stress induces assembly of stress granules in Saccharomyces cerevisiae, Yeast, 28, 339, 10.1002/yea.1842 · DOI
- Grousl, 2022, Yeast stress granules at a glance, Yeast, 39, 247, 10.1002/yea.3681 · DOI
- Jaquet, 2022, Determinants of the temperature adaptation of mRNA degradation, Nucleic Acids Res., 50, 1092, 10.1093/nar/gkab1261 · DOI
- Eshleman, 2020, Alterations of signaling pathways in response to chemical perturbations used to measure mRNA decay rates in yeast, RNA, 26, 10, 10.1261/rna.072892.119 · DOI
- Duffy, 2019, Gaining insight into transcriptome-wide RNA population dynamics through the chemistry of 4-thiouridine, Wiley Interdiscip. Rev. RNA, 10, 10.1002/wrna.1513 · DOI
- Balagopal, 2009, Polysomes, P bodies and stress granules: states and fates of eukaryotic mRNAs, Curr. Opin. Cell Biol., 21, 403, 10.1016/j.ceb.2009.03.005 · DOI
- Riback, 2017, Stress-Triggered Phase Separation Is an Adaptive, Evolutionarily Tuned Response, Cell, 168, 1028, 10.1016/j.cell.2017.02.027 · DOI
- Grousl, 2013, Heat shock-induced accumulation of translation elongation and termination factors precedes assembly of stress granules in S. cerevisiae, PLoS One, 8, 10.1371/journal.pone.0057083 · DOI
- Popper, 2024, Ribosome inactivation regulates translation elongation in neurons, J. Biol. Chem., 300, 10.1016/j.jbc.2024.105648 · DOI
- Leesch, 2023, A molecular network of conserved factors keeps ribosomes dormant in the egg, Nature, 613, 712, 10.1038/s41586-022-05623-y · DOI
- Blandy, 2025, Translational activity of 80S monosomes varies dramatically across different tissues, Nucleic Acids Res., 53, 10.1093/nar/gkaf292 · DOI
- Wada, 2018, Stochastic Gene Choice during Cellular Differentiation, Cell Rep., 24, 3503, 10.1016/j.celrep.2018.08.074 · DOI
- Mondal, 2024, Gene choice in cancer cells is exclusive in ion transport but concurrent in DNA replication, Comput. Struct. Biotechnol. J., 23, 2534, 10.1016/j.csbj.2024.06.004 · DOI
- Holt, 2024, Biological Roles of Local Protein Synthesis in Axons: A Journey of Discovery, Annu. Rev. Genet., 58, 1, 10.1146/annurev-genet-072220-030822 · DOI
- Zid, 2014, Promoter sequences direct cytoplasmic localization and translation of mRNAs during starvation in yeast, Nature, 514, 117, 10.1038/nature13578 · DOI
- Iserman, 2020, Condensation of Ded1p Promotes a Translational Switch from Housekeeping to Stress Protein Production, Cell, 181, 818, 10.1016/j.cell.2020.04.009 · DOI
- Bonner, 2000, Complex regulation of the yeast heat shock transcription factor, Mol. Biol. Cell, 11, 1739, 10.1091/mbc.11.5.1739 · DOI
- Hjorth-Sorensen, 2001, Activation of heat shock transcription factor in yeast is not influenced by the levels of expression of heat shock proteins, Mol. Microbiol., 39, 914, 10.1046/j.1365-2958.2001.02279.x · DOI
- Christiano, 2014, Global proteome turnover analyses of the Yeasts S. cerevisiae and S. pombe, Cell Rep., 9, 1959, 10.1016/j.celrep.2014.10.065 · DOI · Paper page
- Tesina, 2019, Structure of the 80S ribosome-Xrn1 nuclease complex, Nat. Struct. Mol. Biol., 26, 275, 10.1038/s41594-019-0202-5 · DOI
- Love, 2014, Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2, Genome Biol., 15, 550, 10.1186/s13059-014-0550-8 · DOI · Paper page
- Patro, 2017, Salmon provides fast and bias-aware quantification of transcript expression, Nat. Methods, 14, 417, 10.1038/nmeth.4197 · DOI · Paper page
- Ingolia, 2019, Ribosome Profiling: Global Views of Translation, Cold Spring Harb. Perspect. Biol., 11, 10.1101/cshperspect.a032698 · DOI
- Santos, 2019, Cycloheximide can distort measurements of mRNA levels and translation efficiency, Nucleic Acids Res., 47, 4974, 10.1093/nar/gkz205 · DOI
- Sharma, 2021, Combinations of slow-translating codon clusters can increase mRNA half-life in Saccharomyces cerevisiae, Proc. Natl. Acad. Sci. USA, 118, 10.1073/pnas.2026362118 · DOI
- Lahtvee, 2017, Absolute Quantification of Protein and mRNA Abundances Demonstrate Variability in Gene-Specific Translation Efficiency in Yeast, Cell Syst., 4, 495, 10.1016/j.cels.2017.03.003 · DOI · Paper page
- Ho, 2018, Unification of Protein Abundance Datasets Yields a Quantitative Saccharomyces cerevisiae Proteome, Cell Syst., 6, 192, 10.1016/j.cels.2017.12.004 · DOI
- Nagalakshmi, 2008, The transcriptional landscape of the yeast genome defined by RNA sequencing, Science, 320, 1344, 10.1126/science.1158441 · DOI · Paper page
- Jiko, 2024, Large-scale column-free purification of bovine F-ATP synthase, J. Biol. Chem., 300, 10.1016/j.jbc.2023.105603 · DOI
- Samarao, 2009, V H+-ATPase along the yeast secretory pathway: energization of the ER and Golgi membranes, Biochim. Biophys. Acta, 1788, 303, 10.1016/j.bbamem.2008.11.006 · DOI
- Sherman, 2022, DAVID: a web server for functional enrichment analysis and functional annotation of gene lists (2021 update), Nucleic Acids Res., 50, W216, 10.1093/nar/gkac194 · DOI
- Lugowski, 2018, DRUID: a pipeline for transcriptome-wide measurements of mRNA stability, RNA, 24, 623, 10.1261/rna.062877.117 · DOI
- Duffy, 2015, Tracking Distinct RNA Populations Using Efficient and Reversible Covalent Chemistry, Mol. Cell, 59, 858, 10.1016/j.molcel.2015.07.023 · DOI
- Wada, 2017, Impact of Methods on the Measurement of mRNA Turnover, Int. J. Mol. Sci., 18, 10.3390/ijms18122723 · DOI · Paper page
Metadata
- Authors
- Rahaman, S., Schiffelholz, N., Mittal, N., Fröhlich, K. E., Zavolan, M., & Becskei, A.
- Affiliations
- University of Basel (CH)
- Corresponding author
- Becskei, Attila
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2025-10
- Volume
- 44
- Issue
- 10
- Pages
- 116447
- ISSN
- 2211-1247 (ISSN-L)
- OpenAlex
- W4415305008
- Cited by
- 9
- References
- 1
- Citations by year
- 2026: 6 · 2025: 3
- FWCI
- 2.72
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Cell Reports (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- Swiss National Science Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- heat shock, monosomes, polysomes, mRNA turnover, heat shock proteins, translational reprogramming, stress adaptation, yeast
- MeSH terms
- Heat-Shock Proteins, Polyribosomes, Ribosomes, RNA, Messenger, Saccharomyces cerevisiae, Protein Biosynthesis, Heat-Shock Response, RNA Stability, Saccharomyces cerevisiae Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review