scholarly journals GCN5 enables HSP12 induction promoting chromatin remodeling not histone acetylation.

2021 ◽  
Author(s):  
Francesca Antonazzi ◽  
Francesca Di Felice ◽  
Giorgio Camilloni
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Histone Acetylation ◽  
Chromatin Remodeling ◽  
Gene Activation ◽  
Transcriptional Response ◽  
Regulation Of Transcription ◽  
Molecular Response ◽  
H2o2 Treatment ◽  
Shock Response

Regulation of stress responsive genes represents one of the best examples of gene induction and the relevance and involvement of different regulators may change for a given gene depending on the challenging stimulus. HSP12 gene is induced by very different stimuli, however the molecular response to the stress has been characterized in detail only for heat shock treatments. In this work we want to verify whether, the regulation of transcription induced by oxidative stress, utilizes the same epigenetic solutions relative to those employed in heat shock response. We also monitored HSP12 induction employing spermidine, a known acetyltransferase inhibitor, and observed an oxidative stress that synergizes with spermidine treatment. Our data show that during transcriptional response to H2O2, histone acetylation and chromatin remodeling occur. However, when the relevance of Gcn5p on these processes was studied, we observed that induction of transcription is GCN5 dependent and this does not rely on histone acetylation by Gcn5p despite its HAT activity. Chromatin remodeling accompanying gene activation is rather GCN5 dependent. Thus, GCN5 controls HSP12 transcription after H2O2 treatment by allowing chromatin remodeling and it is only partially involved in HSP12 histone acetylation regardless its HAT activity.

scholarly journals Se Alleviated Oxidative Stress-Mediated Complex Poisoning Mechanism in Pb-Treated Chicken Kidneys: Inflammation, Heat Shock Response, and Autophagy

2021 ◽  
Author(s):  
Zhiying Miao ◽  
Weikang Yu ◽  
Yueyang Wang ◽  
Xianhong Gu ◽  
Xiaohua Teng
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Protein Expression ◽  
Heat Shock Response ◽  
Potable Water ◽  
Histological Structure ◽  
Standard Diet ◽  
Shock Response ◽  
Mrna And Protein Expression ◽  
Shock Proteins

Abstract Background: Lead (Pb) is a toxic environmental pollutant and can exerts toxicity in kidneys. It is known that selenium (Se) has an antagonistic effect on Pb poisoning. However, biological events during the process were not well understood in chicken kidneys.Methods: One hundred and eighty male Hyline chickens (7-day-old) were randomly divided into the control group (offering standard diet and potable water), the Se group (offering Na2SeO3-added standard diet and potable water), the Pb group (offering standard diet and (CH3OO)2Pb-added potable water), and the Pb+Se group (offering Na2SeO3-added standard diet and (CH3OO)2Pb-added potable water). On 30th, 60th, and 90th days, kidneys were removed to perform the studies of histological structure, oxidative stress indicators, cytokines, heat shock proteins, and autophagy in the chicken kidneys.Results: The experimental results indicated that Pb poisoning changed renal histological structure; decreased catalase, glutathione-s-transferase, and total antioxidative capacity activities; increased hydrogen peroxide content; induced mRNA and protein expression of heat shock proteins; inhibited interleukin (IL)-2 mRNA expression, and induced IL-4 and IL-12β mRNA expression; inhibited mammalian target of rapamycin mRNA and protein expression, and induced autophagy-related gene mRNA and protein expression in the chicken kidneys. Supplement of Se mitigated the above changes caused by Pb.Conclusion: Our research strengthens the evidence that Pb induced oxidative stress, inflammation, heat shock response, and autophagy and Se administration alleviated Pb poisoning through mitigating oxidative stress in the chicken kidneys.

Proteins containing non-native disulfide bonds generated by oxidative stress can act as signals for the induction of the heat shock response

1997 ◽  
Vol 171 (2) ◽  
pp. 143-151 ◽  
Author(s):  
Alice T. McDuffee ◽  
Guillermo Senisterra ◽  
Steven Huntley ◽  
James R. Lepock ◽  
Konjeti R. Sekhar ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Disulfide Bonds ◽  
Shock Response

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.

scholarly journals Dynamics of Heat Shock Detection and Response in the Intestine of Caenorhabditis elegans

2019 ◽  
Author(s):  
Erin K. Dahlstrom ◽  
Erel Levine
Keyword(s):  
Caenorhabditis Elegans ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Protein Misfolding ◽  
Single Cells ◽  
Molecular Response ◽  
Longitudinal Measurements ◽  
Cell Tissue ◽  
Shock Response ◽  
Protein Misfolding And Aggregation

AbstractThe heat shock response is the organized molecular response to stressors which disrupt proteostasis, potentially leading to protein misfolding and aggregation. While the regulation of the heat shock response is well-studied in single cells, its coordination at the cell, tissue, and systemic levels of a multicellular organism is poorly understood. To probe the interplay between systemic and cell-autonomous responses, we studied the upregulation of HSP-16.2, a molecular chaperone induced throughout the intestine of Caenorhabditis elegans following a heat shock, by taking longitudinal measurements in a microfluidic environment. Based on the dynamics of HSP-16.2 accumulation, we showed that a combination of heat shock temperature and duration define the intensity of stress inflicted on the worm and identified two regimes of low and high intensity stress. Modeling the underlying regulatory dynamics implicated the saturation of heat shock protein mRNA production in defining these two regimes and emphasized the importance of time separation between transcription and translation in establishing these dynamics. By applying a heat shock and measuring the response in separate parts of the animals, we implicated thermosensory neurons in accelerating the response and transducing information within the animal. We discuss possible implications of the systemic and cell level aspects and how they coordinate to facilitate the organismal response.

