scholarly journals Heat-responsive and time-resolved transcriptome and metabolome analyses of Escherichia coli uncover thermo-tolerant mechanisms

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Sinyeon Kim ◽  
Youngshin Kim ◽  
Dong Ho Suh ◽  
Choong Hwan Lee ◽  
Seung Min Yoo ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Late Stage ◽  
Full Range ◽  
Thermal Adaptation ◽  
Morphological Plasticity ◽  
Growth Stages ◽  
Time Resolved ◽  
Shock Response

Abstract Current understanding of heat shock response has been complicated by the fact that heat stress is inevitably accompanied by changes in specific growth rates and growth stages. In this study, a chemostat culture was successfully performed to avoid the physico-chemical and biological changes that accompany heatshock, which provided a unique opportunity to investigate the full range of cellular responses to thermal stress, ranging from temporary adjustment to phenotypic adaptation at multi-omics levels. Heat-responsive and time-resolved changes in the transcriptome and metabolome of a widely used E. coli strain BL21(DE3) were explored in which the temperature was upshifted from 37 to 42 °C. Omics profiles were categorized into early (2 and 10 min), middle (0.5, 1, and 2 h), and late (4, 8, and 40 h) stages of heat stress, each of which reflected the initiation, adaptation, and phenotypic plasticity steps of the stress response. The continued heat stress modulated global gene expression by controlling the expression levels of sigma factors in different time frames, including unexpected downregulation of the second heatshock sigma factor gene (rpoE) upon the heat stress. Trehalose, cadaverine, and enterobactin showed increased production to deal with the heat-induced oxidative stress. Genes highly expressed at the late stage were experimentally validated to provide thermotolerance. Intriguingly, a cryptic capsular gene cluster showed considerably high expression level only at the late stage, and its expression was essential for cell growth at high temperature. Granule-forming and elongated cells were observed at the late stage, which was morphological plasticity occurred as a result of acclimation to the continued heat stress. Whole process of thermal adaptation along with the genetic and metabolic changes at fine temporal resolution will contribute to far-reaching comprehension of the heat shock response. Further, the identified thermotolerant genes will be useful to rationally engineer thermotolerant microorganisms.

scholarly journals Molecular Basis of the Defective Heat Stress Response in Mycobacterium leprae

2007 ◽  
Vol 189 (24) ◽  
pp. 8818-8827 ◽  
Author(s):  
Diana L. Williams ◽  
Tana L. Pittman ◽  
Mike Deshotel ◽  
Sandra Oby-Robinson ◽  
Issar Smith ◽  
...  
Keyword(s):  
Heat Stress ◽  
Stress Response ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Elevated Temperatures ◽  
Transcriptional Response ◽  
Mycobacterium Leprae ◽  
Heat Stress Response ◽  
Regulatory Circuits ◽  
Shock Response

ABSTRACT Mycobacterium leprae, a major human pathogen, grows poorly at 37°C. The basis for its inability to survive at elevated temperatures was investigated. We determined that M. leprae lacks a protective heat shock response as a result of the lack of transcriptional induction of the alternative sigma factor genes sigE and sigB and the major heat shock operons, HSP70 and HSP60, even though heat shock promoters and regulatory circuits for these genes appear to be intact. M. leprae sigE was found to be capable of complementing the defective heat shock response of mycobacterial sigE knockout mutants only in the presence of a functional mycobacterial sigH, which orchestrates the mycobacterial heat shock response. Since the sigH of M. leprae is a pseudogene, these data support the conclusion that a key aspect of the defective heat shock response in M. leprae is the absence of a functional sigH. In addition, 68% of the genes induced during heat shock in M. tuberculosis were shown to be either absent from the M. leprae genome or were present as pseudogenes. Among these is the hsp/acr2 gene, whose product is essential for M. tuberculosis survival during heat shock. Taken together, these results suggest that the reduced ability of M. leprae to survive at elevated temperatures results from the lack of a functional transcriptional response to heat shock and the absence of a full repertoire of heat stress response genes, including sigH.

