Part:BBa_K1458003

Heat shock proteins (HSP) are a key part of the heat shock response in almost all organisms, from bacteria to humans. Their expression is induced drastically when cells expose to stress such as elevated temperature, heavy metals or starvation. The 70 kDa heat shock proteins (Hsp70s) are a family of conserved ubiquitously expressed heat shock proteins. Like many other HSPs, HSP70 is an important part of the cell's machinery of protein folding. Its role is to prevent the aggregation of partially synthesized peptides or damaged proteins. The HSP70 promoter can be regulated by at list two distinct domains, a distal domain which contains sequences responsive to heat shock and cadmium stress, and proximal domain necessary for transcription stimulated by serum. The activity of the promoter can be induced by moderate hyperthermia (39°C to 43°C), metal induction or by addition of serum after starvation (Wu, Kingston, & Morimoto, 1986). Using this promoter allows thermal induced expression in human cell lines.

Wu, B., Kingston, R., & Morimoto, R. (1986). Human HSP70 promoter contains at least two distinct regulatory domains. Proceedings of the National Academy of Sciences of the United States of America, 83(February), 629–633. Retrieved from http://www.pnas.org/content/83/3/629.short