Proteomics

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The heat shock response relies on orthogonal mechanisms to maintain protein homeostasis in yeast

ABSTRACT: We globally analyzed the heat stress response (HSR) in yeast on the transcriptomic, tranlatomic and the proteomic level. The cells were stressed at 37 °C, 42 °C and 46 °C and the fractionated proteomes measured on a Fusion mass spectrometer. With this approach we were able to reveal a modular character of the HSR dependent on the severity of the stress. We showed that at temperatures up to 42 °C besides upregulation of stress protective factors refilling the pool of degraded and aggregating proteins is an important branch of the HSR. Whereas, at sublethal temperatures (46 °C) lots of aggregation and phase transition processes were observed. This is part two of the pride submission and only contains the proteomic data under inhibition of the proteasome with bortezomib.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Moritz Mühlhofer  

LAB HEAD: Johannes Buchner

PROVIDER: PXD016125 | Pride | 2020-01-07

REPOSITORIES: Pride

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Publications

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

Mühlhofer Moritz M   Berchtold Evi E   Stratil Chris G CG   Csaba Gergely G   Kunold Elena E   Bach Nina C NC   Sieber Stephan A SA   Haslbeck Martin M   Zimmer Ralf R   Buchner Johannes J  

Cell reports 20191201 13

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 temp  ...[more]

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