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Vol. 11, Issue 5, 1753-1764, May 2000

The Yeast Heat Shock Transcription Factor Changes Conformation in Response to Superoxide and Temperature

Sengyong Lee,^* Tage Carlson,^* Noah Christian, Kristi Lea, Jennifer Kedzie, James P. Reilly, and J. José Bonner

Departments of Biology and Chemistry, Indiana University, Bloomington, Indiana 47405-3700

In vitro DNA-binding assays demonstrate that the heat shock transcription factor (HSF) from the yeast Saccharomyces cerevisiae can adopt an altered conformation when stressed. This conformation, reflected in a change in electrophoretic mobility, requires that two HSF trimers be bound to DNA. Single trimers do not show this change, which appears to represent an alteration in the cooperative interactions between trimers. HSF isolated from stressed cells displays a higher propensity to adopt this altered conformation. Purified HSF can be stimulated in vitro to undergo the conformational change by elevating the temperature or by exposing HSF to superoxide anion. Mutational analysis maps a region critical for this conformational change to the flexible loop between the minimal DNA-binding domain and the flexible linker that joins the DNA-binding domain to the trimerization domain. The significance of these findings is discussed in the context of the induction of the heat shock response by ischemic stroke, hypoxia, and recovery from anoxia, all known to stimulate the production of superoxide.

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^* These authors contributed equally to this work.

Corresponding author. E-mail address: jbonner{at}bio.indiana.edu.

Present address: Parke Davis, Inc., Ann Arbor, MI 48105.

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Molecular Biology of the Cell
Vol. 11, 1753-1764, May 2000
Copyright © 2000 by The American Society for Cell Biology

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