Sub-lethal heat stress causes apoptosis in an Antarctic fish that lacks an inducible heat shock response

2014 ◽  
Vol 44 ◽  
pp. 119-125 ◽  
Author(s):  
Isaac M. Sleadd ◽  
Marissa Lee ◽  
Daniel O. Hassumani ◽  
Tonya M.A. Stecyk ◽  
Otto K. Zeitz ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Antarctic Fish ◽  
Shock Response

scholarly journals Effect of single and repeated heat stress on chemical signals of heat shock response cascade in the rat’s heart

2017 ◽  
Vol 23 (4) ◽  
pp. 561-570 ◽  
Author(s):  
Gordana Ilievska ◽  
Suzana Dinevska-Kjovkarovska ◽  
Biljana Miova
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Chemical Signals ◽  
Shock Response

scholarly journals The heat shock response in HeLa cells is accompanied by elevated expression of the c-fos proto-oncogene.

1987 ◽  
Vol 7 (10) ◽  
pp. 3452-3458 ◽  
Author(s):  
G K Andrews ◽  
M A Harding ◽  
J P Calvet ◽  
E D Adamson
Keyword(s):  
Heavy Metals ◽  
Protein Synthesis ◽  
Heat Stress ◽  
Heat Shock ◽  
Hela Cells ◽  
Heat Shock Response ◽  
Mrna Level ◽  
Hsp 70 ◽  
Shock Response ◽  
Elevated Expression

Several known inducers of the heat shock response (heat stress, arsenite, and heavy metals) were shown to cause a significant elevation of c-fos mRNA in HeLa cells. Heat stress resulted in a time- and temperature-dependent prolonged elevation in the level of c-fos mRNA, which was accompanied by increased translation of c-fos protein and its appearance in the nucleus. Elevated expression of c-fos during heat stress was paralleled by induction of hsp 70 mRNA, while levels of c-myc and metallothionein mRNAs declined. Treatment of HeLa cells with arsenite or heavy metals also resulted in increased levels of hsp 70, as well as c-fos mRNA. Although elevated expression of c-fos was prevented by inhibitors of RNA synthesis, analysis of relative rates of gene transcription showed that during heat stress there was a negligible change in c-fos transcription. Therefore, the enhanced expression of c-fos during the heat shock response is likely to occur primarily through posttranscriptional processes. Cycloheximide was also shown to significantly increase the c-fos mRNA level in HeLa cells. There results are consistent with the observation that these inducers of the heat shock response, as well as cycloheximide, repress protein synthesis and suggest that the increase in the level of c-fos mRNA is caused by an inhibition of protein synthesis. This supports the hypothesis that c-fos mRNA is preferentially stabilized under conditions which induce the heat shock response, perhaps by decreased synthesis of a short-lived protein which regulates c-fos mRNA turnover.

Thermal adaptation and heat shock response ofTilapia ovary cells

1988 ◽  
Vol 134 (2) ◽  
pp. 189-199 ◽  
Author(s):  
J. Don Chen ◽  
F. H. Yew ◽  
Gloria C. Li
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Thermal Adaptation ◽  
Ovary Cells ◽  
Shock Response

The Heat-Shock Response and Expression of Heat-Shock Proteins in Wheat Under Diurnal Heat Stress and Field Conditions

1994 ◽  
Vol 21 (6) ◽  
pp. 857 ◽  
Author(s):  
HT Nguyen ◽  
CP Joshi ◽  
N Klueva ◽  
J Weng ◽  
KL Hendershot ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Tolerance ◽  
Heat Shock Response ◽  
Field Conditions ◽  
Shock Response ◽  
Heat Tolerant ◽  
Shock Proteins

The occurrence of heat-shock proteins (HSPs) in response to high temperature stress is a universal phenomenon in higher plants and has been well documented. However, in agriculturally important species, less is known about the expression of HSPs under natural environments. A review of the heat-shock response in wheat (Triticum aestivum L.) is presented and recent results on the expression of wheat HSPs under diurnal stress and field conditions are reported. In the field experiment, flag leaf blade temperatures were obtained and leaf blades collected for northern blot analysis using HSP 16.9 cDNA as a probe. Temperatures of leaf blades ranged from 32 to 35�C under the tested field conditions at New Deal near Lubbock, Texas. Messenger RNAs encoding a major class of low molecular weight HSPs, HSP 16.9, were detected in all wheat genotypes examined. The results suggested that HSPs are synthesised in response to heat stress under agricultural production, and furthermore, that HSPs are produced in wheats differing in geographic background. In the controlled growth chamber experiment, HSP expression in two wheat cultivars, Mustang (heat tolerant) and Sturdy (heat susceptible) were analysed to determine if wheat genotypes differing in heat tolerance differ in in vitro HSP synthesis (translatable HSP mRNAs) under a chronic, diurnal heat-stress regime. Leaf tissues were collected from seedlings over a time-course and poly (A)+RNAs were isolated for in vitro translation and 2-D gel electrophoresis. The protein profiles shown in the 2-D gel analysis revealed that there were not only quantitative differences of individual HSPs between these two wheat lines, but also some unique HSPs which were only found in the heat tolerant line. This data provides evidence of a correlation between HSP synthesis and heat tolerance in wheat under a simulated field environment and suggests that further genetic analysis of HSPs in a segregating population is worthy of investigation. In conclusion, the results of this study provide an impetus for the investigation of the roles of HSP genes in heat tolerance in wheat.

