Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 463, Issue 3, Pages 303-308Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2015.05.056
Keywords
Heat shock transcription factors (HSFs); Binding interaction; Fluorescence cross-correlation spectroscopy (FCCS); Heat shock recovery
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Funding
- Asan Institute for Life Sciences, Asan Medical Center, Seoul, Korea [2015-621]
- National Research Foundation of Korea (NRF) - Ministry of Science, ICT and Future Planning [NRF-R13-2008-010-00000-0]
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The cellular response to stress is primarily controlled in cells via transcriptional activation by heat shock factor 1 (HSF1). HSF1 is well-known to form homotrimers for activation upon heat shock and subsequently bind to target DNAs, such as heat-shock elements, by forming stress granules. A previous study demonstrated that nuclear HSF1 and HSF2 molecules in live cells interacted with target DNAs on the stress granules. However, the process underlying the binding interactions of HSF family in cells upon heat shock remains unclear. This study demonstrate for the first time that the interaction kinetics among nuclear HSF1, HSF2, and HSF4 upon heat shock can be detected directly in live cells using dual color fluorescence cross-correlation spectroscopy (FCCS). FCCS analyses indicated that the binding between HSFs was dramatically changed by heat shock. Interestingly, the recovery kinetics of interaction between HSF1 molecules after heat shock could be represented by changes in the relative interaction amplitude and mobility. (C) 2015 Elsevier Inc. All rights reserved.
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