Browse > Article
http://dx.doi.org/10.5352/JLS.2006.16.6.1052

The Role of DNA Binding Domain in hHSF1 through Redox State  

Kim, Sol (Department of Chemistry and Centre for Innovative Bio.physio sensor Technology, Pusan National University)
Hwang, Yun-Jeong (Department of Chemistry and Centre for Innovative Bio.physio sensor Technology, Pusan National University)
Kim, Hee-Eun (Department of Chemistry and Centre for Innovative Bio.physio sensor Technology, Pusan National University)
Lu, Ming (Department of Chemistry and Centre for Innovative Bio.physio sensor Technology, Pusan National University)
Kim, An-D-Re (Department of Chemistry and Centre for Innovative Bio.physio sensor Technology, Pusan National University)
Moon, Ji-Young (Department of Molecular biology, Pusan National University)
Kang, Ho-Sung (Department of Molecular biology, Pusan National University)
Park, Jang-Su (Department of Chemistry and Centre for Innovative Bio.physio sensor Technology, Pusan National University)
Publication Information
Journal of Life Science / v.16, no.6, 2006 , pp. 1052-1059 More about this Journal
Abstract
The heat shock response is induced by environmental stress, pathophysiological state and non-stress conditions and wide spread from bacteria to human. Although translations of most proteins are stopped under a heat shock response, heat shock proteins (HSPs) are produced to protect cell from stress. When heat shock response is induced, conformation of HSF1 was changed from monomer to trimer and HSF1 specifically binds to DNA, which was called a heat shock element(HSE) within the promoter of the heat shock genes. Human HSF1(hHSFl) contains five cysteine(Cys) residues. A thiol group(R-SH) of Cys is a strong nucleophile, the most readily oxidized and nitrosylated in amino acid chain. This consideration suggests that Cys residues may regulate the change of conformation and the activity of hHSF1 through a redox-dependent thiol/disulfide exchange reaction. We want to construct role of five Cys residues of hHSF by redox reagents. According to two studies, Cys residues are related to trimer formation of hHSF1. In this study, we want to demonstrate the correlation between structural change and DNA-binding activity of HSF1 through forming disulfide bond and trimerization. In this results, we could deduce that DNA binding activity of DNA binding domain wasn't affected by redox for always expose outside to easily bind to DNA. DNA binding activity of wild-type HSF's DNA binding domain was affected by conformational change, as conformational structure change (trimerization) caused DNA binding domain.
Keywords
Heat shock response; hHSF1; DNA-binding domain; trimerization; redox;
Citations & Related Records
연도 인용수 순위
  • Reference
1 Westerheide S. D. and R. I. Morimoto, 2005. Heat Shock Response Modulators as Therapeutic Tools for Diseases of Protein Conformation. The Journal of Biological Chemistry 280, 33097-33100   DOI   ScienceOn
2 Shi Y., D. D. Mosser, and R. I. Morimoto, 1998. Molecular chapelones as HSF1-specific transcriptional repressors. Genes & Development 12, 654-666   DOI
3 Liu P. C. C. and D. J. Thiele, 1999. Modulation of Human Heat Shock Factor Trimerization by the Linker Domain. The Journal of Biological Chemistry 274, 17219-17225   DOI
4 Holmberg, C. I., S. E. F. Tran, J. E. Eriksson, and L. Sistonen, 2002. Multisite phosphorylation provides sophisticated regulation of transcription factors. TRENS in Biochemical Sciences 27, 619-627   DOI   ScienceOn
5 Galan, A., A. Troyano, N. E. Vilaboa, C. Fernandez, E. D. Blas, and P. Aller, 2001. Modulation of the stress response during apoptosis and necrosis induction in cadmiumtreated U-937 human promonocytic cells. Biochimica et Biophysica Acta 1538, 38-46   DOI   ScienceOn
