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Originally published In Press as doi:10.1074/jbc.M106301200 on August 16, 2001

J. Biol. Chem., Vol. 276, Issue 43, 40254-40262, October 26, 2001
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The DNA-binding Domain of Yeast Heat Shock Transcription Factor Independently Regulates Both the N- and C-terminal Activation Domains*

Amanda L. BulmanDagger §, Susan T. Hubl§, and Hillary C. M. NelsonDagger ||

From the Dagger  Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104 and the  Department of Molecular and Cell Biology, University of California, Berkeley, California 94720

The expression of heat shock proteins in response to cellular stresses is dependent on the activity of the heat shock transcription factor (HSF). In yeast, HSF is constitutively bound to DNA; however, the mitigation of negative regulation in response to stress dramatically increases transcriptional activity. Through alanine-scanning mutagenesis of the surface residues of the DNA-binding domain, we have identified a large number of mutants with increased transcriptional activity. Six of the strongest mutations were selected for detailed study. Our studies suggest that the DNA-binding domain is involved in the negative regulation of both the N-terminal and C-terminal activation domains of HSF. These mutations do not significantly affect DNA binding. Circular dichroism analysis suggests that a subset of the mutants may have altered secondary structure, whereas a different subset has decreased thermal stability. Our findings suggest that the regulation of HSF transcriptional activity (under both constitutive and stressed conditions) may be partially dependent on the local topology of the DNA-binding domain. In addition, the DNA-binding domain may mediate key interactions with ancillary factors and/or other intramolecular regulatory regions in order to modulate the complex regulation of HSF's transcriptional activity.

* This work was supported by National Institutes of Health Grant GM44086.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ These authors contributed equally to this work and should be considered joint first authors.

|| To whom correspondence should be addressed: Dept. of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, 813 Stellar-Chance, 422 Curie Blvd., Philadelphia, PA 19104-6089. Tel.: 215-573-7473; Fax: 215-573-2503; E-mail: hnelson@mail.med.upenn.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.