ArticlePloS one2013
Heat shock-induced accumulation of translation elongation and termination factors precedes assembly of stress granules in S. cerevisiae.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 65 citations in OpenAlex.
- Mechanosensor-mediated Hsp70 phosphorylation orchestrates the landscape of the heat shock response.Nature communications · 2025Article
- Transcriptome-wide mRNP condensation precedes stress granule formation and excludes new mRNAs.Molecular cell · 2025Article
- Transcriptome-wide mRNP condensation precedes stress granule formation and excludes new mRNAs.bioRxiv : the preprint server for biology · 2025Article
- Osmotic stress induces formation of both liquid condensates and amyloids by a yeast prion domain.The Journal of biological chemistry · 2024Article
- Adaptive preservation of orphan ribosomal proteins in chaperone-dispersed condensates.Nature cell biology · 2023Article
- The Properties and Domain Requirements for Phase Separation of the Sup35 Prion Protein In Vivo.Biomolecules · 2023Article
- Article
- Stressful steps: Progress and challenges in understanding stress-induced mRNA condensation and accumulation in stress granules.Molecular cell · 2022Review
- eIF3a Destabilization and TDP-43 Alter Dynamics of Heat-Induced Stress Granules.International journal of molecular sciences · 2021Article
- Yeast translation elongation factor eEF3 promotes late stages of tRNA translocation.The EMBO journal · 2021Article
- Deciphering the Proteotoxic Stress Responses Triggered by the Perturbed Thylakoid Proteostasis in Arabidopsis.Plants (Basel, Switzerland) · 2021Article
- Tumor suppressor protein p53 expressed in yeast can remain diffuse, form a prion, or form unstable liquid-like droplets.iScience · 2021Article
- Aggregation and disaggregation features of the human proteome.Molecular systems biology · 2020Article
- Methyltransferase 3 Mediated miRNA m6A Methylation Promotes Stress Granule Formation in the Early Stage of Acute Ischemic Stroke.Frontiers in molecular neuroscience · 2020Article
- Non-translational Connections of eEF1B in the Cytoplasm and Nucleus of Cancer Cells.Frontiers in molecular biosciences · 2020Review
- An aggregation-prone mutant of eIF3a forms reversible assemblies escaping spatial control in exponentially growing yeast cells.Current genetics · 2019Article
- Bioconversion of Beet Molasses to Alpha-Galactosidase and Ethanol.Frontiers in microbiology · 2019Article
- Biomolecular Assemblies: Moving from Observation to Predictive Design.Chemical reviews · 2018Review
- Quantifying Nucleation In Vivo Reveals the Physical Basis of Prion-like Phase Behavior.Molecular cell · 2018Article
- Translational Control by Prion-like Proteins.Trends in cell biology · 2018Review
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In response to severe environmental stresses eukaryotic cells shut down translation and accumulate components of the translational machinery in stress granules (SGs). Since they contain mainly mRNA, translation initiation factors and 40S ribosomal subunits, they have been referred to as dominant accumulations of stalled translation preinitiation complexes. Here we present evidence that the robust heat shock-induced SGs of S. cerevisiae also contain translation elongation factors eEF3 (Yef3p) and eEF1Bγ2 (Tef4p) as well as translation termination factors eRF1 (Sup45p) and eRF3 (Sup35p). Despite the presence of the yeast prion protein Sup35 in heat shock-induced SGs, we found out that its prion-like domain is not involved in the SGs assembly. Factors eEF3, eEF1Bγ2 and eRF1 were accumulated and co-localized with Dcp2 foci even upon a milder heat shock at 42°C independently of P-bodies scaffolding proteins. We also show that eEF3 accumulations at 42°C determine sites of the genuine SGs assembly at 46°C. We suggest that identification of translation elongation and termination factors in SGs might help to understand the mechanism of the eIF2α factor phosphorylation-independent repression of translation and SGs assembly.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.