scholarly journals CHIP mutations affect the heat shock response differently in human fibroblasts and iPSC-derived neurons

2020 ◽  
Vol 13 (10) ◽  
pp. dmm045096
Author(s):  
S. Schuster ◽  
E. Heuten ◽  
A. Velic ◽  
J. Admard ◽  
M. Synofzik ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Cortical Neurons ◽  
Human Fibroblasts ◽  
Cerebellar Atrophy ◽  
Spinocerebellar Ataxia Type ◽  
Control Line ◽  
Ataxic Gait ◽  
Shock Response

ABSTRACTC-terminus of HSC70-interacting protein (CHIP) encoded by the gene STUB1 is a co-chaperone and E3 ligase that acts as a key regulator of cellular protein homeostasis. Mutations in STUB1 cause autosomal recessive spinocerebellar ataxia type 16 (SCAR16) with widespread neurodegeneration manifesting as spastic-ataxic gait disorder, dementia and epilepsy. CHIP−/− mice display severe cerebellar atrophy, show high perinatal lethality and impaired heat stress tolerance. To decipher the pathomechanism underlying SCAR16, we investigated the heat shock response (HSR) in primary fibroblasts of three SCAR16 patients. We found impaired HSR induction and recovery compared to healthy controls. HSPA1A/B transcript levels (coding for HSP70) were reduced upon heat shock but HSP70 remained higher upon recovery in patient- compared to control-fibroblasts. As SCAR16 primarily affects the central nervous system we next investigated the HSR in cortical neurons (CNs) derived from induced pluripotent stem cells of SCAR16 patients. We found CNs of patients and controls to be surprisingly resistant to heat stress with high basal levels of HSP70 compared to fibroblasts. Although heat stress resulted in strong transcript level increases of many HSPs, this did not translate into higher HSP70 protein levels upon heat shock, independent of STUB1 mutations. Furthermore, STUB1(−/−) neurons generated by CRISPR/Cas9-mediated genome editing from an isogenic healthy control line showed a similar HSR to patients. Proteomic analysis of CNs showed dysfunctional protein (re)folding and higher basal oxidative stress levels in patients. Our results question the role of impaired HSR in SCAR16 neuropathology and highlight the need for careful selection of proper cell types for modeling human diseases.

scholarly journals Thermotolerance and heat acclimation may share a common mechanism in humans

2011 ◽  
Vol 301 (2) ◽  
pp. R524-R533 ◽  
Author(s):  
Matthew Kuennen ◽  
Trevor Gillum ◽  
Karol Dokladny ◽  
Edward Bedrick ◽  
Suzanne Schneider ◽  
...  
Keyword(s):  
Heart Rate ◽  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Heat Acclimation ◽  
Body Temperatures ◽  
Physiological Strain ◽  
Barrier Permeability ◽  
Shock Response ◽  
Gastrointestinal Barrier

