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Genetic inactivation of essential HSF1 reveals an isolated transcriptional stress response selectively induced by protein misfolding

ABSTRACT: Genetic inactivation of essential HSF1 reveals an isolated transcriptional stress response selectively induced by protein misfolding

PROVIDER: PRJNA971591 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR24510300_1.fastq.gz	Fastqsanger.gz
	SRR24510300_2.fastq.gz	Fastqsanger.gz
	SRR24510301_1.fastq.gz	Fastqsanger.gz
	SRR24510301_2.fastq.gz	Fastqsanger.gz
	SRR24510302_1.fastq.gz	Fastqsanger.gz

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Similar Datasets

Genetic inactivation of essential HSF1 reveals an isolated transcriptional stress response selectively induced by protein misfolding

Project description:Heat Shock Factor 1 (Hsf1) in yeast drives the basal transcription of key proteostasis factors and its activity is induced as part of the core heat shock response. In this study we stringently test the role of Hsf1 under basal and stress conditions using a newly constructed hsf1∆ strain. To assess how cells mount transcriptional stress responses when Hsf1 is inactivated, we performed mRNA-sequencing (mRNA-seq) upon hear shock (HS) or treatment with azetidine-2-carboxylic acid (AzC).

2023-05-16 | GSE232311 | GEO

Genetic inactivation of essential <i>HSF1</i> reveals an isolated transcriptional stress response selectively induced by protein misfolding.

Project description:Heat Shock Factor 1 (Hsf1) in yeast drives the basal transcription of key proteostasis factors and its activity is induced as part of the core heat shock response. Exploring Hsf1 specific functions has been challenging due to the essential nature of the HSF1 gene and the extensive overlap of target promoters with environmental stress response (ESR) transcription factors Msn2 and Msn4 (Msn2/4). In this study, we constructed a viable hsf1∆ strain by replacing the HSF1 open reading frame with genes that constitutively express Hsp40, Hsp70, and Hsp90 from Hsf1-independent promoters. Phenotypic analysis showed that the hsf1∆ strain grows slowly, is sensitive to heat as well as protein misfolding and accumulates protein aggregates. Transcriptome analysis revealed that the transcriptional response to protein misfolding induced by azetidine-2-carboxylic acid is fully dependent on Hsf1. In contrast, the hsf1∆ strain responded to heat shock through the ESR. Following HS, Hsf1 and Msn2/4 showed functional compensatory induction with stronger activation of the remaining stress pathway when the other branch was inactivated. Thus, we provide a long-overdue genetic test of the function of Hsf1 in yeast using the novel hsf1∆ construct. Our data highlight that the accumulation of misfolded proteins is uniquely sensed by Hsf1-Hsp70 chaperone titration inducing a highly selective transcriptional stress response.

| S-EPMC10551698 | biostudies-literature

Yeast HSF1 vs hsf1-ba1

Project description:Upon heat shock, Hsf1 protein is extensively phosphorylated, however, this modification is inhibited by an hsf1-bal mutation. To get genome-wide effect of the hyperphosphorylation on Hsf1-regulated transcription, the heat-induced gene expression profiles in HSF1 and hsf1-bal cells were compared. Keywords: stress response

2005-09-27 | GSE3361 | GEO

hsf1

Project description:Schizosaccharomyces pombe hsf1, transcription factor Hsf1 [Source:PomBase;Acc:SPAC2E12.02], is differentially expressed in 1 experiment(s);

| SPAC2E12.02 | ExpressionAtlas

Defining the Essential Function of Yeast Hsf1 Reveals a Compact Transcriptional Program for Maintaining Eukaryotic Proteostasis

Project description:We used the conditional chemical genetics approach known as “anchor away” (AA) to rapidly inactivate the essential yeast transcription factor Hsf1. We coupled Hsf1-AA to RNA-seq and NET-seq to define the genes whose expression depends on Hsf1 and performed Hsf1-3xFLAG-V5 ChIP-seq to validate direct targets. We also carried out a number of other perturbations to yeast stress pathways to show that most of the gene expression changes during heat shock are Hsf1-independent but depend on PKA signaling and the Msn2/4 general stress transcription factors. Finally, we generated RNA-seq in mouse ES cells and MEFs in wild type and hsf1-/- cells to define HSF1 targets in murine cells.

