scholarly journals H2Av facilitates H3S10 phosphorylation but is not required for heat shock-induced chromatin decondensation or transcriptional elongation

Development ◽  
2017 ◽  
Vol 144 (18) ◽  
pp. 3232-3240
Author(s):  
Yeran Li ◽  
Chao Wang ◽  
Weili Cai ◽  
Saheli Sengupta ◽  
Michael Zavortink ◽  
...  
Keyword(s):  
Heat Shock ◽  
Transcriptional Elongation ◽  
Chromatin Decondensation ◽  
H3s10 Phosphorylation

scholarly journals Transcriptional Activation Domains of Human Heat Shock Factor 1 Recruit Human SWI/SNF

2001 ◽  
Vol 21 (17) ◽  
pp. 5826-5837 ◽  
Author(s):  
E. Kelly Sullivan ◽  
Christine S. Weirich ◽  
Jeffrey R. Guyon ◽  
Saı̈d Sif ◽  
Robert E. Kingston
Keyword(s):  
Heat Shock ◽  
Chromatin Remodeling ◽  
Transcriptional Activation ◽  
Atp Hydrolysis ◽  
Heat Shock Factor ◽  
Transcriptional Elongation ◽  
Heat Shock Factor 1 ◽  
Transcriptional Initiation ◽  
Atpase Subunit ◽  
Activation Domains

ABSTRACT Chromatin remodeling complexes such as SWI/SNF use the energy of ATP hydrolysis to remodel nucleosomal DNA and increase transcription of nucleosomal templates. Human heat shock factor one (hHSF1) is a tightly regulated activator that stimulates transcriptional initiation and elongation using different portions of its activation domains. Here we demonstrate that hHSF1 associates with BRG1, the ATPase subunit of human SWI/SNF (hSWI/SNF) at endogenous protein concentrations. We also show that hHSF1 activation domains recruit hSWI/SNF to a chromatin template in a purified system. Mutation of hHSF1 residues responsible for activation of transcriptional elongation has the most severe effect on recruitment of SWI/SNF and association of hHSF1 with BRG1, suggesting that recruitment of chromatin remodeling activity might play a role in stimulation of elongation.

scholarly journals Caenorhabditis elegans AF4/FMR2 Family Homolog affl-2 Regulates Heat-Shock-Induced Gene Expression

Genetics ◽  
2020 ◽  
Vol 215 (4) ◽  
pp. 1039-1054
Author(s):  
Sophie J. Walton ◽  
Han Wang ◽  
Porfirio Quintero-Cadena ◽  
Alex Bateman ◽  
Paul W. Sternberg
Keyword(s):  
Gene Expression ◽  
Heat Stress ◽  
Caenorhabditis Elegans ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Genetic Locus ◽  
Transcriptional Response ◽  
Transcriptional Elongation ◽  
Link Type ◽  
Shock Response

To mitigate the deleterious effects of temperature increases on cellular organization and proteotoxicity, organisms have developed mechanisms to respond to heat stress. In eukaryotes, HSF1 is the master regulator of the heat shock transcriptional response, but the heat shock response pathway is not yet fully understood. From a forward genetic screen for suppressors of heat-shock-induced gene expression in Caenorhabditis elegans, we found a new allele of hsf-1 that alters its DNA-binding domain, and we found three additional alleles of sup-45, a previously molecularly uncharacterized genetic locus. We identified sup-45 as one of the two hitherto unknown C. elegans orthologs of the human AF4/FMR2 family proteins, which are involved in regulation of transcriptional elongation rate. We thus renamed sup-45 as affl-2 (AF4/FMR2-Like). Through RNA-seq, we demonstrated that affl-2 mutants are deficient in heat-shock-induced transcription. Additionally, affl-2 mutants have herniated intestines, while worms lacking its sole paralog (affl-1) appear wild type. AFFL-2 is a broadly expressed nuclear protein, and nuclear localization of AFFL-2 is necessary for its role in heat shock response. affl-2 and its paralog are not essential for proper HSF-1 expression and localization after heat shock, which suggests that affl-2 may function downstream of, or parallel to, hsf-1. Our characterization of affl-2 provides insights into the regulation of heat-shock-induced gene expression to protect against heat stress.

scholarly journals Caenorhabditis elegans AF4/FMR2 family homolog affl-2 is required for heat shock induced gene expression

2019 ◽  
Author(s):  
Sophie J. Walton ◽  
Han Wang ◽  
Porfirio Quintero-Cadena ◽  
Alex Bateman ◽  
Paul W. Sternberg
Keyword(s):  
Gene Expression ◽  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Genetic Locus ◽  
Transcriptional Response ◽  
Egg Laying ◽  
Transcriptional Elongation ◽  
C Elegans ◽  
Shock Response

