scholarly journals Cytosol-Localized Heat Shock Factor-Binding Protein, AtHSBP, Functions as a Negative Regulator of Heat Shock Response by Translocation to the Nucleus and Is Required for Seed Development in Arabidopsis

2010 ◽  
Vol 153 (2) ◽  
pp. 773-784 ◽  
Author(s):  
Shih-Feng Hsu ◽  
Hui-Chuan Lai ◽  
Tsung-Luo Jinn
Keyword(s):  
Heat Shock ◽  
Seed Development ◽  
Heat Shock Response ◽  
Binding Protein ◽  
Heat Shock Factor ◽  
Negative Regulator ◽  
Factor Binding ◽  
Shock Response

Thermal acclimation changes DNA-binding activity of heat shock factor 1(HSF1) in the gobyGillichthys mirabilis: implications for plasticity in the heat-shock response in natural populations

2002 ◽  
Vol 205 (20) ◽  
pp. 3231-3240 ◽  
Author(s):  
Bradley A. Buckley ◽  
Gretchen E. Hofmann
Keyword(s):  
Gene Expression ◽  
Heat Shock ◽  
Heat Shock Response ◽  
Environmental Control ◽  
Heat Shock Factor ◽  
Thermal Acclimation ◽  
Model Systems ◽  
Threshold Temperature ◽  
Heat Shock Factor 1 ◽  
Shock Response

SUMMARYThe intracellular build-up of thermally damaged proteins following exposure to heat stress results in the synthesis of a family of evolutionarily conserved proteins called heat shock proteins (Hsps) that act as molecular chaperones, protecting the cell against the aggregation of denatured proteins. The transcriptional regulation of heat shock genes by heat shock factor 1(HSF1) has been extensively studied in model systems, but little research has focused on the role HSF1 plays in Hsp gene expression in eurythermal organisms from broadly fluctuating thermal environments. The threshold temperature for Hsp induction in these organisms shifts with the recent thermal history of the individual but the mechanism by which this plasticity in Hsp induction temperature is achieved is unknown. We examined the effect of thermal acclimation on the heat-activation of HSF1 in the eurythermal teleost Gillichthys mirabilis. After a 5-week acclimation period (at 13, 21 or 28°C) the temperature of HSF1 activation was positively correlated with acclimation temperature. HSF1 activation peaked at 27°C in fish acclimated to 13°C, at 33°C in the 21°C group, and at 36°C in the 28°C group. Concentrations of both HSF1 and Hsp70 in the 28°C group were significantly higher than in the colder acclimated fish. Plasticity in HSF1 activation may be important to the adjustable nature of the heat shock response in eurythermal organisms and the environmental control of Hsp gene expression.

During ischemia-reperfusion in rat kidneys, heat shock response is not regulated by expressional changes of heat shock factor 1

2000 ◽  
Vol 13 (4) ◽  
pp. 297-302 ◽  
Author(s):  
Ziya Akçetin ◽  
Reinhard Pregla ◽  
Dorothea Darmer ◽  
Hans-Jürgen Brömme ◽  
Jürgen Holtz
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Ischemia Reperfusion ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1 ◽  
Shock Response ◽  
Rat Kidneys

scholarly journals Regulation of heat shock factor in Schizosaccharomyces pombe more closely resembles regulation in mammals than in Saccharomyces cerevisiae.

1991 ◽  
Vol 11 (1) ◽  
pp. 281-288 ◽  
Author(s):  
G J Gallo ◽  
T J Schuetz ◽  
R E Kingston
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Heat Shock ◽  
Dna Binding ◽  
Schizosaccharomyces Pombe ◽  
Fission Yeast ◽  
Heat Shock Response ◽  
Heat Shock Factor ◽  
Regulatory Sequence ◽  
Heat Shock Element ◽  
Shock Response

The heat shock response appears to be universal. All eucaryotes studied encode a protein, heat shock factor (HSF), that is believed to regulate transcription of heat shock genes. This protein binds to a regulatory sequence, the heat shock element, that is absolutely conserved among eucaryotes. We report here the identification of HSF in the fission yeast Schizosaccharomyces pombe. HSF binding was not observed in extracts from normally growing S. pombe (28 degrees C) but was detected in increasing amounts as the temperature of heat shock increased between 39 and 45 degrees C. This regulation is in contrast to that observed in Saccharomyces cerevisiae, in which HSF binding is detectable at both normal and heat shock temperatures. The S. pombe factor bound specifically to the heat shock element, as judged by methylation interference and DNase I protection analysis. The induction of S. pombe HSF was not inhibited by cycloheximide, suggesting that induction occurs posttranslationally, and the induced factor was shown to be phosphorylated. S. pombe HSF was purified to near homogeneity and was shown to have an apparent mobility of approximately 108 kDa. Since heat-induced DNA binding by HSF had previously been demonstrated only in metazoans, the conservation of heat-induced DNA binding by HSF among S. pombe and metazoans suggests that this mode of regulation is evolutionarily ancient.

scholarly journals HEAT SHOCK FACTOR BINDING PROTEIN limits meiotic crossovers by repressing HEI10 transcription

2021 ◽  
Author(s):  
Juhyun Kim ◽  
Jihye Park ◽  
Heejin Kim ◽  
Namil Son ◽  
Christophe Lambing ◽  
...  
Keyword(s):  
Heat Shock ◽  
Chromatin Immunoprecipitation ◽  
Response Regulator ◽  
Binding Protein ◽  
Temperature Response ◽  
Heat Shock Factor ◽  
Heat Shock Factors ◽  
Forward Genetic Screen ◽  
Factor Binding ◽  
Genome Wide

The number of meiotic crossovers is tightly controlled and most depend on pro-crossover ZMM proteins, such as the E3 ligase HEI10. Despite the importance of HEI10 dosage for crossover formation, how HEI10 transcription is controlled remains unexplored. In a forward genetic screen using a sensitive fluorescent seed crossover reporter in Arabidopsis thaliana we identify heat shock factor binding protein (HSBP) as a repressor of HEI10 transcription and crossover numbers. Using genome-wide crossover mapping and cytogenetics, we show that hsbp mutations or meiotic HSBP knockdowns increase ZMM-dependent crossovers towards the telomeres, mirroring the effects of HEI10 overexpression. Through RNA sequencing, DNA methylome and chromatin immunoprecipitation analysis, we reveal that HSBP directly represses HEI10 transcription by binding with heat shock factors (HSFs) at the HEI10 promoter and maintaining DNA methylation over the HEI10 5′ untranslated region. Our findings provide insights into how the temperature response regulator HSBP restricts meiotic HEI10 transcription and crossover number by attenuating HSF activity.

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