Assessment of Thermotolerance in preshocked hsp70(-/-) and (+/+) cells
Ontology highlight
ABSTRACT:
ORGANISM(S): Mus musculus
PROVIDER: GSE11120 | GEO | 2009/04/09
SECONDARY ACCESSION(S): PRJNA107019
REPOSITORIES: GEO
Similar Datasets
Project description:From preliminary experiments, HSP70 deficient MEF cells display moderate thermotolerance to a severe heatshock of 45.5 degrees after a mild preshock at 43 degrees, even in the absence of hsp70 protein. We would like to determine which genes in these cells are being activated to account for this thermotolerance. Experiment Overall Design: Two cell lines are analyzed - hsp70 knockout and hsp70 rescue cells. 6 microarrays from the (-/-)knockout cells are analyzed (3 Pretreated vs 3 unheated controls). For the (+/+) rescue cells, 4 microarrays are used (2 pretreated and 2 unheated controls). Cells were plated at 3k/well in a 96 well plate, covered with a gas permeable sealer and heat shocked at 43degrees for 30 minutes at the 20 hr time point. The RNA was harvested at 3hrs after heat treatment.
2009-04-17 | E-GEOD-11120 | biostudies-arrayexpress
Project description:Temperature has a major role in plant growth and survival, for example wheat yields decrease by about 6% for every 1°C rise in global temperature [1]. High temperatures induce the expression of protective chaperones and modulate growth responses. Key players in the heat protection response are transcription factors of the HEAT SHOCK FACTOR A1 (HSFA1) family [2]. However the pathways that activate the HSFA1 class TFs, and how these perceive temperature and integrate it with other environmental signals are not clear. Plants are exposed to considerable diurnal temperature variation, and have evolved pathways to anticipate likely future conditions. For example, the cold response pathway is gated by the circadian clock, enabling the degree of responsiveness to cold to be controlled in the context of the environment [3, 4] and genes promoting elongation growth and flowering in response to warm temperature are induced during the night via thermosensory phytochromes [5 ,6]. It is not known in Arabidopsis if the warm temperature protective pathways are gated. In this study we find that there is strong diurnal variation in the heat stress response of Arabidopsis, and we show that this correlates with the expression of HSP70 in the day night cycle. The dark to light transition is in fact sufficient to robustly induce expression of warm temperature protective genes such as HSP70. A forward genetic screen with a HSP70-Luciferase reporter line revealed genes necessary for controlling this process and identified a central role for chloroplast signalling in the warm temperature response that accounts for diurnal variation in thermotolerance.
2018-02-13 | GSE96041 | GEO
Project description:We have been determining signalling components essential for heat tolerance in Arabidopsis thaliana (Larkindale, J., and Knight, M.R. (2002). Protection against heat stress-induced oxidative damage in Arabidopsis involves calcium, abscisic acid, ethylene, and salicylic acid. Plant Physiol 128, 682-695). We have most recently found that a heat-induced respiratory burst is necessary for tolerance to high temperatures in Arabidopsis (Larkindale, Torres, Jones and Knight, unpublished). We have observed that one of the Arabidopsis respiratory burst homologues, AtrbohB, is necessary for the generation of this AOS burst in response to heat, and consequently we have also found that an AtrbohB null mutant shows reduced tolerance to heating (Larkindale, Torres, Jones and Knight, unpublished). This mutant also shows reduced expression of genes from the HSP90 family (Evans, Larkindale and Knight, unpublished).This application is for transcriptomic analysis of the AtrbohB null mutant in response to heat, in order to understand which genes are activated as a result of heat-induced respiratory bursts in Arabidopsis and also which genes are necessary for physiological thermotolerance in Arabidopsis. The experiment will involve 6 samples (chips), 3 from wild type Columbia and 3 from the AtrbohB null mutant. Seedlings will be treated at 20, 30 and 40 degrees centigrade for 1 hour, RNA extracted and submitted to microarray analysis. One hour treatment has been shown to display clear differences in HSP90 expression and physiological damage, and the temperatures chosen because 30 degrees is a temperature at which acquired thermotolerance can be initiated (thus genes involved in this process can be monitored) and 40 degrees is a temperature at which we observe physiological damage, and gives good discrimination between mutant and wild type. Keywords: strain_or_line_design
2007-01-22 | GSE6154 | GEO
Project description:Thermotolerance is a crucial virulence attribute for Cryptococcus neoformans, which causes fatal fungal meningitis in humans. A protein kinase, Sch9, suppresses the thermotolerance of C. neoformans but its regulatory mechanism remains unknown. Here we elucidated the Sch9-dependent and -independent signaling networks for modulating the thermotolerance of C. neoformans through a genome-wide transcriptome analysis and reverse genetics approaches. We found that more than 1,800 genes were under transcriptional control during temperature upshift. Genes encoding for molecular chaperones and heat shock proteins were mainly upregulated, while those for translation, transcription, and sterol biosynthesis were highly suppressed. In this process Sch9 was found to regulate basal or induced expression levels of some temperature-responsive genes. Interestingly we found that Sch9 was involved in transcriptional regulation of the Ire1 kinase, which is a key sensor for the unfolded protein response pathway, and was found to be involved in ER stress response. Most notably, our data demonstrated that expression of HSF1, encoding a heat shock transcription factor 1, was downregulated during temperature upshift and Sch9 suppresses its downregulation. In spite of such expression patterns, Hsf1 was essential for growth and its overexpression indeed promoted the thermotolerance of C. neoformans, suggesting dual roles of Hsf1 in thermotolerance. This idea was supported by additional transcriptome analysis with HSF1 overexpression strain, which revealed that Hsf1 served as both activator and repressor. Hsf1 promoted genes such as Hsp104 and Hsp70 (Ssa1 and Ssa2), both of which were found to be highly upregulated during temperature upshift and required for thermotolerance, while Hsf1 repressed genes involved in oxidative stress and thermotolerance.
