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Updated: Oct 9, 2026

Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70
Published on: March 8, 2024
Polymorphism in the regulatory sequence of the human hsp70-1 gene does not affect heat shock factor binding or heat
F Favatier1, M R Jacquier-Sarlin, E Swierczewski
1Laboratoire de Biologie, Physiologie et Pathologie de la Respiration, UFR Cochin Port-Royal, Saint-Jacques, Université René Descartes, Paris, France. Florence.Favatier@cochin.univ-paris5.fr
Abstract:
A bi-allelic polymorphism found in the regulatory region of the human heat shock (HS) protein (HSP) hsp70-1 gene, which comprises an A-->C transversion, 3 bp upstream of the HS element (HSE), has been associated with extended HLA haplotypes. In view of the chaperoning and protective functions of Hsp70, we investigated whether this hsp70-1 bi-allelic polymorphism could modulate the stress response, which may relate to enhanced resistance or susceptibility to certain diseases. We compared the basal and HS-induced HS factor (HSF)-binding activity of the two polymorphic HSEs, hsp70-1 mRNA accumulation and HSP expression in two human Epstein Barr virus (EBV)-transformed B cell lines typed for hsp70-1 promoter alleles. Our results suggest that hsp70-1 promoter polymorphism does not influence HSF-binding activity, hsp70 mRNA accumulation or synthesis in human EBV-transformed B cell lines.
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