Genome-wide chromatin remodeling modulates the Alu heat shock response

Gene ◽  
2001 ◽  
Vol 276 (1-2) ◽  
pp. 127-133 ◽  
Author(s):  
Cheonkoog Kim ◽  
Carol M. Rubin ◽  
Carl W. Schmid
Keyword(s):  
Heat Shock ◽  
Chromatin Remodeling ◽  
Heat Shock Response ◽  
Genome Wide ◽  
Shock Response

Analysis of RNA for transcripts for catalase and SP71 in rat hearts after in vivo hyperthermia

1991 ◽  
Vol 69 (5-6) ◽  
pp. 375-382 ◽  
Author(s):  
R. William Currie ◽  
Robert M. Tanguay
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Catalase Activity ◽  
Mrna Level ◽  
Regulation Of Transcription ◽  
Rat Tissues ◽  
Mrna Levels ◽  
Control Heart ◽  
Shock Response ◽  
Human Hsp70

Hyperthermic stress induces synthesis of the major inducible (heat) stress protein (SP71) in all rat tissues. In addition, there is an increase in catalase activity in hearts at 24 and 48 h after the induction of the heat shock response. To more precisely define some of the molecular aspects of the induction of the heat shock response in hearts, we examined mRNA levels for the catalase, SP71 and HSP27. RNA was isolated from control hearts and at various time periods (0–24 h) of recovery after brief hyperthermic treatment and was analyzed by Northern blot analysis using as probes cDNA sequences for rat liver catalase, human HSP70 (inducible), and human HSP27. There was no detectable change in mRNA for catalase after heat shock or during recovery. Hyperthermic stress has no apparent effect on the regulation of transcription of mRNA coding for catalase, indicating that the increase in catalase activity is either translationally or post-translationally regulated. The human HSP70 cDNA did not hybridize to control heart RNA, but did hybridize to SP71 transcripts at 0, 1.5, and 3 h post heat shock. The mRNA level for SP71 peaked at 1.5 h, was reduced at 3 h, and became almost undetectable at 6 h post heat shock. Similarly, the human HSP27 cDNA did not hybridize to control heart RNA, but did hybridize to transcripts for HSP27 at 0, 1.5, 3, and up to 15 h post heat shock. Maximal signal for HSP27 was at 3 h post heat shock and was sharply reduced at 6 h post heat shock. The accumulation of transcripts for SP71 and HSP27 after hyperthermic stress is rapid, and degradation of the transcripts is almost complete by 6 h post heat shock.Key words: heat shock proteins, hyperthermia, catalase, heart, RNA.

scholarly journals HDAC6–ubiquitin interaction controls the duration of HSF1 activation after heat shock

2014 ◽  
Vol 25 (25) ◽  
pp. 4187-4194 ◽  
Author(s):  
Lydia Pernet ◽  
Virginie Faure ◽  
Benoit Gilquin ◽  
Solenne Dufour-Guérin ◽  
Saadi Khochbin ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Transcriptional Response ◽  
Heat Shock Gene ◽  
Aaa Atpase ◽  
Protein Ubiquitination ◽  
Regulatory Circuit ◽  
Shock Response ◽  
Rapid Inactivation ◽  
In Cells

After heat shock, HSF1 controls a major cellular transcriptional response involving the activation of early (HSP70) and late (HSP25) heat shock gene expression. Here we show that a full response to heat shock (activation of both HSP70 and HSP25) depends on the duration of HSF1 activation, which is itself controlled by HDAC6, a unique deacetylase known to bind monoubiquitin and polyubiquitin with high affinity. On the basis of a comparative analysis of the heat shock response in cells knocked out for HDAC6 or expressing HDAC6 mutants, we show that HDAC6 binding to ubiquitinated proteins controls the duration of HSF1 activation after heat shock. In cells expressing HDAC6 mutated in the ubiquitin-binding domain, the AAA ATPase factor p97/VCP mediates rapid inactivation of HSF1, precluding late activation of the HSP25 gene. In these cells, knockdown of p97/VCP rescues HSF1 from this rapid inactivation and restores HSP25 expression. We present here a new regulatory circuit that adjusts the duration of the heat shock response to the extent of protein ubiquitination after heat shock.

scholarly journals Glutathionylation of the Bacterial Hsp70 Chaperone DnaK Provides a Link between Oxidative Stress and the Heat Shock Response

2016 ◽  
Vol 291 (13) ◽  
pp. 6967-6981 ◽  
Author(s):  
Hong Zhang ◽  
Jie Yang ◽  
Si Wu ◽  
Weibin Gong ◽  
Chang Chen ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Chaperone Dnak ◽  
Shock Response ◽  
Hsp70 Chaperone
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