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The heat shock response in yeast is modular and maintains protein homeostasis via distinct mechanisms

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 and Q-Exactive Plus (both Thermo) mass spectrometer, respectively. 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.

INSTRUMENT(S): Orbitrap Fusion, Q Exactive Plus

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

SUBMITTER: Moritz Mühlhofer

LAB HEAD: Johannes Buchner

PROVIDER: PXD014189 | Pride | 2019-12-25

REPOSITORIES: Pride

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			Action	DRS
	20180322_MM_37.raw	Raw
	20180322_MM_38.raw	Raw
	20180322_MM_39.raw	Raw
	20180322_MM_40.raw	Raw
	20180322_MM_41.raw	Raw

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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]

PMID: 31875563

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

Project description: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.

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Co-targeting HSP90 alpha and CDK7 overcomes resistance against HSP90 inhibitors in BCR-ABL1+ leukemia cells

Project description:HSP90 inhibitors (HSP90i) have not entered routinely in the clinics, primarily due to the associated resistance via heat shock response (HSR) induction and dose limiting toxicity. In this study, we employed genetic KO and knockdown (KD) models of HSP90 isoforms (α and β) for extensive multi-omics-based in vitro and in vivo characterization and identified HSP90α as the primary driver of malignancy of the two isoforms in BCR-ABL1+ leukemia cells. Notably, combinatorial ex vivo drug sensitivity screenings identified CDK7 inhibitors (CDK7i) as drugs synergizing with HSP90α inhibition.

2024-01-26 | PXD041871 | Pride

Multi-facetted proteomics of mitochondrial TMBIM5 deficient cell lines: Regulation of mitochondrial proteostasis by the proton gradient

Project description:Mitochondria adapt to different energetic demands reshaping their proteome. Mitochondrial proteases are emerging as key regulators of these adaptive processes. Here, we use a multi-proteomic approach to demonstrate regulation of the m-AAA protease AFG3L2 by the mitochondrial proton gradient, coupling mitochondrial protein turnover to the energetic status of mitochondria. We identify TMBIM5 (previously also known as GHITM or MICS1) as a Ca2+/H+ exchanger in the mitochondrial inner membrane, which binds to and inhibits the m-AAA protease. TMBIM5 ensures cell survival and respiration, allowing Ca2+ efflux from mitochondria and limiting mitochondrial hyperpolarization. Persistent hyperpolarization, however, triggers degradation of TMBIM5 and activation of the m-AAA protease. The m-AAA protease broadly remodels the mitochondrial proteome and mediates the proteolytic breakdown of respiratory complex I to confine ROS production and oxidative damage in hyperpolarized mitochondria. TMBIM5 thus integrates mitochondrial Ca2+ signaling and the energetic status of mitochondria with protein turnover rates to reshape the mitochondrial proteome and adjust the cellular metabolism.

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Proteome Profiling of Polyomavirus Nuclear Replication Centers Using iPOND

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2024-10-07 | PXD055210 | Pride

Genomewide measurements of neural-specific mRNA decay in Drosophila embryos

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Subcellular localization of the J-protein Sis1 regulates the heat shock response

Project description:How heat shock inducesthe heat shock response (HSR) – a gene expression program encoding chaperones and other protein homeostasis (proteostasis) factors –remains an unresolved question in eukaryotic cell biology. Here we show that subcellular localization of the conserved J-protein Sis1 is a key regulator of the HSRin yeast. Under nonstress conditions, nucleoplasmic Sis1 promotes interaction between the chaperone Hsp70 and the transcription factor Hsf1to repress the HSR. Heat shock triggers Sis1 to localize to the nucleolar periphery and condense on the ER surface with the ribosome quality control complex. Sis1 recruits the proteasome to this spatial network.Through localization dynamics, Sis1 relaysthe condition of the proteome to Hsf1.Thus, the activation state of the HSR is built into spatial organization of the proteostasis network.

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