The Regulatory Domain of Human Heat Shock Factor 1 Is Sufficient To Sense Heat Stress

REFERENCES

• Ausubel, F. M., R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.). 1989. Current protocols in molecular biology. John Wiley & Sons, New York.
   Google Scholar
• Bonner, J. J., S. Heyward, and D. L. Fackenthal. 1992. Temperature-dependent regulation of a heterologous transcriptional activation domain fused to yeast heat shock transcription factor. Mol. Cell. Biol. 12:1021–1030.
   PubMedGoogle Scholar
• Bruce, J. L., B. D. Price, C. N. Coleman, and S. K. Calderwood. 1993. Oxidative injury rapidly activates the heat shock transcription factor but fails to increase levels of heat shock proteins. Cancer Res. 53:12–15.
   PubMed Web of Science ®Google Scholar
• Cress, W. D., and S. J. Triezenberg. 1991. Critical structural elements of the VP16 transcriptional activation domain. Science 251:87–90.
   PubMedGoogle Scholar
• Gallo, G. J., T. J. Schuetz, and R. E. Kingston. 1991. Regulation of heat shock factor in Schizosaccharomyces pombe more closely resembles regulation in mammals than in Saccharomyces cerevisiae. Mol. Cell. Biol. 11:281-288.
   PubMedGoogle Scholar
• Giardina, C., and J. T. Lis. 1995. Dynamic protein-DNA architecture of a yeast heat shock promoter. Mol. Cell. Biol. 15:2737–2744.
   PubMedGoogle Scholar
• Green, M., T. J. Schuetz, E. K. Sullivan, and R. E. Kingston. 1995. A heat shock-responsive domain of human HSF1 that regulates transcription activation domain function. Mol. Cell. Biol. 15:3354–3362.
   PubMed Web of Science ®Google Scholar
• Hensold, J. O., C. R. Hunt, S. K. Calderwood, D. E. Housman, and R. E. Kingston. 1990. DNA binding ofheat shock factor to the heat shock element is insufficient for transcriptional activation in murine erythroleukemia cells. Mol. Cell. Biol. 10:1600–1608.
   PubMedGoogle Scholar
• Hightower, L. E. 1991. Heat shock, stress proteins, chaperones, and proteotoxicity. Cell 66:191–197.
   PubMed Web of Science ®Google Scholar
• Hoj, A., and B. K. Jakobsen. 1994. A short element required for turning off heat shock transcription factor: evidence that phosphorylation enhances deactivation. EMBO J. 13:2617–2624.
   PubMedGoogle Scholar
• Hope, I. A., and K. Struhl. 1987. GCN4, a eukaryotic transcriptional activator protein, binds as a dimer to target DNA. EMBO J. 6:2781–2784.
   PubMed Web of Science ®Google Scholar
• Jakobsen, B. K., and H. R. B. Pelham. 1988. Constitutive binding of yeast heat shock factor to DNA in vivo. Mol. Cell. Biol. 8:5040–5042.
   PubMed Web of Science ®Google Scholar
• Jakobsen, B. K., and H. R. B. Pelham. 1991. A conserved heptapeptide restrains the activity of the yeast heat shock transcription factor. EMBO J. 10:369–375.
   PubMedGoogle Scholar
• Jurivich, D. A., L. Sistonen, R. A. Kroes, and R. I. Morimoto. 1992. Effect of sodium salicylate on the human heat shock response. Science 255:1243–1245.
   PubMed Web of Science ®Google Scholar
• Jurivich, D. A., L. Sistonen, K. D. Sarge, and R. I. Morimoto. 1994. Arachi-donate is a potent modulator of human heat shock gene transcription. Proc. Natl. Acad. Sci. USA 91:2280–2284.
   PubMed Web of Science ®Google Scholar
• Kingston, R. E., R. I. Cowie, R. I. Morimoto, and K. A. Gwinn. 1986. Binding of polyomavirus large T antigen to the human hsp70 promoter is not required for transactivation. Mol. Cell. Biol. 6:3180–3190.
   PubMedGoogle Scholar
• Kingston, R. E., T. J. Schuetz, and Z. Larin. 1987. Heat-inducible human factor that binds to a human hsp70 promoter. Mol. Cell. Biol. 7:1530–1534.
