The Yeast Heat Shock Transcription Factor Changes Conformation in Response to Superoxide and Temperature
View/ Open
Issue Date
2000-05Author
Lee, Sengyong
Carlson, Tage
Christian, Noah
Lea, Kristi
Raff, Jennifer
Publisher
American Society for Cell Biology
Type
Article
Article Version
Scholarly/refereed, publisher version
Rights
Copyright © 2000, The American Society for Cell Biology
Metadata
Show full item recordAbstract
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.
Collections
Citation
Lee, S., Carlson, T., Christian, N., Lea, K., Kedzie, J., Reilly, J. P., & Bonner, J. J. (2000). The Yeast Heat Shock Transcription Factor Changes Conformation in Response to Superoxide and Temperature. Molecular Biology of the Cell, 11(5), 1753–1764.
Items in KU ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
We want to hear from you! Please share your stories about how Open Access to this item benefits YOU.