The Heat Shock Response in Yeast Maintains Protein Homeostasis by Chaperoning and Replenishing Proteins.

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ID: 76120
2019
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Abstract
Life is resilient because living systems are able to respond to elevated temperatures with an ancient gene expression program called the heat shock response (HSR). In yeast, the transcription of hundreds of genes is upregulated at stress temperatures. Besides stress protection conferred by chaperones, the function of the majority of the upregulated genes under stress has remained enigmatic. We show that those genes are required to directly counterbalance increased protein turnover at stress temperatures and to maintain the metabolism. This anaplerotic reaction together with molecular chaperones allows yeast to efficiently buffer proteotoxic stress. When the capacity of this system is exhausted at extreme temperatures, aggregation processes stop translation and growth pauses. The emerging concept is that the HSR is modular with distinct programs dependent on the severity of the stress.
Reference Key
muhlhofer2019thecell Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Mühlhofer, Moritz;Berchtold, Evi;Stratil, Chris G;Csaba, Gergely;Kunold, Elena;Bach, Nina C;Sieber, Stephan A;Haslbeck, Martin;Zimmer, Ralf;Buchner, Johannes;
Journal Cell reports
Year 2019
DOI
S2211-1247(19)31632-8
URL
Keywords
Mass spectrometry protein aggregation transcriptome proteome s. cerevisiae chaperones heat shock response ribosome profiling translatome

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