Monitoring of the Heat Shock Response with a Real-Time Luciferase Reporter.
Drug screen
Heat shock factor 1 (HSF1)
Heat shock protein 90 (HSP90)
Heat shock response
Luciferase assay
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2023
2023
Historique:
medline:
7
8
2023
pubmed:
4
8
2023
entrez:
4
8
2023
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 37540422
doi: 10.1007/978-1-0716-3342-7_1
doi:
Substances chimiques
Heat Shock Transcription Factors
0
Transcription Factors
0
Heat-Shock Proteins
0
Luciferases
EC 1.13.12.-
HSP70 Heat-Shock Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1-11Informations de copyright
© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
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