   PubMed Web of Science ®Google Scholar
• Larson, J. S., T. J. Schuetz, and R. E. Kingston. 1988. Activation in vitro of sequence-specific DNA binding by a human regulatory factor. Nature (London) 335:372–375.
   PubMed Web of Science ®Google Scholar
• Larson, J. S., T. J. Schuetz, and R. E. Kingston. 1995. In vitro activation of purified human heat shock factor by heat. Biochemistry 34:1902–1911.
   PubMed Web of Science ®Google Scholar
• Lee, K. A. W., A. Bindereif, and M. R. Green. 1988. A small-scale procedure for preparation of nuclear extracts that support efficient transcription and pre-mRNA splicing. Gene Anal. Tech. 5:22–31.
   PubMedGoogle Scholar
• Lindquist, S. 1986. The heat-shock response. Annu. Rev. Biochem. 55:1151–1191.
   PubMed Web of Science ®Google Scholar
• Newton, E. M. Unpublished data.
   Google Scholar
• Picard, D., S. J. Salser, and K. R. Yamamoto. 1988. Amovable and regulable inactivation function within the steroid binding domain of the glucocorticoid receptor. Cell 54:1073–1080.
   PubMed Web of Science ®Google Scholar
• Price, B. D., and S. K. Calderwood. 1991. Ca2+ is essential for multistep activation of the heat shock factor in permeabilized cells. Mol. Cell. Biol. 11:3365–3368.
   PubMed Web of Science ®Google Scholar
• Regier, J. L., F. Shen, and S. J. Triezenberg. 1993. Pattern of aromatic and hydrophobic amino acids critical for one of the two subdomains of the VP16 transcriptional activator. Proc. Natl. Acad. Sci. USA 90:883–887.
   PubMed Web of Science ®Google Scholar
• Sarge, K. D., S. P. Murphy, and R. I. Morimoto. 1993. Activation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNA-binding activity, and nuclear localization and can occur in the absence of stress. Mol. Cell. Biol. 13:1392–1407.
   PubMed Web of Science ®Google Scholar
• Sheldon, L. A., and R. E. Kingston. 1993. Hydrophobic coiled-coil domains regulate the subcellular localization of human heat shock factor 2. Genes Dev. 7:1549–1558.
   PubMedGoogle Scholar
• Shi, Y., P. E. Kroeger, and R. I. Morimoto. 1995. The carboxyl-terminal transactivation domain of heat shock factor 1 is negatively regulated and stress responsive. Mol. Cell. Biol. 15:4309–4318.
   PubMed Web of Science ®Google Scholar
• Sorger, P. K. 1990. Yeast heat shock factor contains separable transient and sustained response transcriptional activators. Cell 62:793–805.
   PubMed Web of Science ®Google Scholar
• Sorger, P. K., M. J. Lewis, and H. R. B. Pelham. 1987. Heat shock factor is regulated differently in yeast and HeLa cells. Nature (London) 329:81–84.
   PubMed Web of Science ®Google Scholar
• Sorger, P. K., and H. R. B. Pelham. 1988. Yeast heat shock factor is an essential DNA-binding protein that exhibits temperature-dependent phosphorylation. Cell 54:855–864.
   PubMed Web of Science ®Google Scholar
• Taylor, I. C. A. 1991. Ph.D. thesis. Harvard University, Cambridge, Mass.
   Google Scholar
• Wu, C. 1984. Activating protein factor binds in vitro to upstream control sequences in heat shock gene chromatin. Nature (London) 311:81–84.
   PubMed Web of Science ®Google Scholar
• Zimarino, V., C. Tsai, and C. Wu. 1990. Complex modes ofheat shock factor activation. Mol. Cell. Biol. 10:752–759.
   PubMed Web of Science ®Google Scholar
• Zimarino, V., and C. Wu. 1987. Induction of sequence-specific binding of Drosophila heat shock activator protein without protein synthesis. Nature (London) 327:727–730.
   PubMed Web of Science ®Google Scholar
• Zuo, J., D. Rungger, and R. Voellmy. 1995. Multiple layers of regulation of human heat shock transcription factor 1. Mol. Cell. Biol. 15:4319–4330.
   PubMed Web of Science ®Google Scholar