6 Choi H. S., Z. Lin, B. Li, and Y. C. Liu, 1990. Age-dependent Decrease in the Heat-inducible DNA Sequencespecific Binding Activity in Human Diploid Fibroblasts. The Journal of Biological Chemistry 265, 18005-18011
7 Lu J., J. H. Park, Y. C. Liu, and K. Y. Chen, 2000. Activation of Heat Shock Factor 1 by Hyperosmotic or Hypo-Osmotic Stress Is Drastically Attenuated in Normal Human Fibroblasts During Senescence. Journal of Cellular Physiology 184, 183-190   DOI   ScienceOn
8 Paroo Z., M. J. Meredith, M. Locke, J. V. Haist, M. Karmazyn, and E. G. Noble, 2002. Redox signaling of cardiac HSF1 DNA binding. American Physiological Society 283, C404-C411   DOI   ScienceOn
9 Bonner, J. J., D. Chen, K. Storey, M. Tushan, and K. Lea, 2000. Structural Analysis of Yeast HSF by Site-specipic Crosslinking. Journal of Molecular Biology 302, 581-592   DOI   ScienceOn
10 Dai, Q., C. Zhang, Y. Wu, H. McDonough, R. A. Whaley, V. Godfrey, H. H. Li, N. Madamanchi, W. Xu, L. Neckers, and C. Patterson, 2003. CHIP activate HSF1 and confers protection against apoptosis and cellular stress. European Molecular Biology Organization Journal 22, 5446- 5458   DOI   ScienceOn
11 Jacquier-Sarlin, M. R. and B. S. Polla, 1996. Dual regulation of heat-shock transcription factor (HSF) activation and DNA-binding activity by $H_2O_2$ : role of thioredoxin. Biochemistry 318, 187-193   DOI
12 Kim, H. R., H. S. Kang, and H. D. Kim, 1999. Geldanamycin Induces Heat Shock Protein Expression Through Activation of HSF1 in K562 Erythroleukemic Cells. JUBMB Life 48, 429-433
13 Manalo, D. J. and A. Y. Liu, 2001. Resolution, Detection, and Characterization of Redox Conformers of Human HSF1. The Journal of Biological Chemistry 276, 23554-23561   DOI   ScienceOn
14 Dai R., W. Frejtag, B. He, Y. Zhang, and N. F. Mivech, 2000. c-Jun $NH_2-terminal$ Kinase Targeting and Phosphorylation of Heat Shock Factor-1 Suppress Its Transcriptional Activity. The Journal of Biological Chemistry 275, 18210-18218   DOI   ScienceOn
15 Ahn S. G., and D. J. Thiele, 2003. Redox regulation of mammalian heat shock factor 1 is essential for Hsp gene activation and protection from stress. Genes & Development 17, 516-528   DOI   ScienceOn
16 Bharadwaj S., A. Ali, and N. Ovsenek, 1999. Multiple Components of the HSP90 Chaperone Complex Function in Regulation of Heat Shock Factor 1 in Vivo. Molecular and Cellular Biology 19, 8033-8041   DOI
17 Chen T. and C. S. Parker, 2001. Dynamic association of transcriptional activation domains and regulatory regions in Saccharomyces cerevisiae heat shock factor. Proceedings of National Academy of Science 99, 1200-1205
18 Green M., T. J. Schuetz, K. Sullivan, and R. E. Kingston, 1995. A Heat Shock-Responsive Domain of Human HSF1 That Regulates Transcription Activation Domain Function. Molecular and Cellular Biology 12, 3354-3362
19 Kim S. A., J. H. Yoon, S. H. Lee, and S. G. Ahn, 2005. Polo-like Kinase 1 Phospholylates Heat Shock Transcription Factor 1 and Mediates Its Nuclear Translocation during Heat Stress. The Journal of Biological Chemistry 280, 12653-12657   DOI   ScienceOn
20 Pirkkala L., T. P. Alastalo, X. Zuo, I. J. Benjamin, and L. Sistonen, 2000. Distruption of Heat Shock Factor 1 Reveals an Essential Role in the Ubiquitin Proteolytic Pathway. Molecular and Cellular Biology 20, 2670-2675   DOI
21 Manalo, D. J., Z. Lin, and A. Y. Liu, 2002. Redox- Dependent Regulation of the Conformation and Function of Human Heat Shock Factor 1. Biochemistry 41, 2580-2588   DOI   ScienceOn
22 Shamovsky, I. and D. Gershon, 2004. Novel regulatory factors of HSF-1 activation: facts and perspectives regarding their involvement in the age-associated attenuation of heat shock response. Mechanisms of Aging and Development 125, 767-775   DOI   ScienceOn
23 Morimoto R. I., 1998. Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators. Genes & Development 12, 3788-3796   DOI   ScienceOn