2018-01-11 | GSE108736 | GEO

Identification of genes regulated by human HSF1, chicken HSF1 and chicken HSF3

Project description:To examine whether human HSF1, chicken HSF1 and chicken HSF3 regulates the expression of different genes, we performed DNA microarray analysis.

2024-09-18 | GSE262549 | GEO

Transcription profiling of mouse HSF1+/+ and HSF1-/- fibroblasts heat shock time series

Project description:Mouse HSF1+/+ and HSF1-/- Fibroblasts Heat Shock Time Courses Scanned on Scanner 7 (Axon 4000B)

2005-07-21 | E-SMDB-1853 | biostudies-arrayexpress

yeast hsf1-R206S/F256S mutant

Project description:Effect of hsf1-R206S/F256S mutation on heat-induced transcription of genes is analyzed. Total RNA was isolated from HSF1 wild type and hsf1-R206S/F256S cells grown at 39oC for 15 min. Probe cDNA was primed by oligo(dT) and was synthesized in the presence of 33P-dCTP. Hybridization was carried out using the same GF100 GeneFilter. Value higher than 30 in HSF1 wild type cells is confident. Values from duplicate experiments were averaged, and the average fold changes were calculated. Keywords = yeast Keywords = HSF1 Keywords: other

2004-12-24 | GSE2103 | GEO

Excess protein synthesis, denatured proteins or molecular crowding spontaneously induce HSF1 trimerisation and activation

Project description:Stress responses are a key feature of normal physiology and are usurped by cancer cells to ensure enhanced protein synthesis for growth, to compensate for genomic instability, and to protect cancer cells from therapy induced stress. Heat shock factor-1 (HSF1) is a major stress-response transcription factor, and its activity is markedly enhanced in cancer. Stress induces HSF1 conformational changes and post-translational modifications, leading to assembly of active HSF1 trimers that bind DNA to control target gene expression. Although the function of HSF1 in transcription is relatively well-known, the mechanisms leading to HSF1 activation and enhanced stress response in tumours are unclear. To investigate whether HSF1 is a primary sensor of proteotoxic stress in vivo, we studied the range of conditions that can cause HSF1 activation in vitro and in cells, and conditions that prevent its activation. We show that purified recombinant HSF1 adopts a stable monomeric conformation in vitro. Heat stress caused a conformational change and the assembly of HSF1 trimers. Conditions leading to protein denaturation, including heat stress, crowding, Hsp90 inhibition, or proteasome inhibition, all directly lead to HSF1 activation. In contrast, HSF1 activation in vivo is prevented by proteosynthesis inhibition, which reduces the amount of denatured proteins in the cell. These results establish that HSF1 is a direct sensor of proteotoxic stress, independent of post-translational modification, where abrupt environmental changes that cause protein denaturation simultaneously induce a conformational change in monomeric HSF1 leading to its activation. This mechanism explains the universal ability of cells to respond to proteotoxic stress and trigger a protective response when increased chaperone activities are required to restore homeostasis.

2024-08-14 | PXD037662 | Pride

HSF1 Activation Can Restrict HIV Replication

Project description:Host protein folding stress responses can play important roles in RNA virus replication and evolution. Intriguingly, prior work revealed a complicated interplay between the cytosolic proteostasis stress response, controlled by its master regulator heat shock factor 1 (HSF1) and human immunodeficiency virus-1 (HIV-1). We sought to isolate HSF1 transcription factor activity from proteostasis stress and elucidate the function of HSF1 in HIV-1 lifecycle in absence of cellular stress. We used chemical genetic, stress-independent control of HSF1 activity to establish whether and how HSF1 influences HIV-1 replication. Stress-independent HSF1 induction decreased both the total quantity and infectivity of HIV-1 virions. Moreover, HIV-1 was unable to escape HSF1-mediated restriction over the course of several serial passages. These results promote continued consideration of the heat shock response as a potential target for antiviral drugs.

2022-01-30 | GSE137591 | GEO

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