AbstractTo mitigate the deleterious effects of temperature increases on cellular organization and proteotoxicity, organisms have developed mechanisms to respond to heat stress. In eukaryotes, HSF1 is the master regulator of the heat shock transcriptional response, but the heat shock response pathway is not yet fully understood. From a forward genetic screen for suppressors of heat shock induced gene expression in C. elegans, we identified a new allele of hsf-1 that alters its DNA-binding domain, and three additional alleles of sup-45, a previously uncharacterized genetic locus. We identified sup-45 as one of the two hitherto unknown C. elegans orthologs of the human AF4/FMR2 family proteins, which are involved in regulation of transcriptional elongation rate. We thus renamed sup-45 as affl-2 (AF4/FMR2-Like). affl-2 mutants are egg-laying defective and dumpy, but worms lacking its sole paralog (affl-1) appear wild-type. AFFL-2 is a broadly expressed nuclear protein, and nuclear localization of AFFL-2 is necessary for its role in heat shock response. affl-2 and its paralog are not essential for proper HSF-1 expression and localization after heat shock, which suggests that affl-2 may function downstream or parallel of hsf-1. Our characterization of affl-2 provides insights into the complex processes of transcriptional elongation and regulating heat shock induced gene expression to protect against heat stress.

Fish kidney cell line in response to heat shock

1992 ◽  
Vol 50 (1) ◽  
pp. 704-705
Author(s):  
Li-Chu Tung ◽  
Yung-Reui Chen ◽  
Shiu-Nan Chen ◽  
Guang-Hsiung Kuo
Keyword(s):  
Heat Shock ◽  
Cell Line ◽  
Fetal Calf Serum ◽  
Calf Serum ◽  
Uranyl Acetate ◽  
Ultrastructural Changes ◽  
Heat Shock Treatment ◽  
Acanthopagrus Schlegeli ◽  
Cacodylate Buffer ◽  
Fish Kidney

In the present study, the ultrastructural changes of BPK cells, a fibroblast-like cell line, derived from the kidney of juvenile black porgy Acanthopagrus schlegeli, under heat shock treatment are described.The BPK cells were maintained in L-15 medium supplemented with 10% fetal calf serum and 0.15 M NaCl at 28|C2. The heating was carried out in precalibrated water baths. Monolayers of cells, grown on coverslips in parafilm-sealed petri dishes were submerged under water for 30 min at 40|C treatments. Cells were fixed in 2.5% glutaraldehyde in 0.1 M cacodylate buffer supplemented with 6.6% sucrose, postfixed in 1% OsO4 and flat embedded in Spurr’s resin. Silver section were cut parallel to the substratum, stained with uranyl acetate and Reynold’s lead citrate, and examined in a Hitachi H-600 electron microscope at 75 KV.

Absence of temporal ordering of apoptotic features in heat-shock treated leukemia and lymphoma cell lines

1996 ◽  
Vol 54 ◽  
pp. 758-759
Author(s):  
D. W. Fairbain ◽  
M.D. Standing ◽  
K.L. O'Neill
Keyword(s):  
Heat Shock ◽  
Cell Lines ◽  
Chromatin Condensation ◽  
Membrane Integrity ◽  
Resistant Cell ◽  
Membrane Blebbing ◽  
Late Loss ◽  
Induced Apoptosis ◽  
Dying Cells ◽  
In Cells

Apoptosis is a genetically defined response to physiological stimuli that results in cellular suicide. Features common to apoptotic cells include chromatin condensation, oligonucleosomal DNA fragmentation, membrane blebbing, nuclear destruction, and late loss of ability to exclude vital dyes. These characteristics contrast markedly from pathological necrosis, in which membrane integrity loss is demonstrated early, and other features of apoptosis, which allow a non-inflammatory removal of dead and dying cells, are absent. Using heat shock-induced apoptosis as a model for examining stress response in cells, we undertook to categorize a variety of human leukemias and lymphomas with regard to their response to heat shock. We were also interested in determining whether a common temporal order was followed in cells dying by apoptosis. In addition, based on our previous results, we investigated whether increasing heat load resulted in increased apoptosis, with particular interest in relatively resistant cell lines, or whether the mode of death changed from apoptosis to necrosis.

Glycyrrhizin effects rat hepatocytes via the reduction of heat shock protein 90 expression

2001 ◽  
Vol 120 (5) ◽  
pp. A357-A357
Author(s):  
T YOH ◽  
T NAKASHIMA ◽  
Y SUMIDA ◽  
Y KAKISAKA ◽  
H ISHIKAWA ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Rat Hepatocytes

Ammonia aggravates emotional stress-induced gastric mucosal oxidative injury through the cancellation of heat shock protein 70 (HSP70)

2001 ◽  
Vol 120 (5) ◽  
pp. A152-A152
Author(s):  
H SUZUKI ◽  
S NAGAHASHI ◽  
M MIYAZAWA ◽  
M MORI ◽  
H NAGATA ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Emotional Stress ◽  
Heat Shock Protein 70 ◽  
Oxidative Injury
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