In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation

Dick D. Mosser*, Paul T. Kotzbauer, Kevin D. Sarge, Richard I. Morimoto

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

231 Scopus citations

Abstract

The transcription of heat shock genes in response to physiological stress requires activation of heat shock transcription factor (HSF). Although the transcriptional response is most commonly induced by temperature elevation, the biochemical events involved in HSF activation in vivo can also be triggered at normal physiological temperatures by chemicals that inhibit metabolic processes. We have used a HeLa cell-free system in which HSF DNA-binding is activated by conditions that affect protein conformation, including increasing concentrations of hydrogen ions, urea, or nonionic detergents. Treatment with calcium ions also results in a concentration- and time-dependent activation of HSF in vitro. Pretreatment with each of these biochemical conditions reduces the temperature dependence for HSF activation in vitro. These results suggest that HSF is activated either directly by undergoing a conformational change or indirectly through interactions with unfolded proteins.

Original languageEnglish (US)
Pages (from-to)3748-3752
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume87
Issue number10
DOIs
StatePublished - 1990

ASJC Scopus subject areas

  • General

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