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Cytoplasmic protein misfolding titrates Hsp70 to activate nuclear Hsf1
Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute. Stockholm University, Science for Life Laboratory (SciLifeLab).
Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
Stockholm University, Faculty of Science, Department of Molecular Biosciences, The Wenner-Gren Institute.
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Number of Authors: 72019 (English)In: eLIFE, E-ISSN 2050-084X, Vol. 8, article id e47791Article in journal (Refereed) Published
Abstract [en]

Hsf1 is an ancient transcription factor that responds to protein folding stress by inducing the heat-shock response (HSR) that restore perturbed proteostasis. Hsp70 chaperones negatively regulate the activity of Hsf1 via stress-responsive mechanisms that are poorly understood. Here, we have reconstituted budding yeast Hsf1-Hsp70 activation complexes and find that surplus Hsp70 inhibits Hsf1 DNA-binding activity. Hsp70 binds Hsf1 via its canonical substrate binding domain and Hsp70 regulates Hsf1 DNA-binding activity. During heat shock, Hsp70 is out-titrated by misfolded proteins derived from ongoing translation in the cytosol. Pushing the boundaries of the regulatory system unveils a genetic hyperstress program that is triggered by proteostasis collapse and involves an enlarged Hsf1 regulon. The findings demonstrate how an apparently simple chaperone-titration mechanism produces diversified transcriptional output in response to distinct stress loads.

Place, publisher, year, edition, pages
2019. Vol. 8, article id e47791
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Biochemistry and Molecular Biology
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URN: urn:nbn:se:su:diva-175704DOI: 10.7554/eLife.47791ISI: 000489554600001PubMedID: 31552827OAI: oai:DiVA.org:su-175704DiVA, id: diva2:1369968
Available from: 2019-11-13 Created: 2019-11-13 Last updated: 2019-11-13Bibliographically approved

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Masser, Anna E.Kang, WenjingRoy, JoydeepQuintana-Cordero, JanyFriedländer, Marc R.Andréasson, Claes
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Department of Molecular Biosciences, The Wenner-Gren InstituteScience for Life Laboratory (SciLifeLab)
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