scholarly journals Transcriptional regulation and binding of heat shock factor 1 and heat shock factor 2 to 32 human heat shock genes during thermal stress and differentiation

10.1379/481.1 ◽  
2004 ◽  
Vol 9 (1) ◽  
pp. 21-28 ◽  
Author(s):  
Nathan D. Trinklein ◽  
Will C. Chen ◽  
Robert E. Kingston ◽  
Richard M. Myers
Keyword(s):  
Transcriptional Regulation ◽  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1 ◽  
Heat Shock Genes

Human heat shock factor 1 is predominantly a nuclear protein before and after heat stress

1999 ◽  
Vol 112 (16) ◽  
pp. 2765-2774 ◽  
Author(s):  
P.A. Mercier ◽  
N.A. Winegarden ◽  
J.T. Westwood
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Nuclear Protein ◽  
Heat Shock Factor ◽  
Nuclear Fraction ◽  
Heat Shock Factor 1 ◽  
Heat Shock Genes ◽  
Before And After ◽  
Biochemical Fractionation ◽  
Multistep Process

The induction of the heat shock genes in eukaryotes by heat and other forms of stress is mediated by a transcription factor known as heat shock factor 1 (HSF1). HSF1 is present in unstressed metazoan cells as a monomer with low affinity for DNA, and upon exposure to stress it is converted to an ‘active’ homotrimer that binds the promoters of heat shock genes with high affinity and induces their transcription. The conversion of HSF1 to its active form is hypothesized to be a multistep process involving physical changes in the HSF1 molecule and the possible translocation of HSF1 from the cytoplasm to the nucleus. While all studies to date have found active HSF1 to be a nuclear protein, there have been conflicting reports on whether the inactive form of HSF is predominantly a cytoplasmic or nuclear protein. In this study, we have made antibodies against human HSF1 and have reexamined its localization in unstressed and heat-shocked human HeLa and A549 cells, and in green monkey Vero cells. Biochemical fractionation of heat-shocked HeLa cells followed by western blot analysis showed that HSF1 was mostly found in the nuclear fraction. In extracts made from unshocked cells, HSF1 was predominantly found in the cytoplasmic fraction using one fractionation procedure, but was distributed approximately equally between the cytoplasmic and nuclear fractions when a different procedure was used. Immunofluorescence microscopy revealed that HSF1 was predominantly a nuclear protein in both heat shocked and unstressed cells. Quantification of HSF1 staining showed that approximately 80% of HSF1 was present in the nucleus both before and after heat stress. These results suggest that HSF1 is predominantly a nuclear protein prior to being exposed to stress, but has low affinity for the nucleus and is easily extracted using most biochemical fractionation procedures. These results also imply that HSF1 translocation is probably not part of the multistep process in HSF1 activation for many cell types.

scholarly journals Heat Shock Factor 1 (HSF1) Controls Chemoresistance and Autophagy through Transcriptional Regulation of Autophagy-related Protein 7 (ATG7)

2013 ◽  
Vol 288 (13) ◽  
pp. 9165-9176 ◽  
Author(s):  
Shruti Desai ◽  
Zixing Liu ◽  
Jun Yao ◽  
Nishant Patel ◽  
Jieqing Chen ◽  
...  
Keyword(s):  
Transcriptional Regulation ◽  
Heat Shock ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1 ◽  
Related Protein

Heat shock factor 1 regulates heat shock proteins and immune-related genes in Penaeus monodon under thermal stress

2018 ◽  
Vol 88 ◽  
pp. 19-27 ◽  
Author(s):  
Phornphan Sornchuer ◽  
Wisarut Junprung ◽  
Warumporn Yingsunthonwattana ◽  
Anchalee Tassanakajon
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Penaeus Monodon ◽  
Heat Shock Factor ◽  
Heat Shock Factor 1 ◽  
Immune Related Genes ◽  
Shock Proteins

scholarly journals Transcriptional Regulation of Selenoprotein F by Heat Shock Factor 1 during Selenium Supplementation and Stress Response

Cells ◽  
2019 ◽  
Vol 8 (5) ◽  
pp. 479 ◽  
Author(s):  
Bingyu Ren ◽  
Yanmei Huang ◽  
Chen Zou ◽  
Yingying Wu ◽  
Yuru Huang ◽  
...  
Keyword(s):  
Transcriptional Regulation ◽  
Heat Shock ◽  
Binding Sites ◽  
Heat Shock Factor ◽  
Selenium Supplementation ◽  
Heat Shock Factor 1 ◽  
Chip Assay ◽  
Over Expression ◽  
Protein Levels ◽  
Flanking Regions

Changes of Selenoprotein F (SELENOF) protein levels have been reported during selenium supplementation, stressful, and pathological conditions. However, the mechanisms of how these external factors regulate SELENOF gene expression are largely unknown. In this study, HEK293T cells were chosen as an in vitro model. The 5′-flanking regions of SELENOF were analyzed for promoter features. Dual-Glo Luciferase assays were used to detect promoter activities. Putative binding sites of Heat Shock Factor 1 (HSF1) were predicted in silico and the associations were further proved by chromatin immunoprecipitation (ChIP) assay. Selenate and tunicamycin (Tm) treatment were used to induce SELENOF up-regulation. The fold changes in SELENOF expression and other relative proteins were analyzed by Q-PCR and western blot. Our results showed that selenate and Tm treatment up-regulated SELENOF at mRNA and protein levels. SELENOF 5′-flanking regions from −818 to −248 were identified as core positive regulatory element regions. Four putative HSF1 binding sites were predicted in regions from −1430 to −248, and six out of seven primers detected positive results in ChIP assay. HSF1 over-expression and heat shock activation increased the promoter activities, and mRNA and protein levels of SELENOF. Over-expression and knockdown of HSF1 showed transcriptional regulation effects on SELENOF during selenate and Tm treatment. In conclusion, HSF1 was discovered as one of the transcription factors that were associated with SELENOF 5′-flanking regions and mediated the up-regulation of SELENOF during selenate and Tm treatment. Our work has provided experimental data for the molecular mechanism of SELENOF gene regulation, as well as uncovered the involvement of HSF1 in selenotranscriptomic for the first time.

Sign in / Sign up

Export Citation Format

Share Document