2015-06-01 | GSE66508 | GEO
Project description:Thermotolerance is a crucial virulence attribute for Cryptococcus neoformans, which causes fatal fungal meningitis in humans. A protein kinase, Sch9, suppresses the thermotolerance of C. neoformans but its regulatory mechanism remains unknown. Here we elucidated the Sch9-dependent and -independent signaling networks for modulating the thermotolerance of C. neoformans through a genome-wide transcriptome analysis and reverse genetics approaches. We found that more than 1,800 genes were under transcriptional control during temperature upshift. Genes encoding for molecular chaperones and heat shock proteins were mainly upregulated, while those for translation, transcription, and sterol biosynthesis were highly suppressed. In this process Sch9 was found to regulate basal or induced expression levels of some temperature-responsive genes. Interestingly we found that Sch9 was involved in transcriptional regulation of the Ire1 kinase, which is a key sensor for the unfolded protein response pathway, and was found to be involved in ER stress response. Most notably, our data demonstrated that expression of HSF1, encoding a heat shock transcription factor 1, was downregulated during temperature upshift and Sch9 suppresses its downregulation. In spite of such expression patterns, Hsf1 was essential for growth and its overexpression indeed promoted the thermotolerance of C. neoformans, suggesting dual roles of Hsf1 in thermotolerance. This idea was supported by additional transcriptome analysis with HSF1 overexpression strain, which revealed that Hsf1 served as both activator and repressor. Hsf1 promoted genes such as Hsp104 and Hsp70 (Ssa1 and Ssa2), both of which were found to be highly upregulated during temperature upshift and required for thermotolerance, while Hsf1 repressed genes involved in oxidative stress and thermotolerance.
2015-06-01 | GSE66509 | GEO
Project description:Investigation of whole genome gene expression level in E. coli K-12 MG1655 in glucose M9 minimal media with/without heatshock
2013-06-20 | GSE42675 | GEO
Project description:During thermotolerance development, B. subtilis cells can be primed by a short mild heat shock to survive a subsequent severe, otherwise lethal, heat stress. We wanted to assess the influence of transcriptional regulation during thermotolerance development in B. subtilis. We prepared total RNA of four differently treated samples of B. subtilis cells. For this purpose, exponential B. subtilis cells grown at 37 °C were divided and exposed for additional 15 min to temperatures of 37 °C, 48 °C, 53 °C or 15 min 48 °C followed by 15 min at 53 °C.
2014-05-01 | GSE45972 | GEO
Project description:Heterogeneous Tg(hsp70-hRASG12V) embryos were obtained by mating the male homozygous transgenic fish to wildtype females. They were raised to 24 hour-post fertilization (hpf) stage and received heatshock at 37°C in waterbath for one hour, and kept in 28.5°C till 30hpf for RNA extraction. Wildtype embryos receiving the same heatshock treatment were used as controls. Each microarray sample was prepared by pooling 50 embryos and biological duplication was used.
2013-02-16 | GSE44364 | GEO
Project description:Investigation of whole genome gene expression level in E. coli K-12 MG1655 in glucose M9 minimal media with/without heatshock A six chip study using total RNA recovered from E. coli K-12 MG1655 grown up to OD600nm 0.6 (mid-exponential phase) in M9 minimal media supplemented with 0.2% glucose with/without heatshock in 42oC. The high-density oligonucleotide tiling arrays used were consisted of 371,034 oligonucleotide probes with 50-bp length that are spaced 25 bp apart across the E. coli genome (NimbleGen). Experiments were performed with three biological replicates.
2013-06-20 | E-GEOD-42675 | biostudies-arrayexpress
Project description:Exposure to heat stress triggers a well-defined acute response marked by HSF1-dependent transcriptional upregulation of heat shock proteins. Cells allowed to recover acquire thermotolerance, but this adaptation is poorly understood. By quantitative proteomics, we discovered selective upregulation of HSP70-family chaperone HSPA1 and its co-factors, HSPH1 and DNAJB1, in MCF7 breast cancer cells acquiring thermotolerance. HSPA1 was found to have dual function during heat stress response: (i) during acute stress, it promotes the recruitment of the 26S proteasome to translating ribosomes, thus poising cells for rapid protein degradation and resumption of protein synthesis upon recovery; (ii) during thermotolerance, HSPA1 together with HSPH1 maintains ubiquitylated nascent/newly synthesized proteins in a soluble state required for their efficient proteasomal clearance. Consistently, deletion of HSPH1 impedes thermotolerance and esophageal tumor growth in mice, thus providing a potential explanation for the poor prognosis of digestive tract cancers with low HSPH1, and nominating HSPH1 as a cancer drug target. We propose dual roles of HSPA1 either alone or in complex with HSPH1 and DNAJB1 in promoting quality control of nascent/newly synthesized proteins and cellular thermotolerance.
2021-05-02 | PXD025123 | Pride