Thermotolerance and heat acclimation are key adaptation processes that have been hitherto viewed as separate phenomena. Here, we provide evidence that these processes may share a common basis, as both may potentially be governed by the heat shock response. We evaluated the effects of a heat shock response-inhibitor (quercetin; 2,000 mg/day) on established markers of thermotolerance [gastrointestinal barrier permeability, plasma TNF-α, IL-6, and IL-10 concentrations, and leukocyte heat shock protein 70 (HSP70) content]. Heat acclimation reduced body temperatures, heart rate, and physiological strain during exercise/heat stress) in male subjects ( n = 8) completing a 7-day heat acclimation protocol. These same subjects completed an identical protocol under placebo supplementation (placebo). Gastrointestinal barrier permeability and TNF-α were increased on the 1st day of exercise/heat stress in quercetin; no differences in these variables were reported in placebo. Exercise HSP70 responses were increased, and plasma cytokines (IL-6, IL-10) were decreased on the 7th day of heat acclimation in placebo; with concomitant reductions in exercise body temperatures, heart rate, and physiological strain. In contrast, gastrointestinal barrier permeability remained elevated, HSP70 was not increased, and IL-6, IL-10, and exercise body temperatures were not reduced on the 7th day of heat acclimation in quercetin. While exercise heart rate and physiological strain were reduced in quercetin, this occurred later in exercise than with placebo. Consistent with the concept that thermotolerance and heat acclimation are related through the heat shock response, repeated exercise/heat stress increases cytoprotective HSP70 and reduces circulating cytokines, contributing to reductions in cellular and systemic markers of heat strain. Exercising under a heat shock response-inhibitor prevents both cellular and systemic heat adaptations.

Heat Shock Response in the Thermophilic Enteric Yeast Arxiozyma telluris

1998 ◽  
Vol 64 (8) ◽  
pp. 3063-3065 ◽  
Author(s):  
Michelle L. Deegenaars ◽  
Kenneth Watson
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Response ◽  
Ecological Niche ◽  
Hsp 70 ◽  
Shock Response ◽  
Heat Stress Tolerance ◽  
Shock Proteins ◽  
Hsp 90

ABSTRACT Heat stress tolerance was examined in the thermophilic enteric yeast Arxiozyma telluris. Heat shock acquisition of thermotolerance and synthesis of heat shock proteins hsp 104, hsp 90, hsp 70, and hsp 60 were induced by a mild heat shock at temperatures from 35 to 40°C for 30 min. The results demonstrate that a yeast which occupies a specialized ecological niche exhibits a typical heat shock response.

scholarly journals Rosemary Reduces Heat Stress by Inducing CRYAB and HSP70 Expression in Broiler Chickens

2018 ◽  
Vol 2018 ◽  
pp. 1-10 ◽  
Author(s):  
Shu Tang ◽  
Bin Yin ◽  
Jiao Xu ◽  
Endong Bao
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Oxidative Damage ◽  
Heat Shock Response ◽  
Broiler Chickens ◽  
Rosemary Extract ◽  
Control Group ◽  
Poultry Production ◽  
Intense Staining ◽  
Shock Response

Heat stress negatively affects poultry production and animal health. In response, animals invoke a heat stress response by inducing heat shock proteins (HSPs). Scientists are actively seeking natural products that can enhance the heat shock response. The present study aimed at assessing the effects of a purified rosemary extract comprising antioxidant compounds on the heat shock response and HSP expression profile in broiler chickens. The response of broilers to HS in the presence of purified rosemary extract was assessed using an in vivo myocardial cell model. Pathological lesions of heart tissue were examined microscopically. The levels and activities of enzymes associated with heart damage and oxidative damage were detected. Immunohistochemical staining was performed for HSPs in myocardial cells. The results showed that lactate dehydrogenase (LDH), creatine kinase (CK), and myocardial CK (CKMB) levels were reduced by the purified rosemary extract before and during heat stress. Heat stress alone increased CK and CKMB levels. The levels of oxidative damage-associated enzymes were compared between the rosemary + heat stress and heat stress-alone groups. The results indicated that in terms of these enzymes, the purified rosemary extract induced a more antioxidative state. Pathological examinations showed that heat stress caused myocardial fiber fracture, karyopyknosis, and degeneration. The addition of purified rosemary extract ameliorated these lesions to some degree, preserving more of the basic structure. Heat stress decreased the cellular levels of crystallin alpha B (CRYAB) and HSP70. The addition of the purified rosemary extract significantly increased the levels of CRYAB and HSP70 during heat stress (p<0.0001). Immunohistochemistry showed that after rosemary treatment, CRYAB and HSP70 showed more intense staining compared with the no heat stress control group. In the rosemary + heat group, after 10 hours of heat stress, the staining intensity of these two proteins remained higher than in the heat stress group. Thus, purified rosemary extract could induce high levels of HSP70 and CRYAB in chicken hearts before and during heat stress. Purified rosemary extract could be used to alleviate heat stress in broiler chickens.

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