Chapter title |
Monitoring of the Heat Shock Response with a Real-Time Luciferase Reporter
|
---|---|
Chapter number | 3 |
Book title |
Chaperones
|
Published in |
Methods in molecular biology, January 2018
|
DOI | 10.1007/978-1-4939-7477-1_3 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7476-4, 978-1-4939-7477-1
|
Authors |
Toshiki Kijima, Takanori Eguchi, Len Neckers, Thomas L. Prince |
Abstract |
The heat shock response (HSR) is a cellular mechanism for counteracting acute proteotoxic stress. In eukaryotes, transcriptional activation of the HSR is regulated by heat shock factor 1 (HSF1). Activation of HSF1 induces the expression of heat shock proteins (HSPs) that function as molecular chaperones to fold and maintain the three-dimensional structure of misfolded proteins. The regulation of the degree and duration of the HSR is controlled by multiple biochemical mechanisms that include posttranslational modification of HSF1 and numerous protein-protein interactions. In this chapter, we describe a method to evaluate the activation and deactivation of the HSR at the transcriptional level using a short half-life luciferase reporter assay. This assay can be used to further characterize the HSR or as a screen for small-molecule inducers, amplifiers, or repressors. |
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Medicine and Dentistry | 1 | 7% |
Other | 0 | 0% |
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